---
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abstract:
- lang: eng
text: The plant hormone auxin regulates growth and development through at least
two distinct signaling pathways. The nuclear pathway, involving TIR1/AFB receptors,
mediates transcription; whereas the cell surface ABP1-TMK1 auxin perception triggers
global ultrafast phosphorylation response. Here, we revisit the rich history of
the disputed ABP1 auxin receptor, highlighting recent findings of the involvement
of TMKs and other molecular components and focusing on their role in auxin canalization-mediated
development.
acknowledgement: We gratefully acknowledge the funding by the Austrian Science Fund
(FWF; I 6123-B and P 37051-B) and the European Research Council (ERC; 101142681
CYNIPS).We would like to thank Lukas Fiedler for his significant input and thoughtful
revision of this manuscript.
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Aline
full_name: Monzer, Aline
id: 2DB5D88C-D7B3-11E9-B8FD-7907E6697425
last_name: Monzer
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
citation:
ama: Monzer A, Friml J. Historical and mechanistic perspective on ABP1-TMK1-mediated
cell surface auxin signaling. npj Science of Plants. 2025;1(1):2. doi:10.1038/s44383-025-00002-8
apa: Monzer, A., & Friml, J. (2025). Historical and mechanistic perspective
on ABP1-TMK1-mediated cell surface auxin signaling. Npj Science of Plants.
Springer Nature. https://doi.org/10.1038/s44383-025-00002-8
chicago: Monzer, Aline, and Jiří Friml. “Historical and Mechanistic Perspective
on ABP1-TMK1-Mediated Cell Surface Auxin Signaling.” Npj Science of Plants.
Springer Nature, 2025. https://doi.org/10.1038/s44383-025-00002-8.
ieee: A. Monzer and J. Friml, “Historical and mechanistic perspective on ABP1-TMK1-mediated
cell surface auxin signaling.,” npj Science of Plants, vol. 1, no. 1. Springer
Nature, p. 2, 2025.
ista: Monzer A, Friml J. 2025. Historical and mechanistic perspective on ABP1-TMK1-mediated
cell surface auxin signaling. npj Science of Plants. 1(1), 2.
mla: Monzer, Aline, and Jiří Friml. “Historical and Mechanistic Perspective on ABP1-TMK1-Mediated
Cell Surface Auxin Signaling.” Npj Science of Plants, vol. 1, no. 1, Springer
Nature, 2025, p. 2, doi:10.1038/s44383-025-00002-8.
short: A. Monzer, J. Friml, Npj Science of Plants 1 (2025) 2.
corr_author: '1'
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name: Guanylate cyclase activity of TIR1/AFBs auxin receptors
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publication: npj Science of Plants
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title: Historical and mechanistic perspective on ABP1-TMK1-mediated cell surface auxin
signaling.
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abstract:
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text: Phytohormone auxin and its directional transport mediate much of the remarkably
plastic development of higher plants. Positive feedback between auxin signaling
and transport is a prerequisite for (1) self-organizing processes, including vascular
tissue formation, and (2) directional growth responses such as gravitropism. Here,
we identify a mechanism by which auxin signaling directly targets PIN auxin transporters.
Via the cell-surface AUXIN-BINDING PROTEIN1 (ABP1)-TRANSMEMBRANE KINASE 1 (TMK1)
receptor module, auxin rapidly induces phosphorylation and thus stabilization
of PIN2. Following gravistimulation, initial auxin asymmetry activates autophosphorylation
of the TMK1 kinase. This induces TMK1 interaction with and phosphorylation of
PIN2, stabilizing PIN2 at the lower root side, thus reinforcing asymmetric auxin
flow for root bending. Upstream of TMK1 in this regulation, ABP1 acts redundantly
with the root-expressed ABP1-LIKE 3 (ABL3) auxin receptor. Such positive feedback
between cell-surface auxin signaling and PIN-mediated polar auxin transport is
fundamental for robust root gravitropism and presumably for other self-organizing
developmental phenomena.
acknowledged_ssus:
- _id: Bio
- _id: LifeSc
acknowledgement: We gratefully acknowledge Tongda Xu for experimental, material, and
conceptual support. We thank William Gray for providing material, Nataliia Gnyliukh
and Ema Cervenova for help with manuscript preparation, and Julia Schmid for help
with cloning. We thank Dolf Weijers, Mark Roosjen, and Andre Kuhn for discussions
and support with phospho-proteomic analyses. We thank the Bioimaging and Life Science
facilities at the Institute of Science and Technology Austria (ISTA) for their excellent
service and assistance. The research leading to these results has received funding
from the European Union (ERC, CYNIPS, 101142681) and Austrian Science Fund (FWF;
I 6123-B) to J.F., and Y.J. was funded by ERC no. 3363360-APPL under FP/2007-2013.
L.R. was supported by the FP7-PEOPLE-2011-COFUND ISTFELLOW program (IC1023FELL01)
and the European Molecular Biology Organization (EMBO) long-term postdoctoral fellowship
(ALTF 985-2016). S.T. was supported by the National Natural Science Foundation of
China (32321001, 32570366). The work of J.H. was supported by the project JG_2024_003
implemented within the Palacký University Young Researcher Grant.
article_processing_charge: Yes (via OA deal)
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author:
- first_name: Lesia
full_name: Rodriguez Solovey, Lesia
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last_name: Zou
- first_name: Caterina
full_name: Giannini, Caterina
id: e3fdddd5-f6e0-11ea-865d-ca99ee6367f4
last_name: Giannini
- first_name: Aline
full_name: Monzer, Aline
id: 2DB5D88C-D7B3-11E9-B8FD-7907E6697425
last_name: Monzer
- first_name: Dmitrii
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last_name: Vladimirtsev
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last_name: Gelová
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id: 362BF7FE-F248-11E8-B48F-1D18A9856A87
last_name: Verstraeten
orcid: 0000-0001-7241-2328
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full_name: Hajny, Jakub
id: 4800CC20-F248-11E8-B48F-1D18A9856A87
last_name: Hajny
orcid: 0000-0003-2140-7195
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full_name: Chen, Meng
last_name: Chen
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full_name: Tan, Shutang
id: 2DE75584-F248-11E8-B48F-1D18A9856A87
last_name: Tan
orcid: 0000-0002-0471-8285
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full_name: Hörmayer, Lukas
id: 2EEE7A2A-F248-11E8-B48F-1D18A9856A87
last_name: Hörmayer
orcid: 0000-0001-8295-2926
- first_name: Lanxin
full_name: Li, Lanxin
id: 367EF8FA-F248-11E8-B48F-1D18A9856A87
last_name: Li
orcid: 0000-0002-5607-272X
- first_name: Maria Mar
full_name: Marques-Bueno, Maria Mar
last_name: Marques-Bueno
- first_name: Zainab
full_name: Quddoos, Zainab
id: 32ff3c64-04a0-11f0-a50f-d0c45bfac466
last_name: Quddoos
- first_name: Gergely
full_name: Molnar, Gergely
id: 34F1AF46-F248-11E8-B48F-1D18A9856A87
last_name: Molnar
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full_name: Kulich, Ivan
id: 57a1567c-8314-11eb-9063-c9ddc3451a54
last_name: Kulich
- first_name: Yvon
full_name: Jaillais, Yvon
last_name: Jaillais
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
citation:
ama: Rodriguez Solovey L, Fiedler L, Zou M, et al. ABP1/ABL3-TMK1 cell-surface auxin
signaling targets PIN2-mediated auxin fluxes for root gravitropism. Cell.
2025;188(22):6138-6150.e17. doi:10.1016/j.cell.2025.08.026
apa: Rodriguez Solovey, L., Fiedler, L., Zou, M., Giannini, C., Monzer, A., Vladimirtsev,
D., … Friml, J. (2025). ABP1/ABL3-TMK1 cell-surface auxin signaling targets PIN2-mediated
auxin fluxes for root gravitropism. Cell. Elsevier. https://doi.org/10.1016/j.cell.2025.08.026
chicago: Rodriguez Solovey, Lesia, Lukas Fiedler, Minxia Zou, Caterina Giannini,
Aline Monzer, Dmitrii Vladimirtsev, Marek Randuch, et al. “ABP1/ABL3-TMK1 Cell-Surface
Auxin Signaling Targets PIN2-Mediated Auxin Fluxes for Root Gravitropism.” Cell.
