---
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. <i>Molecular Plant</i>.
    2024;17(12):1850-1865. doi:<a href="https://doi.org/10.1016/j.molp.2024.11.001">10.1016/j.molp.2024.11.001</a>
  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. <i>Molecular Plant</i>. Elsevier. <a href="https://doi.org/10.1016/j.molp.2024.11.001">https://doi.org/10.1016/j.molp.2024.11.001</a>
  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.” <i>Molecular
    Plant</i>. Elsevier, 2024. <a href="https://doi.org/10.1016/j.molp.2024.11.001">https://doi.org/10.1016/j.molp.2024.11.001</a>.
  ieee: M. Králová <i>et al.</i>, “A decoy receptor derived from alternative splicing
    fine-tunes cytokinin signaling in Arabidopsis,” <i>Molecular Plant</i>, 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.” <i>Molecular Plant</i>, vol. 17,
    no. 12, Elsevier, 2024, pp. 1850–65, doi:<a href="https://doi.org/10.1016/j.molp.2024.11.001">10.1016/j.molp.2024.11.001</a>.
  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
has_accepted_license: '1'
intvolume: '        17'
isi: 1
issue: '12'
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc-nd/4.0/
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: '12239'
abstract:
- lang: eng
  text: Biological systems are the sum of their dynamic three-dimensional (3D) parts.
    Therefore, it is critical to study biological structures in 3D and at high resolution
    to gain insights into their physiological functions. Electron microscopy of metal
    replicas of unroofed cells and isolated organelles has been a key technique to
    visualize intracellular structures at nanometer resolution. However, many of these
    methods require specialized equipment and personnel to complete them. Here, we
    present novel accessible methods to analyze biological structures in unroofed
    cells and biochemically isolated organelles in 3D and at nanometer resolution,
    focusing on Arabidopsis clathrin-coated vesicles (CCVs). While CCVs are essential
    trafficking organelles, their detailed structural information is lacking due to
    their poor preservation when observed via classical electron microscopy protocols
    experiments. First, we establish a method to visualize CCVs in unroofed cells
    using scanning transmission electron microscopy tomography, providing sufficient
    resolution to define the clathrin coat arrangements. Critically, the samples are
    prepared directly on electron microscopy grids, removing the requirement to use
    extremely corrosive acids, thereby enabling the use of this method in any electron
    microscopy lab. Secondly, we demonstrate that this standardized sample preparation
    allows the direct comparison of isolated CCV samples with those visualized in
    cells. Finally, to facilitate the high-throughput and robust screening of metal
    replicated samples, we provide a deep learning analysis method to screen the “pseudo
    3D” morphologies of CCVs imaged with 2D modalities. Collectively, our work establishes
    accessible ways to examine the 3D structure of biological samples and provide
    novel insights into the structure of plant CCVs.
acknowledged_ssus:
- _id: EM-Fac
- _id: LifeSc
- _id: Bio
acknowledgement: A.J. is supported by funding from the Austrian Science Fund I3630B25
  (to J.F.). This research was supported by the Scientific Service Units of Institute
  of Science and Technology Austria (ISTA) through resources provided by the Electron
  Microscopy Facility, Lab Support Facility, and the Imaging and Optics Facility.
  We acknowledge Prof. David Robinson (Heidelberg) and Prof. Jan Traas (Lyon) for
  making us aware of previously published classical on-grid preparation methods. No
  conflict of interest declared.
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- 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: Walter
  full_name: Kaufmann, Walter
  id: 3F99E422-F248-11E8-B48F-1D18A9856A87
  last_name: Kaufmann
  orcid: 0000-0001-9735-5315
- first_name: Christoph M
  full_name: Sommer, Christoph M
  id: 4DF26D8C-F248-11E8-B48F-1D18A9856A87
  last_name: Sommer
  orcid: 0000-0003-1216-9105
- first_name: Tommaso
  full_name: Costanzo, Tommaso
  id: D93824F4-D9BA-11E9-BB12-F207E6697425
  last_name: Costanzo
  orcid: 0000-0001-9732-3815
- first_name: Dana A.
  full_name: Dahhan, Dana A.
  last_name: Dahhan
- first_name: Sebastian Y.
  full_name: Bednarek, Sebastian Y.
  last_name: Bednarek
- first_name: Jiří
  full_name: Friml, Jiří
  id: 4159519E-F248-11E8-B48F-1D18A9856A87
  last_name: Friml
  orcid: 0000-0002-8302-7596
citation:
  ama: Johnson AJ, Kaufmann W, Sommer CM, et al. Three-dimensional visualization of
    planta clathrin-coated vesicles at ultrastructural resolution. <i>Molecular Plant</i>.