Elsevier, 2025. https://doi.org/10.1016/j.cell.2025.08.026.
ieee: L. Rodriguez Solovey et al., “ABP1/ABL3-TMK1 cell-surface auxin signaling
targets PIN2-mediated auxin fluxes for root gravitropism,” Cell, vol. 188,
no. 22. Elsevier, p. 6138–6150.e17, 2025.
ista: Rodriguez Solovey L, Fiedler L, Zou M, Giannini C, Monzer A, Vladimirtsev
D, Randuch M, Yu Y, Gelová Z, Verstraeten I, Hajny J, Chen M, Tan S, Hörmayer
L, Li L, Marques-Bueno MM, Quddoos Z, Molnar G, Kulich I, Jaillais Y, Friml J.
2025. ABP1/ABL3-TMK1 cell-surface auxin signaling targets PIN2-mediated auxin
fluxes for root gravitropism. Cell. 188(22), 6138–6150.e17.
mla: Rodriguez Solovey, Lesia, et al. “ABP1/ABL3-TMK1 Cell-Surface Auxin Signaling
Targets PIN2-Mediated Auxin Fluxes for Root Gravitropism.” Cell, vol. 188,
no. 22, Elsevier, 2025, p. 6138–6150.e17, doi:10.1016/j.cell.2025.08.026.
short: L. Rodriguez Solovey, L. Fiedler, M. Zou, C. Giannini, A. Monzer, D. Vladimirtsev,
M. Randuch, Y. Yu, Z. Gelová, I. Verstraeten, J. Hajny, M. Chen, S. Tan, L. Hörmayer,
L. Li, M.M. Marques-Bueno, Z. Quddoos, G. Molnar, I. Kulich, Y. Jaillais, J. Friml,
Cell 188 (2025) 6138–6150.e17.
corr_author: '1'
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title: ABP1/ABL3-TMK1 cell-surface auxin signaling targets PIN2-mediated auxin fluxes
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text: "Plant growth and development rely significantly on phytohormones, with auxin
serving as a master regulator, orchestrating processes from embryogenesis to organogenesis,
vascular patterning, and environmental adaptation. Since its conceptual proposition
by Charles Darwin in 1880 as an endogenous chemical signal influencing phototropism
in grass, auxin has captivated scientists seeking to understand how such a small
molecule exerts a profound influence on plant development.\r\nOne particularly
fascinating aspect of auxin function is its ability to self-organize its transport.
Through a feedback mechanism between auxin perception and directional transport—primarily
mediated by PIN auxin transporters—auxin establishes narrow transport channels.
This phenomenon, known as auxin canalization, is fundamental to vascular formation,
regeneration, and other key developmental processes. Despite advances in our understanding,
driven by experimental studies and computational models, auxin canalization remains
an enigma, with many unanswered questions.\r\nLike other hormones, auxin functions
through intricate signaling pathways. It operates through at least two distinct
signaling mechanisms: the well-characterized canonical pathway and the less understood
non-canonical pathway. While significant progress has been made in elucidating
the canonical pathway, the non-canonical mechanisms remain less defined and require
further investigation.\r\nIn this study, we revisit the non-canonical auxin signaling
pathway mediated by the cell-surface complex Auxin Binding Protein 1-Transmembrane
Kinase 1 (ABP1-TMK1), with a particular focus on its downstream phosphorylation
events. We reveal that this auxin-mediated phosphorylation is conserved across
the green lineage, underscoring its fundamental role in plant development. We
explore key phosphorylation targets, particularly PIN2, which is essential for
root gravitropism. To further understand TMK1’s role in diverse developmental
processes, we identified and investigated its interactors as potential co-receptors
or regulatory components within its signaling network.\r\nGiven the previously
established role of ABP1-TMK1 in auxin canalization, we sought to further investigate
this process and identified several TMK1 interactors also involved in this intricate
mechanism.\r\nThese findings provide new insights into the complex regulation
of auxin canalization, highlighting a broader and more interconnected signaling
framework than previously understood."
acknowledged_ssus:
- _id: LifeSc
- _id: Bio
acknowledgement: I would like to acknowledge the facilities at ISTA, particularly
LSF, IOF, and, of course, the plant facility, for providing the necessary resources
for my research.
alternative_title:
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full_name: Monzer, Aline
id: 2DB5D88C-D7B3-11E9-B8FD-7907E6697425
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citation:
ama: 'Monzer A. Cell-surface auxin signaling: Linking molecular pathways to plant
development. 2025. doi:10.15479/AT-ISTA-19395'
apa: 'Monzer, A. (2025). Cell-surface auxin signaling: Linking molecular pathways
to plant development. Institute of Science and Technology Austria. https://doi.org/10.15479/AT-ISTA-19395'
chicago: 'Monzer, Aline. “Cell-Surface Auxin Signaling: Linking Molecular Pathways
to Plant Development.” Institute of Science and Technology Austria, 2025. https://doi.org/10.15479/AT-ISTA-19395.'
ieee: 'A. Monzer, “Cell-surface auxin signaling: Linking molecular pathways to plant
development,” Institute of Science and Technology Austria, 2025.'
ista: 'Monzer A. 2025. Cell-surface auxin signaling: Linking molecular pathways
to plant development. Institute of Science and Technology Austria.'
mla: 'Monzer, Aline. Cell-Surface Auxin Signaling: Linking Molecular Pathways
to Plant Development. Institute of Science and Technology Austria, 2025, doi:10.15479/AT-ISTA-19395.'
short: 'A. Monzer, Cell-Surface Auxin Signaling: Linking Molecular Pathways to Plant
Development, Institute of Science and Technology Austria, 2025.'
corr_author: '1'
date_created: 2025-03-12T14:25:42Z
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id: 4159519E-F248-11E8-B48F-1D18A9856A87
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orcid: 0000-0002-8302-7596
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abstract:
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text: Phytohormone auxin and its directional transport mediate much of the remarkably
plastic development of higher plants. Positive feedback between auxin signaling
and transport is a key prerequisite for (i) self-organizing processes including
vascular tissue formation and (ii) directional growth responses such as gravitropism.
Here we identify a mechanism, by which auxin signaling directly targets PIN auxin
transporters. Via the cell-surface ABP1-TMK1 receptor module, auxin rapidly induces
phosphorylation and thus stabilization of PIN2. Following gravistimulation, initial
auxin asymmetry activates autophosphorylation of the TMK1 kinase. This induces
TMK1 interaction with and phosphorylation of PIN2, stabilizing PIN2 at the lower
root side, thus reinforcing asymmetric auxin flow for root bending. Upstream of
TMK1 in this regulation, ABP1 acts redundantly with the root-expressed ABP1-LIKE
auxin receptor ABL3. Such positive feedback between cell-surface auxin signaling
and PIN-mediated polar auxin transport is fundamental for robust root gravitropism
and presumably also for other self-organizing developmental phenomena.
acknowledged_ssus:
- _id: Bio
- _id: LifeSc
acknowledgement: 'We thank W. Gray for providing material; N. Gnyliukh and E. Cervenova
for help with manuscript preparation; J. Schmid for help with cloning. We thank
Dolf Weijers, Mark Roosjen, and Andre Kuhn for discussions and support with phospho-proteomic
analyses. We thank the Bioimaging and Life Science facilities at ISTA for their
excellent service and assistance. The research leading to these results has received
funding from the European Research Council (ERC) under the European Union’s Horizon
2020 research and innovation program grant agreement No 742985 and Austrian Science
Fund (FWF): I3630-775 B25 to J.F; National Natural Science Foundation of China (Grant
32130010, 31422008), start-up funds from FAFU to T.X., Y.J. was funded by ERC no.
3363360-APPL under FP/2007-2013. L.R. was supported by FP7-PEOPLE-2011-COFUND ISTFELLOW
program (IC1023FELL01) and the European Molecular Biology Organization (EMBO) long-term
postdoctoral fellowship (ALTF 985- 2016). S.T. was supported by the National Natural
Science Foundation of China (32321001).'
article_processing_charge: No
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- first_name: Lesia
full_name: Rodriguez Solovey, Lesia
id: 3922B506-F248-11E8-B48F-1D18A9856A87
last_name: Rodriguez Solovey
orcid: 0000-0002-7244-7237
- first_name: Lukas
full_name: Fiedler, Lukas
id: 7c417475-8972-11ed-ae7b-8b674ca26986
last_name: Fiedler
- first_name: Minxia
full_name: Zou, Minxia
id: 5c243f41-03f3-11ec-841c-96faf48a7ef9
last_name: Zou
- first_name: Caterina
full_name: Giannini, Caterina
id: e3fdddd5-f6e0-11ea-865d-ca99ee6367f4
last_name: Giannini
- first_name: Aline
full_name: Monzer, Aline
id: 2DB5D88C-D7B3-11E9-B8FD-7907E6697425
last_name: Monzer
- first_name: Dmitrii
full_name: Vladimirtsev, Dmitrii
id: 60466724-5355-11ee-ae5a-fa55e8f99c3d
last_name: Vladimirtsev
- first_name: Marek
full_name: Randuch, Marek
id: 6ac4636d-15b2-11ec-abd3-fb8df79972ae
last_name: Randuch
- first_name: Yongfan
full_name: Yu, Yongfan
last_name: Yu
- first_name: Zuzana
full_name: Gelová, Zuzana
id: 0AE74790-0E0B-11E9-ABC7-1ACFE5697425
last_name: Gelová
orcid: 0000-0003-4783-1752
- first_name: Inge
full_name: Verstraeten, Inge
id: 362BF7FE-F248-11E8-B48F-1D18A9856A87
last_name: Verstraeten
orcid: 0000-0001-7241-2328
- first_name: Jakub
full_name: Hajny, Jakub
id: 4800CC20-F248-11E8-B48F-1D18A9856A87
last_name: Hajny
orcid: 0000-0003-2140-7195
- first_name: Meng
full_name: Chen, Meng
last_name: Chen
- first_name: Shutang
full_name: Tan, Shutang
id: 2DE75584-F248-11E8-B48F-1D18A9856A87
last_name: Tan
orcid: 0000-0002-0471-8285
- first_name: Lukas
full_name: Hörmayer, Lukas
id: 2EEE7A2A-F248-11E8-B48F-1D18A9856A87
last_name: Hörmayer
orcid: 0000-0001-8295-2926
- first_name: Lanxin
full_name: Li, Lanxin
id: 367EF8FA-F248-11E8-B48F-1D18A9856A87
last_name: Li
orcid: 0000-0002-5607-272X
- first_name: Maria Mar
full_name: Marques-Bueno, Maria Mar
last_name: Marques-Bueno
- first_name: Zainab
full_name: Quddoos, Zainab
id: 32ff3c64-04a0-11f0-a50f-d0c45bfac466
last_name: Quddoos
- first_name: Gergely
full_name: Molnar, Gergely
id: 34F1AF46-F248-11E8-B48F-1D18A9856A87
last_name: Molnar
- first_name: Tongda
full_name: Xu, Tongda
last_name: Xu
- first_name: Ivan
full_name: Kulich, Ivan
id: 57a1567c-8314-11eb-9063-c9ddc3451a54
last_name: Kulich
- first_name: Yvon
full_name: Jaillais, Yvon
last_name: Jaillais
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
citation:
ama: Rodriguez Solovey L, Fiedler L, Zou M, et al. ABP1/ABL3-TMK1 cell-surface auxin
signaling directly targets PIN2-mediated auxin fluxes for root gravitropism. bioRxiv.
doi:10.1101/2022.11.30.518503
apa: Rodriguez Solovey, L., Fiedler, L., Zou, M., Giannini, C., Monzer, A., Vladimirtsev,
D., … Friml, J. (n.d.). ABP1/ABL3-TMK1 cell-surface auxin signaling directly targets
PIN2-mediated auxin fluxes for root gravitropism. bioRxiv. https://doi.org/10.1101/2022.11.30.518503
chicago: Rodriguez Solovey, Lesia, Lukas Fiedler, Minxia Zou, Caterina Giannini,
Aline Monzer, Dmitrii Vladimirtsev, Marek Randuch, et al. “ABP1/ABL3-TMK1 Cell-Surface
Auxin Signaling Directly Targets PIN2-Mediated Auxin Fluxes for Root Gravitropism.”
BioRxiv, n.d. https://doi.org/10.1101/2022.11.30.518503.
ieee: L. Rodriguez Solovey et al., “ABP1/ABL3-TMK1 cell-surface auxin signaling
directly targets PIN2-mediated auxin fluxes for root gravitropism,” bioRxiv.
.
ista: Rodriguez Solovey L, Fiedler L, Zou M, Giannini C, Monzer A, Vladimirtsev
D, Randuch M, Yu Y, Gelová Z, Verstraeten I, Hajny J, Chen M, Tan S, Hörmayer
L, Li L, Marques-Bueno MM, Quddoos Z, Molnar G, Xu T, Kulich I, Jaillais Y, Friml
J. ABP1/ABL3-TMK1 cell-surface auxin signaling directly targets PIN2-mediated
auxin fluxes for root gravitropism. bioRxiv, 10.1101/2022.11.30.518503.
mla: Rodriguez Solovey, Lesia, et al. “ABP1/ABL3-TMK1 Cell-Surface Auxin Signaling
Directly Targets PIN2-Mediated Auxin Fluxes for Root Gravitropism.” BioRxiv,
doi:10.1101/2022.11.30.518503.
short: L. Rodriguez Solovey, L. Fiedler, M. Zou, C. Giannini, A. Monzer, D. Vladimirtsev,
M. Randuch, Y. Yu, Z. Gelová, I. Verstraeten, J. Hajny, M. Chen, S. Tan, L. Hörmayer,
L. Li, M.M. Marques-Bueno, Z. Quddoos, G. Molnar, T. Xu, I. Kulich, Y. Jaillais,
J. Friml, BioRxiv (n.d.).
corr_author: '1'
das_tickbox: '1'
date_created: 2025-03-13T08:36:48Z
date_published: 2025-02-20T00:00:00Z
date_updated: 2026-08-14T09:33:45Z
day: '20'
ddc:
- '580'
department:
- _id: JiFr
- _id: XiFe
doi: 10.1101/2022.11.30.518503
ec_funded: 1
fulldoi: https://doi.org/10.1101/2022.11.30.518503
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1101/2022.11.30.518503
month: '02'
oa: 1
oa_version: Published Version
project:
- _id: 261099A6-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '742985'
name: Tracing Evolution of Auxin Transport and Polarity in Plants
- _id: 26538374-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: I03630
name: Molecular mechanisms of endocytic cargo recognition in plants
- _id: 25681D80-B435-11E9-9278-68D0E5697425
call_identifier: FP7
grant_number: '291734'
name: International IST Postdoc Fellowship Programme
- _id: 26060676-B435-11E9-9278-68D0E5697425
grant_number: ALTF 985-2016
name: Cell surface receptor complexes for auxin signaling in plants
publication: bioRxiv
publication_status: draft
related_material:
record:
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relation: later_version
status: public
- id: '20364'
relation: dissertation_contains
status: public
- id: '19395'
relation: dissertation_contains
status: public
status: public
title: ABP1/ABL3-TMK1 cell-surface auxin signaling directly targets PIN2-mediated
auxin fluxes for root gravitropism
type: preprint
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2025'
...
---
OA_place: repository
OA_type: green
_id: '19398'
abstract:
- lang: eng
text: Receptor-like kinases (RLKs), particularly the Transmembrane Kinase (TMK)
family, play essential roles in signaling and development, with TMKs being key
components of auxin perception and downstream phosphorylation events. While TMKs’
involvement in auxin canalization, a process essential for vasculature formation
and regeneration, has been established, nonetheless, the additional signaling
and regulatory partners remain poorly understood. In this study, we identify and
characterize seven leucine-rich repeat RLKs (TINT1–TINT7) as novel interactors
of TMK1, revealing their diverse evolutionary, structural, and functional characteristics.