    2022;15(10):1533-1542. doi:<a href="https://doi.org/10.1016/j.molp.2022.09.003">10.1016/j.molp.2022.09.003</a>
  apa: Johnson, A. J., Kaufmann, W., Sommer, C. M., Costanzo, T., Dahhan, D. A., Bednarek,
    S. Y., &#38; Friml, J. (2022). Three-dimensional visualization of planta clathrin-coated
    vesicles at ultrastructural resolution. <i>Molecular Plant</i>. Elsevier. <a href="https://doi.org/10.1016/j.molp.2022.09.003">https://doi.org/10.1016/j.molp.2022.09.003</a>
  chicago: Johnson, Alexander J, Walter Kaufmann, Christoph M Sommer, Tommaso Costanzo,
    Dana A. Dahhan, Sebastian Y. Bednarek, and Jiří Friml. “Three-Dimensional Visualization
    of Planta Clathrin-Coated Vesicles at Ultrastructural Resolution.” <i>Molecular
    Plant</i>. Elsevier, 2022. <a href="https://doi.org/10.1016/j.molp.2022.09.003">https://doi.org/10.1016/j.molp.2022.09.003</a>.
  ieee: A. J. Johnson <i>et al.</i>, “Three-dimensional visualization of planta clathrin-coated
    vesicles at ultrastructural resolution,” <i>Molecular Plant</i>, vol. 15, no.
    10. Elsevier, pp. 1533–1542, 2022.
  ista: Johnson AJ, Kaufmann W, Sommer CM, Costanzo T, Dahhan DA, Bednarek SY, Friml
    J. 2022. Three-dimensional visualization of planta clathrin-coated vesicles at
    ultrastructural resolution. Molecular Plant. 15(10), 1533–1542.
  mla: Johnson, Alexander J., et al. “Three-Dimensional Visualization of Planta Clathrin-Coated
    Vesicles at Ultrastructural Resolution.” <i>Molecular Plant</i>, vol. 15, no.
    10, Elsevier, 2022, pp. 1533–42, doi:<a href="https://doi.org/10.1016/j.molp.2022.09.003">10.1016/j.molp.2022.09.003</a>.
  short: A.J. Johnson, W. Kaufmann, C.M. Sommer, T. Costanzo, D.A. Dahhan, S.Y. Bednarek,
    J. Friml, Molecular Plant 15 (2022) 1533–1542.
corr_author: '1'
date_created: 2023-01-16T09:51:49Z
date_published: 2022-10-03T00:00:00Z
date_updated: 2025-04-15T07:32:09Z
day: '03'
ddc:
- '580'
department:
- _id: JiFr
- _id: EM-Fac
- _id: Bio
doi: 10.1016/j.molp.2022.09.003
external_id:
  isi:
  - '000882769800009'
  pmid:
  - '36081349'
file:
- access_level: open_access
  checksum: 04d5c12490052d03e4dc4412338a43dd
  content_type: application/pdf
  creator: dernst
  date_created: 2023-01-30T07:46:51Z
  date_updated: 2023-01-30T07:46:51Z
  file_id: '12435'
  file_name: 2022_MolecularPlant_Johnson.pdf
  file_size: 2307251
  relation: main_file
  success: 1
file_date_updated: 2023-01-30T07:46:51Z
has_accepted_license: '1'
intvolume: '        15'
isi: 1
issue: '10'
keyword:
- Plant Science
- Molecular Biology
language:
- iso: eng
license: https://creativecommons.org/licenses/by/4.0/
month: '10'
oa: 1
oa_version: Published Version
page: 1533-1542
pmid: 1
project:
- _id: 26538374-B435-11E9-9278-68D0E5697425
  call_identifier: FWF
  grant_number: I03630
  name: Molecular mechanisms of endocytic cargo recognition in plants
publication: Molecular Plant
publication_identifier:
  issn:
  - 1674-2052
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Three-dimensional visualization of planta clathrin-coated vesicles at ultrastructural
  resolution
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: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 15
year: '2022'
...
---
_id: '8992'
abstract:
- lang: eng
  text: The phytohormone auxin plays a central role in shaping plant growth and development.
    With decades of genetic and biochemical studies, numerous core molecular components
    and their networks, underlying auxin biosynthesis, transport, and signaling, have
    been identified. Notably, protein phosphorylation, catalyzed by kinases and oppositely
    hydrolyzed by phosphatases, has been emerging to be a crucial type of post-translational
    modification, regulating physiological and developmental auxin output at all levels.