Our results show that TINTs interact with TMK1 and highlight their roles in regulating
various developmental processes. Majority of TINTs contributes, together with
TMK1, to auxin canalization, with TINT5 linking TMK1 to other canalization component
CAMEL. Beyond canalization, we also establish the role of TINT-TMK1 interactions
in processes such as stomatal movement and the hypocotyl’s gravitropic response.
These findings suggest that TINTs, through their interaction with TMK1, are integral
components of various signaling networks, contributing to both auxin canalization
and broader plant development.
acknowledged_ssus:
- _id: Bio
- _id: LifeSc
acknowledgement: We deeply appreciate M. Wrzaczek’s constructive input and insightful
discussions, which significantly enriched this work. We thank L. Fiedler for helping
with the heat map and for the discussions. We also thank the facilities at ISTA,
the imaging and optics (IOF) and Lab Support (LSF) facilities for their service
and assistance.
article_processing_charge: No
author:
- first_name: Aline
full_name: Monzer, Aline
id: 2DB5D88C-D7B3-11E9-B8FD-7907E6697425
last_name: Monzer
- first_name: Ewa
full_name: Mazur, Ewa
last_name: Mazur
- first_name: Lesia
full_name: Rodriguez Solovey, Lesia
id: 3922B506-F248-11E8-B48F-1D18A9856A87
last_name: Rodriguez Solovey
orcid: 0000-0002-7244-7237
- first_name: Michelle C
full_name: Gallei, Michelle C
id: 35A03822-F248-11E8-B48F-1D18A9856A87
last_name: Gallei
orcid: 0000-0003-1286-7368
- first_name: Minxia
full_name: Zou, Minxia
id: 5c243f41-03f3-11ec-841c-96faf48a7ef9
last_name: Zou
- first_name: Michael
full_name: Smejkal, Michael
id: 79a5a1be-04a3-11f0-ba18-a1730e0b58e9
last_name: Smejkal
- first_name: Ema
full_name: Cervenova, Ema
id: 9f185b95-04a3-11f0-8245-f5e32eeb470f
last_name: Cervenova
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
citation:
ama: Monzer A, Mazur E, Rodriguez Solovey L, et al. TMK interacting network of receptor
like kinases for auxin canalization and beyond. bioRxiv. doi:10.1101/2025.02.28.640727
apa: Monzer, A., Mazur, E., Rodriguez Solovey, L., Gallei, M. C., Zou, M., Smejkal,
M., … Friml, J. (n.d.). TMK interacting network of receptor like kinases for auxin
canalization and beyond. bioRxiv. https://doi.org/10.1101/2025.02.28.640727
chicago: Monzer, Aline, Ewa Mazur, Lesia Rodriguez Solovey, Michelle C Gallei, Minxia
Zou, Michael Smejkal, Ema Cervenova, and Jiří Friml. “TMK Interacting Network
of Receptor like Kinases for Auxin Canalization and Beyond.” BioRxiv, n.d.
https://doi.org/10.1101/2025.02.28.640727.
ieee: A. Monzer et al., “TMK interacting network of receptor like kinases
for auxin canalization and beyond,” bioRxiv. .
ista: Monzer A, Mazur E, Rodriguez Solovey L, Gallei MC, Zou M, Smejkal M, Cervenova
E, Friml J. TMK interacting network of receptor like kinases for auxin canalization
and beyond. bioRxiv, 10.1101/2025.02.28.640727.
mla: Monzer, Aline, et al. “TMK Interacting Network of Receptor like Kinases for
Auxin Canalization and Beyond.” BioRxiv, doi:10.1101/2025.02.28.640727.
short: A. Monzer, E. Mazur, L. Rodriguez Solovey, M.C. Gallei, M. Zou, M. Smejkal,
E. Cervenova, J. Friml, BioRxiv (n.d.).
corr_author: '1'
das_tickbox: '1'
date_created: 2025-03-12T14:28:53Z
date_published: 2025-03-02T00:00:00Z
date_updated: 2026-08-14T09:33:45Z
day: '02'
ddc:
- '580'
department:
- _id: GradSch
- _id: JiFr
- _id: EvBe
doi: 10.1101/2025.02.28.640727
fulldoi: https://doi.org/10.1101/2025.02.28.640727
has_accepted_license: '1'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1101/2025.02.28.640727
month: '03'
oa: 1
oa_version: Published Version
publication: bioRxiv
publication_status: draft
related_material:
record:
- id: '19395'
relation: dissertation_contains
status: public
status: public
title: TMK interacting network of receptor like kinases for auxin canalization and
beyond
tmp:
image: /images/cc_by_nc_nd.png
legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode
name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
(CC BY-NC-ND 4.0)
short: CC BY-NC-ND (4.0)
type: preprint
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2025'
...
---
OA_place: publisher
OA_type: hybrid
_id: '15330'
abstract:
- lang: eng
text: Clathrin-mediated endocytosis (CME) is vital for the regulation of plant growth
and development by controlling plasma membrane protein composition and cargo uptake.
CME relies on the precise recruitment of regulators for vesicle maturation and
release. Homologues of components of mammalian vesicle scission are strong candidates
to be part of the scission machinery in plants, but the precise roles of these
proteins in this process are not fully understood. Here, we characterised the
roles of Plant Dynamin-Related Proteins 2 (DRP2s) and SH3-domain containing protein
2 (SH3P2), the plant homologue to Dynamins’ recruiters, like Endophilin and Amphiphysin,
in the CME by combining high-resolution imaging of endocytic events in vivo and
characterisation of the purified proteins in vitro. Although DRP2s and SH3P2 arrive
similarly late during CME and physically interact, genetic analysis of the sh3p123
triple-mutant and complementation assays with non-SH3P2-interacting DRP2 variants
suggests that SH3P2 does not directly recruit DRP2s to the site of endocytosis.
These observations imply that despite the presence of many well-conserved endocytic
components, plants have acquired a distinct mechanism for CME.
acknowledged_ssus:
- _id: EM-Fac
- _id: LifeSc
- _id: Bio
acknowledgement: "Nataliia Gnyliukh was partially funded by the European Union’s Horizon
2020 research and\r\ninnovation program (2018-2020) under the Marie Sklodowska-Curie
Grant (agreement no.\r\n665385). Taif University Researchers Supporting Project:
TURSP-HC2022/02. and Austrian\r\nScience Fund (FWF): I 6123-B.We thank Prof. Eileen
Lafer and Liping Wang for their suggestions regarding the optimisation of protein
expression and purification. We thank Prof. Sebastian Y. Bednarek for the useful
comments and constructive criticism of the project. We thank Maciek Adamowski for
providing genetic material. This research was supported by the Scientific Service
Units (SSU) of IST-Austria through resources provided by the Electron microscopy
(EMF), Lab Support Facility (LSF) (particularly Dorota Jaworska) and the Bioimaging
Facility (BIF)."
article_number: jcs.261720
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Nataliia
full_name: Gnyliukh, Nataliia
id: 390C1120-F248-11E8-B48F-1D18A9856A87
last_name: Gnyliukh
orcid: 0000-0002-2198-0509
- first_name: Alexander J
full_name: Johnson, Alexander J
id: 46A62C3A-F248-11E8-B48F-1D18A9856A87
last_name: Johnson
orcid: 0000-0002-2739-8843
- first_name: MK
full_name: Nagel, MK
last_name: Nagel
- first_name: Aline
full_name: Monzer, Aline
id: 2DB5D88C-D7B3-11E9-B8FD-7907E6697425
last_name: Monzer
- first_name: David
full_name: Babic, David
id: db566d23-f6e0-11ea-865d-e6f270e968e7
last_name: Babic
- first_name: Annamaria
full_name: Hlavata, Annamaria
id: 36062FEC-F248-11E8-B48F-1D18A9856A87
last_name: Hlavata
- first_name: SS
full_name: Alotaibi, SS
last_name: Alotaibi
- first_name: E
full_name: Isono, E
last_name: Isono
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
citation:
ama: Gnyliukh N, Johnson AJ, Nagel M, et al. Role of dynamin-related proteins 2
and SH3P2 in clathrin-mediated endocytosis in Arabidopsis thaliana. Journal
of Cell Science. 2024;137(8). doi:10.1242/jcs.261720
apa: Gnyliukh, N., Johnson, A. J., Nagel, M., Monzer, A., Babic, D., Hlavata, A.,
… Friml, J. (2024). Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated
endocytosis in Arabidopsis thaliana. Journal of Cell Science. The Company
of Biologists. https://doi.org/10.1242/jcs.261720
chicago: Gnyliukh, Nataliia, Alexander J Johnson, MK Nagel, Aline Monzer, David
Babic, Annamaria Hlavata, SS Alotaibi, E Isono, Martin Loose, and Jiří Friml.
“Role of Dynamin-Related Proteins 2 and SH3P2 in Clathrin-Mediated Endocytosis
in Arabidopsis Thaliana.” Journal of Cell Science. The Company of Biologists,
2024. https://doi.org/10.1242/jcs.261720.
ieee: N. Gnyliukh et al., “Role of dynamin-related proteins 2 and SH3P2 in
clathrin-mediated endocytosis in Arabidopsis thaliana,” Journal of Cell Science,
vol. 137, no. 8. The Company of Biologists, 2024.
ista: Gnyliukh N, Johnson AJ, Nagel M, Monzer A, Babic D, Hlavata A, Alotaibi S,
Isono E, Loose M, Friml J. 2024. Role of dynamin-related proteins 2 and SH3P2
in clathrin-mediated endocytosis in Arabidopsis thaliana. Journal of Cell Science.
137(8), jcs. 261720.
mla: Gnyliukh, Nataliia, et al. “Role of Dynamin-Related Proteins 2 and SH3P2 in
Clathrin-Mediated Endocytosis in Arabidopsis Thaliana.” Journal of Cell Science,
vol. 137, no. 8, jcs. 261720, The Company of Biologists, 2024, doi:10.1242/jcs.261720.
short: N. Gnyliukh, A.J. Johnson, M. Nagel, A. Monzer, D. Babic, A. Hlavata, S.
Alotaibi, E. Isono, M. Loose, J. Friml, Journal of Cell Science 137 (2024).
corr_author: '1'
date_created: 2024-04-19T09:54:59Z
date_published: 2024-04-01T00:00:00Z
date_updated: 2025-09-04T13:49:45Z
day: '01'
ddc:
- '570'
department:
- _id: MaLo
- _id: JiFr
- _id: CaBe
doi: 10.1242/jcs.261720
ec_funded: 1
external_id:
isi:
- '001266917100005'
pmid:
- '38506228'
file:
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checksum: 6dc023f0cc7052ad3cf0a42589d2e30f
content_type: application/pdf
creator: dernst
date_created: 2025-01-09T08:41:16Z
date_updated: 2025-01-09T08:41:16Z
file_id: '18792'
file_name: 2024_JourCellScience_Gnyliukh.pdf
file_size: 25845948
relation: main_file
success: 1
file_date_updated: 2025-01-09T08:41:16Z
fulldoi: https://doi.org/10.1242/jcs.261720
has_accepted_license: '1'
intvolume: ' 137'
isi: 1
issue: '8'
language:
- iso: eng
month: '04'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: 2564DBCA-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '665385'
name: International IST Doctoral Program
- _id: bd76d395-d553-11ed-ba76-f678c14f9033
grant_number: I06123
name: Peptide receptors for auxin canalization in Arabidopsis
publication: Journal of Cell Science
publication_identifier:
eissn:
- 1477-9137
issn:
- 0021-9533
publication_status: published
publisher: The Company of Biologists
quality_controlled: '1'
related_material:
record:
- id: '14591'
relation: earlier_version
status: public
scopus_import: '1'
status: public
title: Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated endocytosis
in Arabidopsis thaliana
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 137
year: '2024'
...
---
OA_place: publisher
OA_type: hybrid
_id: '18596'
abstract:
- lang: eng
text: Hormone perception and signaling pathways have a fundamental regulatory function
in the physiological processes of plants. Cytokinins, a class of plant hormones,
regulate cell division and meristem maintenance. The cytokinin signaling pathway
is well established in the model plant Arabidopsis thaliana. Several negative
feedback mechanisms, tightly controlling cytokinin signaling output, have been
described previously. In this study, we identified a new feedback mechanism executed
through alternative splicing of the cytokinin receptor AHK4/CRE1. A novel splicing
variant named CRE1int7 results from seventh intron retention, introducing a premature
termination codon in the transcript. We showed that CRE1int7 is translated in
planta into a truncated receptor lacking the C-terminal receiver domain essential
for signal transduction. CRE1int7 can bind cytokinin but cannot activate the downstream
cascade. We present a novel negative feedback mechanism of the cytokinin signaling
pathway, facilitated by a decoy receptor that can inactivate canonical cytokinin
receptors via dimerization and compete with them for ligand binding. Ensuring
proper plant growth and development requires precise control of the cytokinin
signaling pathway at several levels. CRE1int7 represents a so-far unknown mechanism
for fine-tuning the cytokinin signaling pathway in Arabidopsis.
acknowledged_ssus:
- _id: Bio
- _id: LifeSc
acknowledgement: We dedicate this paper to the deceased Petr Galuszka for his inspiration
and support of our project. We thank Prof. Peter Hedden for constructive criticism
of the manuscript and English editing. No conflict of interest is declared.
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Michaela
full_name: Králová, Michaela
last_name: Králová
- first_name: Ivona
full_name: Kubalová, Ivona
last_name: Kubalová
- first_name: Jakub
full_name: Hajný, Jakub
last_name: Hajný
- first_name: Karolina
full_name: Kubiasova, Karolina
id: 946011F4-3E71-11EA-860B-C7A73DDC885E
last_name: Kubiasova
orcid: 0000-0001-5630-9419
- first_name: Karolína
full_name: Vagaská, Karolína
last_name: Vagaská
- first_name: Zengxiang
full_name: Ge, Zengxiang
id: f43371a3-09ff-11eb-8013-bd0c6a2f6de8
last_name: Ge
orcid: 0000-0001-9381-3577
- first_name: Michelle C
full_name: Gallei, Michelle C
id: 35A03822-F248-11E8-B48F-1D18A9856A87
last_name: Gallei
orcid: 0000-0003-1286-7368
- first_name: Hana
full_name: Semerádová, Hana
id: 42FE702E-F248-11E8-B48F-1D18A9856A87
last_name: Semerádová
- first_name: Anna
full_name: Kuchařová, Anna
last_name: Kuchařová
- first_name: Martin
full_name: Hönig, Martin
last_name: Hönig
- first_name: Aline
full_name: Monzer, Aline
id: 2DB5D88C-D7B3-11E9-B8FD-7907E6697425
last_name: Monzer
- first_name: Martin
full_name: Kovačik, Martin
last_name: Kovačik
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
- first_name: Ondřej
full_name: Novák, Ondřej
last_name: Novák
- first_name: Eva
full_name: Benková, Eva
id: 38F4F166-F248-11E8-B48F-1D18A9856A87
last_name: Benková
orcid: 0000-0002-8510-9739
- first_name: Yoshihisa
full_name: Ikeda, Yoshihisa
last_name: Ikeda
- first_name: David
full_name: Zalabák, David
last_name: Zalabák
citation:
ama: Králová M, Kubalová I, Hajný J, et al. A decoy receptor derived from alternative
splicing fine-tunes cytokinin signaling in Arabidopsis. Molecular Plant.