    In this review, we comprehensively discuss earlier and recent advances in our
    understanding of genetics, biochemistry, and cell biology of the kinases and phosphatases
    participating in auxin action. We provide insights into the mechanisms by which
    reversible protein phosphorylation defines developmental auxin responses, discuss
    current challenges, and provide our perspectives on future directions involving
    the integration of the control of protein phosphorylation into the molecular auxin
    network.
acknowledgement: This work was supported by the European Union’s Horizon 2020 Program
  (ERC grant agreement no. 742985 to J.F.). S.T. was funded by a European Molecular
  Biology Organization (EMBO) long-term postdoctoral fellowship (ALTF 723-2015). C.L.
  is supported by the Austrian Science Fund (FWF; P 31493).
article_processing_charge: No
article_type: original
author:
- first_name: Shutang
  full_name: Tan, Shutang
  id: 2DE75584-F248-11E8-B48F-1D18A9856A87
  last_name: Tan
  orcid: 0000-0002-0471-8285
- first_name: Christian
  full_name: Luschnig, Christian
  last_name: Luschnig
- first_name: Jiří
  full_name: Friml, Jiří
  id: 4159519E-F248-11E8-B48F-1D18A9856A87
  last_name: Friml
  orcid: 0000-0002-8302-7596
citation:
  ama: 'Tan S, Luschnig C, Friml J. Pho-view of auxin: Reversible protein phosphorylation
    in auxin biosynthesis, transport and signaling. <i>Molecular Plant</i>. 2021;14(1):151-165.
    doi:<a href="https://doi.org/10.1016/j.molp.2020.11.004">10.1016/j.molp.2020.11.004</a>'
  apa: 'Tan, S., Luschnig, C., &#38; Friml, J. (2021). Pho-view of auxin: Reversible
    protein phosphorylation in auxin biosynthesis, transport and signaling. <i>Molecular
    Plant</i>. Elsevier. <a href="https://doi.org/10.1016/j.molp.2020.11.004">https://doi.org/10.1016/j.molp.2020.11.004</a>'
  chicago: 'Tan, Shutang, Christian Luschnig, and Jiří Friml. “Pho-View of Auxin:
    Reversible Protein Phosphorylation in Auxin Biosynthesis, Transport and Signaling.”
    <i>Molecular Plant</i>. Elsevier, 2021. <a href="https://doi.org/10.1016/j.molp.2020.11.004">https://doi.org/10.1016/j.molp.2020.11.004</a>.'
  ieee: 'S. Tan, C. Luschnig, and J. Friml, “Pho-view of auxin: Reversible protein
    phosphorylation in auxin biosynthesis, transport and signaling,” <i>Molecular
    Plant</i>, vol. 14, no. 1. Elsevier, pp. 151–165, 2021.'
  ista: 'Tan S, Luschnig C, Friml J. 2021. Pho-view of auxin: Reversible protein phosphorylation
    in auxin biosynthesis, transport and signaling. Molecular Plant. 14(1), 151–165.'
  mla: 'Tan, Shutang, et al. “Pho-View of Auxin: Reversible Protein Phosphorylation
    in Auxin Biosynthesis, Transport and Signaling.” <i>Molecular Plant</i>, vol.
    14, no. 1, Elsevier, 2021, pp. 151–65, doi:<a href="https://doi.org/10.1016/j.molp.2020.11.004">10.1016/j.molp.2020.11.004</a>.'
  short: S. Tan, C. Luschnig, J. Friml, Molecular Plant 14 (2021) 151–165.
date_created: 2021-01-03T23:01:23Z
date_published: 2021-01-04T00:00:00Z
date_updated: 2025-07-10T12:01:28Z
day: '04'
ddc:
- '580'
department:
- _id: JiFr
doi: 10.1016/j.molp.2020.11.004
ec_funded: 1
external_id:
  isi:
  - '000605359400014'
  pmid:
  - '33186755'
file:
- access_level: open_access
  checksum: 917e60e57092f22e16beac70b1775ea6
  content_type: application/pdf
  creator: dernst
  date_created: 2021-01-07T14:03:53Z
  date_updated: 2021-01-07T14:03:53Z
  file_id: '8995'
  file_name: 2020_MolecularPlant_Tan.pdf
  file_size: 871088
  relation: main_file
  success: 1
file_date_updated: 2021-01-07T14:03:53Z
has_accepted_license: '1'
intvolume: '        14'
isi: 1
issue: '1'
language:
- iso: eng
month: '01'
oa: 1
oa_version: Published Version
page: 151-165
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: 256FEF10-B435-11E9-9278-68D0E5697425
  grant_number: 723-2015
  name: Molecular Mechanism underlying Salicylic Acid Regulation of Endocytic Trafficking
    in Arabidopsis
publication: Molecular Plant
publication_identifier:
  eissn:
  - 1752-9867
  issn:
  - 1674-2052
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'Pho-view of auxin: Reversible protein phosphorylation in auxin biosynthesis,
  transport and signaling'
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: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 14
year: '2021'
...