2024;17(12):1850-1865. doi:10.1016/j.molp.2024.11.001
apa: Králová, M., Kubalová, I., Hajný, J., Kubiasova, K., Vagaská, K., Ge, Z., …
Zalabák, D. (2024). A decoy receptor derived from alternative splicing fine-tunes
cytokinin signaling in Arabidopsis. Molecular Plant. Elsevier. https://doi.org/10.1016/j.molp.2024.11.001
chicago: Králová, Michaela, Ivona Kubalová, Jakub Hajný, Karolina Kubiasova, Karolína
Vagaská, Zengxiang Ge, Michelle C Gallei, et al. “A Decoy Receptor Derived from
Alternative Splicing Fine-Tunes Cytokinin Signaling in Arabidopsis.” Molecular
Plant. Elsevier, 2024. https://doi.org/10.1016/j.molp.2024.11.001.
ieee: M. Králová et al., “A decoy receptor derived from alternative splicing
fine-tunes cytokinin signaling in Arabidopsis,” Molecular Plant, vol. 17,
no. 12. Elsevier, pp. 1850–1865, 2024.
ista: Králová M, Kubalová I, Hajný J, Kubiasova K, Vagaská K, Ge Z, Gallei MC, Semerádová
H, Kuchařová A, Hönig M, Monzer A, Kovačik M, Friml J, Novák O, Benková E, Ikeda
Y, Zalabák D. 2024. A decoy receptor derived from alternative splicing fine-tunes
cytokinin signaling in Arabidopsis. Molecular Plant. 17(12), 1850–1865.
mla: Králová, Michaela, et al. “A Decoy Receptor Derived from Alternative Splicing
Fine-Tunes Cytokinin Signaling in Arabidopsis.” Molecular Plant, vol. 17,
no. 12, Elsevier, 2024, pp. 1850–65, doi:10.1016/j.molp.2024.11.001.
short: M. Králová, I. Kubalová, J. Hajný, K. Kubiasova, K. Vagaská, Z. Ge, M.C.
Gallei, H. Semerádová, A. Kuchařová, M. Hönig, A. Monzer, M. Kovačik, J. Friml,
O. Novák, E. Benková, Y. Ikeda, D. Zalabák, Molecular Plant 17 (2024) 1850–1865.
date_created: 2024-11-28T11:13:35Z
date_published: 2024-12-02T00:00:00Z
date_updated: 2025-09-08T14:46:45Z
day: '02'
ddc:
- '580'
department:
- _id: JiFr
- _id: EvBe
doi: 10.1016/j.molp.2024.11.001
external_id:
isi:
- '001373778300001'
pmid:
- '39501563'
file:
- access_level: open_access
checksum: a11feea4b1677df76b632eca04bfc1dd
content_type: application/pdf
creator: dernst
date_created: 2024-12-03T11:08:09Z
date_updated: 2024-12-03T11:08:09Z
file_id: '18612'
file_name: 2024_MolecularPlant_Kralova.pdf
file_size: 3308945
relation: main_file
success: 1
file_date_updated: 2024-12-03T11:08:09Z
fulldoi: https://doi.org/10.1016/j.molp.2024.11.001
has_accepted_license: '1'
intvolume: ' 17'
isi: 1
issue: '12'
language:
- iso: eng
month: '12'
oa: 1
oa_version: Published Version
page: 1850-1865
pmid: 1
publication: Molecular Plant
publication_identifier:
issn:
- 1674-2052
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: A decoy receptor derived from alternative splicing fine-tunes cytokinin signaling
in Arabidopsis
tmp:
image: /images/cc_by_nc_nd.png
legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode
name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
(CC BY-NC-ND 4.0)
short: CC BY-NC-ND (4.0)
type: journal_article
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 17
year: '2024'
...
---
_id: '14826'
abstract:
- lang: eng
text: The plant-signaling molecule auxin triggers fast and slow cellular responses
across land plants and algae. The nuclear auxin pathway mediates gene expression
and controls growth and development in land plants, but this pathway is absent
from algal sister groups. Several components of rapid responses have been identified
in Arabidopsis, but it is unknown if these are part of a conserved mechanism.
We recently identified a fast, proteome-wide phosphorylation response to auxin.
Here, we show that this response occurs across 5 land plant and algal species
and converges on a core group of shared targets. We found conserved rapid physiological
responses to auxin in the same species and identified rapidly accelerated fibrosarcoma
(RAF)-like protein kinases as central mediators of auxin-triggered phosphorylation
across species. Genetic analysis connects this kinase to both auxin-triggered
protein phosphorylation and rapid cellular response, thus identifying an ancient
mechanism for fast auxin responses in the green lineage.
acknowledgement: 'We are grateful to Asuka Shitaku and Eri Koide for generating and
sharing the Marchantia PRAF-mCitrine line and Peng-Cheng Wang for sharing the Arabidopsis
raf mutant. We are grateful to our team members for discussions and helpful advice.
This work was supported by funding from the Netherlands Organization for Scientific
Research (NWO): VICI grant 865.14.001 and ENW-KLEIN OCENW.KLEIN.027 grants to D.W.;
VENI grant VI.VENI.212.003 to A.K.; the European Research Council AdG DIRNDL (contract
number 833867) to D.W.; CoG CATCH to J.S.; StG CELLONGATE (contract 803048) to M.F.;
and AdG ETAP (contract 742985) to J.F.; MEXT KAKENHI grant number JP19H05675 to
T.K.; JSPS KAKENHI grant number JP20H03275 to R.N.; Takeda Science Foundation to
R.N.; and the Austrian Science Fund (FWF, P29988) to J.F.'
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Andre
full_name: Kuhn, Andre
last_name: Kuhn
- first_name: Mark
full_name: Roosjen, Mark
last_name: Roosjen
- first_name: Sumanth
full_name: Mutte, Sumanth
last_name: Mutte
- first_name: Shiv Mani
full_name: Dubey, Shiv Mani
last_name: Dubey
- first_name: Vanessa Polet
full_name: Carrillo Carrasco, Vanessa Polet
last_name: Carrillo Carrasco
- first_name: Sjef
full_name: Boeren, Sjef
last_name: Boeren
- first_name: Aline
full_name: Monzer, Aline
id: 2DB5D88C-D7B3-11E9-B8FD-7907E6697425
last_name: Monzer
- first_name: Jasper
full_name: Koehorst, Jasper
last_name: Koehorst
- first_name: Takayuki
full_name: Kohchi, Takayuki
last_name: Kohchi
- first_name: Ryuichi
full_name: Nishihama, Ryuichi
last_name: Nishihama
- first_name: Matyas
full_name: Fendrych, Matyas
id: 43905548-F248-11E8-B48F-1D18A9856A87
last_name: Fendrych
orcid: 0000-0002-9767-8699
- first_name: Joris
full_name: Sprakel, Joris
last_name: Sprakel
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
- first_name: Dolf
full_name: Weijers, Dolf
last_name: Weijers
citation:
ama: Kuhn A, Roosjen M, Mutte S, et al. RAF-like protein kinases mediate a deeply
conserved, rapid auxin response. Cell. 2024;187(1):130-148.e17. doi:10.1016/j.cell.2023.11.021
apa: Kuhn, A., Roosjen, M., Mutte, S., Dubey, S. M., Carrillo Carrasco, V. P., Boeren,
S., … Weijers, D. (2024). RAF-like protein kinases mediate a deeply conserved,
rapid auxin response. Cell. Elsevier. https://doi.org/10.1016/j.cell.2023.11.021
chicago: Kuhn, Andre, Mark Roosjen, Sumanth Mutte, Shiv Mani Dubey, Vanessa Polet
Carrillo Carrasco, Sjef Boeren, Aline Monzer, et al. “RAF-like Protein Kinases
Mediate a Deeply Conserved, Rapid Auxin Response.” Cell. Elsevier, 2024.
https://doi.org/10.1016/j.cell.2023.11.021.
ieee: A. Kuhn et al., “RAF-like protein kinases mediate a deeply conserved,
rapid auxin response,” Cell, vol. 187, no. 1. Elsevier, p. 130–148.e17,
2024.
ista: Kuhn A, Roosjen M, Mutte S, Dubey SM, Carrillo Carrasco VP, Boeren S, Monzer
A, Koehorst J, Kohchi T, Nishihama R, Fendrych M, Sprakel J, Friml J, Weijers
D. 2024. RAF-like protein kinases mediate a deeply conserved, rapid auxin response.
Cell. 187(1), 130–148.e17.
mla: Kuhn, Andre, et al. “RAF-like Protein Kinases Mediate a Deeply Conserved, Rapid
Auxin Response.” Cell, vol. 187, no. 1, Elsevier, 2024, p. 130–148.e17,
doi:10.1016/j.cell.2023.11.021.
short: A. Kuhn, M. Roosjen, S. Mutte, S.M. Dubey, V.P. Carrillo Carrasco, S. Boeren,
A. Monzer, J. Koehorst, T. Kohchi, R. Nishihama, M. Fendrych, J. Sprakel, J. Friml,
D. Weijers, Cell 187 (2024) 130–148.e17.
date_created: 2024-01-17T12:45:40Z
date_published: 2024-01-04T00:00:00Z
date_updated: 2026-08-14T09:33:45Z
day: '04'
ddc:
- '580'
department:
- _id: JiFr
doi: 10.1016/j.cell.2023.11.021
ec_funded: 1
external_id:
isi:
- '001152705700001'
pmid:
- '38128538'
file:
- access_level: open_access
checksum: 06fd236a9ee0b46ccb05f44695bfc34b
content_type: application/pdf
creator: dernst
date_created: 2024-01-22T13:41:41Z
date_updated: 2024-01-22T13:41:41Z
file_id: '14874'
file_name: 2024_Cell_Kuhn.pdf
file_size: 13194060
relation: main_file
success: 1
file_date_updated: 2024-01-22T13:41:41Z
fulldoi: https://doi.org/10.1016/j.cell.2023.11.021
has_accepted_license: '1'
intvolume: ' 187'
isi: 1
issue: '1'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc/4.0/
month: '01'
oa: 1
oa_version: Published Version
page: 130-148.e17
pmid: 1
project:
- _id: 261099A6-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '742985'
name: Tracing Evolution of Auxin Transport and Polarity in Plants
- _id: 262EF96E-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: P29988
name: RNA-directed DNA methylation in plant development
publication: Cell
publication_identifier:
eissn:
- 1097-4172
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
related_material:
record:
- id: '19395'
relation: dissertation_contains
status: public
scopus_import: '1'
status: public
title: RAF-like protein kinases mediate a deeply conserved, rapid auxin response
tmp:
image: /images/cc_by_nc.png
legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode
name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)
short: CC BY-NC (4.0)
type: journal_article
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 187
year: '2024'
...
---
OA_place: repository
_id: '14591'
abstract:
- lang: eng
text: Clathrin-mediated endocytosis (CME) is vital for the regulation of plant growth
and development by controlling plasma membrane protein composition and cargo uptake.
CME relies on the precise recruitment of regulators for vesicle maturation and
release. Homologues of components of mammalian vesicle scission are strong candidates
to be part of the scissin machinery in plants, but the precise roles of these
proteins in this process is not fully understood. Here, we characterised the roles
of Plant Dynamin-Related Proteins 2 (DRP2s) and SH3-domain containing protein
2 (SH3P2), the plant homologue to Dynamins’ recruiters, like Endophilin and Amphiphysin,
in the CME by combining high-resolution imaging of endocytic events in vivo and
characterisation of the purified proteins in vitro. Although DRP2s and SH3P2 arrive
similarly late during CME and physically interact, genetic analysis of the Dsh3p1,2,3
triple-mutant and complementation assays with non-SH3P2-interacting DRP2 variants
suggests that SH3P2 does not directly recruit DRP2s to the site of endocytosis.
These observations imply that despite the presence of many well-conserved endocytic
components, plants have acquired a distinct mechanism for CME. One Sentence Summary
In contrast to predictions based on mammalian systems, plant Dynamin-related proteins
2 are recruited to the site of Clathrin-mediated endocytosis independently of
BAR-SH3 proteins.
acknowledged_ssus:
- _id: EM-Fac
- _id: LifeSc
- _id: Bio
article_processing_charge: No
author:
- first_name: Nataliia
full_name: Gnyliukh, Nataliia
id: 390C1120-F248-11E8-B48F-1D18A9856A87
last_name: Gnyliukh
orcid: 0000-0002-2198-0509
- first_name: Alexander J
full_name: Johnson, Alexander J
id: 46A62C3A-F248-11E8-B48F-1D18A9856A87
last_name: Johnson
orcid: 0000-0002-2739-8843
- first_name: Marie-Kristin
full_name: Nagel, Marie-Kristin
last_name: Nagel
- first_name: Aline
full_name: Monzer, Aline
id: 2DB5D88C-D7B3-11E9-B8FD-7907E6697425
last_name: Monzer
- first_name: Annamaria
full_name: Hlavata, Annamaria
id: 36062FEC-F248-11E8-B48F-1D18A9856A87
last_name: Hlavata
- first_name: Erika
full_name: Isono, Erika
last_name: Isono
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
citation:
ama: Gnyliukh N, Johnson AJ, Nagel M-K, et al. Role of dynamin-related proteins
2 and SH3P2 in clathrin-mediated endocytosis in plants. bioRxiv. doi:10.1101/2023.10.09.561523
apa: Gnyliukh, N., Johnson, A. J., Nagel, M.-K., Monzer, A., Hlavata, A., Isono,
E., … Friml, J. (n.d.). Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated
endocytosis in plants. bioRxiv. https://doi.org/10.1101/2023.10.09.561523
chicago: Gnyliukh, Nataliia, Alexander J Johnson, Marie-Kristin Nagel, Aline Monzer,
Annamaria Hlavata, Erika Isono, Martin Loose, and Jiří Friml. “Role of Dynamin-Related
Proteins 2 and SH3P2 in Clathrin-Mediated Endocytosis in Plants.” BioRxiv,
n.d. https://doi.org/10.1101/2023.10.09.561523.
ieee: N. Gnyliukh et al., “Role of dynamin-related proteins 2 and SH3P2 in
clathrin-mediated endocytosis in plants,” bioRxiv. .
ista: Gnyliukh N, Johnson AJ, Nagel M-K, Monzer A, Hlavata A, Isono E, Loose M,
Friml J. Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated endocytosis
in plants. bioRxiv, 10.1101/2023.10.09.561523.
mla: Gnyliukh, Nataliia, et al. “Role of Dynamin-Related Proteins 2 and SH3P2 in
Clathrin-Mediated Endocytosis in Plants.” BioRxiv, doi:10.1101/2023.10.09.561523.
short: N. Gnyliukh, A.J. Johnson, M.-K. Nagel, A. Monzer, A. Hlavata, E. Isono,
M. Loose, J. Friml, BioRxiv (n.d.).
corr_author: '1'
date_created: 2023-11-22T10:17:49Z
date_published: 2023-10-10T00:00:00Z
date_updated: 2026-09-11T22:30:57Z
day: '10'
department:
- _id: JiFr
- _id: MaLo
- _id: CaBe
doi: 10.1101/2023.10.09.561523
ec_funded: 1
fulldoi: https://doi.org/10.1101/2023.10.09.561523
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1101/2023.10.09.561523
month: '10'
oa: 1
oa_version: Preprint
project:
- _id: 2564DBCA-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '665385'
name: International IST Doctoral Program
publication: bioRxiv
publication_status: draft
related_material:
record:
- id: '15330'
relation: later_version
status: public
- id: '14510'
relation: dissertation_contains
status: public
status: public
title: Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated endocytosis
in plants
type: preprint
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2023'
...
---
_id: '12291'
abstract:
- lang: eng
text: The phytohormone auxin triggers transcriptional reprogramming through a well-characterized
perception machinery in the nucleus. By contrast, mechanisms that underlie fast
effects of auxin, such as the regulation of ion fluxes, rapid phosphorylation
of proteins or auxin feedback on its transport, remain unclear1,2,3. Whether auxin-binding
protein 1 (ABP1) is an auxin receptor has been a source of debate for decades1,4.