---
_id: '15037'
abstract:
- lang: eng
  text: Protein abundance and localization at the plasma membrane (PM) shapes plant
    development and mediates adaptation to changing environmental conditions. It is
    regulated by ubiquitination, a post-translational modification crucial for the
    proper sorting of endocytosed PM proteins to the vacuole for subsequent degradation.
    To understand the significance and the variety of roles played by this reversible
    modification, the function of ubiquitin receptors, which translate the ubiquitin
    signature into a cellular response, needs to be elucidated. In this study, we
    show that TOL (TOM1-like) proteins function in plants as multivalent ubiquitin
    receptors, governing ubiquitinated cargo delivery to the vacuole via the conserved
    Endosomal Sorting Complex Required for Transport (ESCRT) pathway. TOL2 and TOL6
    interact with components of the ESCRT machinery and bind to K63-linked ubiquitin
    via two tandemly arranged conserved ubiquitin-binding domains. Mutation of these
    domains results not only in a loss of ubiquitin binding but also altered localization,
    abolishing TOL6 ubiquitin receptor activity. Function and localization of TOL6
    is itself regulated by ubiquitination, whereby TOL6 ubiquitination potentially
    modulates degradation of PM-localized cargoes, assisting in the fine-tuning of
    the delicate interplay between protein recycling and downregulation. Taken together,
    our findings demonstrate the function and regulation of a ubiquitin receptor that
    mediates vacuolar degradation of PM proteins in higher plants.
article_processing_charge: No
article_type: original
author:
- first_name: Jeanette
  full_name: Moulinier-Anzola, Jeanette
  last_name: Moulinier-Anzola
- first_name: Maximilian
  full_name: Schwihla, Maximilian
  last_name: Schwihla
- first_name: Lucinda
  full_name: De-Araújo, Lucinda
  last_name: De-Araújo
- first_name: Christina
  full_name: Artner, Christina
  id: 45DF286A-F248-11E8-B48F-1D18A9856A87
  last_name: Artner
- first_name: Lisa
  full_name: Jörg, Lisa
  last_name: Jörg
- first_name: Nataliia
  full_name: Konstantinova, Nataliia
  last_name: Konstantinova
- first_name: Christian
  full_name: Luschnig, Christian
  last_name: Luschnig
- first_name: Barbara
  full_name: Korbei, Barbara
  last_name: Korbei
citation:
  ama: Moulinier-Anzola J, Schwihla M, De-Araújo L, et al. TOLs function as ubiquitin
    receptors in the early steps of the ESCRT pathway in higher plants. <i>Molecular
    Plant</i>. 2020;13(5):717-731. doi:<a href="https://doi.org/10.1016/j.molp.2020.02.012">10.1016/j.molp.2020.02.012</a>
  apa: Moulinier-Anzola, J., Schwihla, M., De-Araújo, L., Artner, C., Jörg, L., Konstantinova,
    N., … Korbei, B. (2020). TOLs function as ubiquitin receptors in the early steps
    of the ESCRT pathway in higher plants. <i>Molecular Plant</i>. Elsevier. <a href="https://doi.org/10.1016/j.molp.2020.02.012">https://doi.org/10.1016/j.molp.2020.02.012</a>
  chicago: Moulinier-Anzola, Jeanette, Maximilian Schwihla, Lucinda De-Araújo, Christina
    Artner, Lisa Jörg, Nataliia Konstantinova, Christian Luschnig, and Barbara Korbei.