Here we show that a fraction of Arabidopsis thaliana ABP1 is secreted and binds
auxin specifically at an acidic pH that is typical of the apoplast. ABP1 and its
plasma-membrane-localized partner, transmembrane kinase 1 (TMK1), are required
for the auxin-induced ultrafast global phospho-response and for downstream processes
that include the activation of H+-ATPase and accelerated cytoplasmic streaming.
abp1 and tmk mutants cannot establish auxin-transporting channels and show defective
auxin-induced vasculature formation and regeneration. An ABP1(M2X) variant that
lacks the capacity to bind auxin is unable to complement these defects in abp1
mutants. These data indicate that ABP1 is the auxin receptor for TMK1-based cell-surface
signalling, which mediates the global phospho-response and auxin canalization.
acknowledged_ssus:
- _id: Bio
- _id: EM-Fac
- _id: LifeSc
acknowledgement: We acknowledge K. Kubiasová for excellent technical assistance, J.
Neuhold, A. Lehner and A. Sedivy for technical assistance with protein production
and purification at Vienna Biocenter Core Facilities; Creoptix for performing GCI;
and the Bioimaging, Electron Microscopy and Life Science Facilities at ISTA, the
Plant Sciences Core Facility of CEITEC Masaryk University, the Core Facility CELLIM
(MEYS CR, LM2018129 Czech-BioImaging) and J. Sprakel for their assistance. J.F.
is grateful to R. Napier for many insightful suggestions and support. We thank all
past and present members of the Friml group for their support and for other contributions
to this effort to clarify the controversial role of ABP1 over the past seven years.
The project received funding from the European Research Council (ERC) under the
European Union’s Horizon 2020 research and innovation program (grant agreement no.
742985 to J.F. and 833867 to D.W.); the Austrian Science Fund (FWF; P29988 to J.F.);
the Netherlands Organization for Scientific Research (NWO; VICI grant 865.14.001
to D.W. and VENI grant VI.Veni.212.003 to A.K.); the Ministry of Education, Science
and Technological Development of the Republic of Serbia (contract no. 451-03-68/2022-14/200053
to B.D.Ž.); and the MEXT/JSPS KAKENHI to K.T. (20K06685) and T.K. (20H05687 and
20H05910).
article_processing_charge: No
article_type: original
author:
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
- first_name: Michelle C
full_name: Gallei, Michelle C
id: 35A03822-F248-11E8-B48F-1D18A9856A87
last_name: Gallei
orcid: 0000-0003-1286-7368
- first_name: Zuzana
full_name: Gelová, Zuzana
id: 0AE74790-0E0B-11E9-ABC7-1ACFE5697425
last_name: Gelová
orcid: 0000-0003-4783-1752
- first_name: Alexander J
full_name: Johnson, Alexander J
id: 46A62C3A-F248-11E8-B48F-1D18A9856A87
last_name: Johnson
orcid: 0000-0002-2739-8843
- first_name: Ewa
full_name: Mazur, Ewa
last_name: Mazur
- first_name: Aline
full_name: Monzer, Aline
id: 2DB5D88C-D7B3-11E9-B8FD-7907E6697425
last_name: Monzer
- first_name: Lesia
full_name: Rodriguez Solovey, Lesia
id: 3922B506-F248-11E8-B48F-1D18A9856A87
last_name: Rodriguez Solovey
orcid: 0000-0002-7244-7237
- first_name: Mark
full_name: Roosjen, Mark
last_name: Roosjen
- first_name: Inge
full_name: Verstraeten, Inge
id: 362BF7FE-F248-11E8-B48F-1D18A9856A87
last_name: Verstraeten
orcid: 0000-0001-7241-2328
- first_name: Branka D.
full_name: Živanović, Branka D.
last_name: Živanović
- first_name: Minxia
full_name: Zou, Minxia
id: 5c243f41-03f3-11ec-841c-96faf48a7ef9
last_name: Zou
- first_name: Lukas
full_name: Fiedler, Lukas
id: 7c417475-8972-11ed-ae7b-8b674ca26986
last_name: Fiedler
- first_name: Caterina
full_name: Giannini, Caterina
id: e3fdddd5-f6e0-11ea-865d-ca99ee6367f4
last_name: Giannini
- first_name: Peter
full_name: Grones, Peter
last_name: Grones
- first_name: Mónika
full_name: Hrtyan, Mónika
id: 45A71A74-F248-11E8-B48F-1D18A9856A87
last_name: Hrtyan
- first_name: Walter
full_name: Kaufmann, Walter
id: 3F99E422-F248-11E8-B48F-1D18A9856A87
last_name: Kaufmann
orcid: 0000-0001-9735-5315
- first_name: Andre
full_name: Kuhn, Andre
last_name: Kuhn
- first_name: Madhumitha
full_name: Narasimhan, Madhumitha
id: 44BF24D0-F248-11E8-B48F-1D18A9856A87
last_name: Narasimhan
orcid: 0000-0002-8600-0671
- first_name: Marek
full_name: Randuch, Marek
id: 6ac4636d-15b2-11ec-abd3-fb8df79972ae
last_name: Randuch
- first_name: Nikola
full_name: Rýdza, Nikola
last_name: Rýdza
- first_name: Koji
full_name: Takahashi, Koji
last_name: Takahashi
- first_name: Shutang
full_name: Tan, Shutang
id: 2DE75584-F248-11E8-B48F-1D18A9856A87
last_name: Tan
orcid: 0000-0002-0471-8285
- first_name: Anastasiia
full_name: Teplova, Anastasiia
id: e3736151-106c-11ec-b916-c2558e2762c6
last_name: Teplova
- first_name: Toshinori
full_name: Kinoshita, Toshinori
last_name: Kinoshita
- first_name: Dolf
full_name: Weijers, Dolf
last_name: Weijers
- first_name: Hana
full_name: Rakusová, Hana
last_name: Rakusová
citation:
ama: Friml J, Gallei MC, Gelová Z, et al. ABP1–TMK auxin perception for global phosphorylation
and auxin canalization. Nature. 2022;609(7927):575-581. doi:10.1038/s41586-022-05187-x
apa: Friml, J., Gallei, M. C., Gelová, Z., Johnson, A. J., Mazur, E., Monzer, A.,
… Rakusová, H. (2022). ABP1–TMK auxin perception for global phosphorylation and
auxin canalization. Nature. Springer Nature. https://doi.org/10.1038/s41586-022-05187-x
chicago: Friml, Jiří, Michelle C Gallei, Zuzana Gelová, Alexander J Johnson, Ewa
Mazur, Aline Monzer, Lesia Rodriguez Solovey, et al. “ABP1–TMK Auxin Perception
for Global Phosphorylation and Auxin Canalization.” Nature. Springer Nature,
2022. https://doi.org/10.1038/s41586-022-05187-x.
ieee: J. Friml et al., “ABP1–TMK auxin perception for global phosphorylation
and auxin canalization,” Nature, vol. 609, no. 7927. Springer Nature, pp.
575–581, 2022.
ista: Friml J, Gallei MC, Gelová Z, Johnson AJ, Mazur E, Monzer A, Rodriguez Solovey
L, Roosjen M, Verstraeten I, Živanović BD, Zou M, Fiedler L, Giannini C, Grones
P, Hrtyan M, Kaufmann W, Kuhn A, Narasimhan M, Randuch M, Rýdza N, Takahashi K,
Tan S, Teplova A, Kinoshita T, Weijers D, Rakusová H. 2022. ABP1–TMK auxin perception
for global phosphorylation and auxin canalization. Nature. 609(7927), 575–581.
mla: Friml, Jiří, et al. “ABP1–TMK Auxin Perception for Global Phosphorylation and
Auxin Canalization.” Nature, vol. 609, no. 7927, Springer Nature, 2022,
pp. 575–81, doi:10.1038/s41586-022-05187-x.
short: J. Friml, M.C. Gallei, Z. Gelová, A.J. Johnson, E. Mazur, A. Monzer, L. Rodriguez
Solovey, M. Roosjen, I. Verstraeten, B.D. Živanović, M. Zou, L. Fiedler, C. Giannini,
P. Grones, M. Hrtyan, W. Kaufmann, A. Kuhn, M. Narasimhan, M. Randuch, N. Rýdza,
K. Takahashi, S. Tan, A. Teplova, T. Kinoshita, D. Weijers, H. Rakusová, Nature
609 (2022) 575–581.
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