    “TOLs Function as Ubiquitin Receptors in the Early Steps of the ESCRT Pathway
    in Higher Plants.” <i>Molecular Plant</i>. Elsevier, 2020. <a href="https://doi.org/10.1016/j.molp.2020.02.012">https://doi.org/10.1016/j.molp.2020.02.012</a>.
  ieee: J. Moulinier-Anzola <i>et al.</i>, “TOLs function as ubiquitin receptors in
    the early steps of the ESCRT pathway in higher plants,” <i>Molecular Plant</i>,
    vol. 13, no. 5. Elsevier, pp. 717–731, 2020.
  ista: Moulinier-Anzola J, Schwihla M, De-Araújo L, Artner C, Jörg L, Konstantinova
    N, Luschnig C, Korbei B. 2020. TOLs function as ubiquitin receptors in the early
    steps of the ESCRT pathway in higher plants. Molecular Plant. 13(5), 717–731.
  mla: Moulinier-Anzola, Jeanette, et al. “TOLs Function as Ubiquitin Receptors in
    the Early Steps of the ESCRT Pathway in Higher Plants.” <i>Molecular Plant</i>,
    vol. 13, no. 5, Elsevier, 2020, pp. 717–31, doi:<a href="https://doi.org/10.1016/j.molp.2020.02.012">10.1016/j.molp.2020.02.012</a>.
  short: J. Moulinier-Anzola, M. Schwihla, L. De-Araújo, C. Artner, L. Jörg, N. Konstantinova,
    C. Luschnig, B. Korbei, Molecular Plant 13 (2020) 717–731.
date_created: 2024-02-28T08:55:56Z
date_published: 2020-05-04T00:00:00Z
date_updated: 2024-02-28T12:41:52Z
day: '04'
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publication_identifier:
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publisher: Elsevier
quality_controlled: '1'
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title: TOLs function as ubiquitin receptors in the early steps of the ESCRT pathway
  in higher plants
tmp:
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  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
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acknowledgement: We thank Dr. Gai Huang for his comments and help. We apologize to
  authors whose work could not be cited due to space limitation. No conflict of interest
  declared.
article_processing_charge: No
article_type: original
author:
- first_name: Peng
  full_name: He, Peng
  last_name: He
- first_name: Yuzhou
  full_name: Zhang, Yuzhou
  id: 3B6137F2-F248-11E8-B48F-1D18A9856A87
  last_name: Zhang
  orcid: 0000-0003-2627-6956
- first_name: Guanghui
  full_name: Xiao, Guanghui
  last_name: Xiao
citation:
  ama: He P, Zhang Y, Xiao G. Origin of a subgenome and genome evolution of allotetraploid
    cotton species. <i>Molecular Plant</i>. 2020;13(9):1238-1240. doi:<a href="https://doi.org/10.1016/j.molp.2020.07.006">10.1016/j.molp.2020.07.006</a>
  apa: He, P., Zhang, Y., &#38; Xiao, G. (2020). Origin of a subgenome and genome
    evolution of allotetraploid cotton species. <i>Molecular Plant</i>. Elsevier.
    <a href="https://doi.org/10.1016/j.molp.2020.07.006">https://doi.org/10.1016/j.molp.2020.07.006</a>
  chicago: He, Peng, Yuzhou Zhang, and Guanghui Xiao. “Origin of a Subgenome and Genome
    Evolution of Allotetraploid Cotton Species.” <i>Molecular Plant</i>. Elsevier,
    2020. <a href="https://doi.org/10.1016/j.molp.2020.07.006">https://doi.org/10.1016/j.molp.2020.07.006</a>.
  ieee: P. He, Y. Zhang, and G. Xiao, “Origin of a subgenome and genome evolution
    of allotetraploid cotton species,” <i>Molecular Plant</i>, vol. 13, no. 9. Elsevier,
    pp. 1238–1240, 2020.
  ista: He P, Zhang Y, Xiao G. 2020. Origin of a subgenome and genome evolution of
    allotetraploid cotton species. Molecular Plant. 13(9), 1238–1240.
  mla: He, Peng, et al. “Origin of a Subgenome and Genome Evolution of Allotetraploid
    Cotton Species.” <i>Molecular Plant</i>, vol. 13, no. 9, Elsevier, 2020, pp. 1238–40,
    doi:<a href="https://doi.org/10.1016/j.molp.2020.07.006">10.1016/j.molp.2020.07.006</a>.
  short: P. He, Y. Zhang, G. Xiao, Molecular Plant 13 (2020) 1238–1240.
date_created: 2020-08-16T22:00:57Z
date_published: 2020-09-07T00:00:00Z
date_updated: 2025-06-25T07:51:18Z
day: '07'
department:
- _id: JiFr
doi: 10.1016/j.molp.2020.07.006
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month: '09'
oa: 1
oa_version: Published Version
page: 1238-1240
pmid: 1
publication: Molecular Plant
publication_identifier:
  eissn:
  - 1752-9867
  issn:
  - 1674-2052
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Origin of a subgenome and genome evolution of allotetraploid cotton species
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 13
year: '2020'
...
