---
_id: '1213'
abstract:
- lang: eng
text: Bacterial cytokinesis is commonly initiated by the Z-ring, a dynamic cytoskeletal
structure that assembles at the site of division. Its primary component is FtsZ,
a tubulin-like GTPase, that like its eukaryotic relative forms protein filaments
in the presence of GTP. Since the discovery of the Z-ring 25 years ago, various
models for the role of FtsZ have been suggested. However, important information
about the architecture and dynamics of FtsZ filaments during cytokinesis is still
missing. One reason for this lack of knowledge has been the small size of bacteria,
which has made it difficult to resolve the orientation and dynamics of individual
FtsZ filaments in the Z-ring. While superresolution microscopy experiments have
helped to gain more information about the organization of the Z-ring in the dividing
cell, they were not yet able to elucidate a mechanism of how FtsZ filaments reorganize
during assembly and disassembly of the Z-ring. In this chapter, we explain how
to use an in vitro reconstitution approach to investigate the self-organization
of FtsZ filaments recruited to a biomimetic lipid bilayer by its membrane anchor
FtsA. We show how to perform single-molecule experiments to study the behavior
of individual FtsZ monomers during the constant reorganization of the FtsZ-FtsA
filament network. We describe how to analyze the dynamics of single molecules
and explain why this information can help to shed light onto possible mechanism
of Z-ring constriction. We believe that similar experimental approaches will be
useful to study the mechanism of membrane-based polymerization of other cytoskeletal
systems, not only from prokaryotic but also eukaryotic origin.
acknowledged_ssus:
- _id: Bio
acknowledgement: Natalia Baranova is supported by an EMBO Long-Term Fellowship (EMBO
ALTF 1163-2015) and Martin Loose by an ERC Starting Grant (ERCStG-2015-SelfOrganiCell).
alternative_title:
- Methods in Cell Biology
article_processing_charge: No
author:
- first_name: Natalia
full_name: Baranova, Natalia
id: 38661662-F248-11E8-B48F-1D18A9856A87
last_name: Baranova
orcid: 0000-0002-3086-9124
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
citation:
ama: 'Baranova NS, Loose M. Single-molecule measurements to study polymerization
dynamics of FtsZ-FtsA copolymers. In: Echard A, ed. Cytokinesis. Vol 137.
Academic Press; 2017:355-370. doi:10.1016/bs.mcb.2016.03.036'
apa: Baranova, N. S., & Loose, M. (2017). Single-molecule measurements to study
polymerization dynamics of FtsZ-FtsA copolymers. In A. Echard (Ed.), Cytokinesis
(Vol. 137, pp. 355–370). Academic Press. https://doi.org/10.1016/bs.mcb.2016.03.036
chicago: Baranova, Natalia S., and Martin Loose. “Single-Molecule Measurements to
Study Polymerization Dynamics of FtsZ-FtsA Copolymers.” In Cytokinesis,
edited by Arnaud Echard, 137:355–70. Academic Press, 2017. https://doi.org/10.1016/bs.mcb.2016.03.036.
ieee: N. S. Baranova and M. Loose, “Single-molecule measurements to study polymerization
dynamics of FtsZ-FtsA copolymers,” in Cytokinesis, vol. 137, A. Echard,
Ed. Academic Press, 2017, pp. 355–370.
ista: 'Baranova NS, Loose M. 2017.Single-molecule measurements to study polymerization
dynamics of FtsZ-FtsA copolymers. In: Cytokinesis. Methods in Cell Biology, vol.
137, 355–370.'
mla: Baranova, Natalia S., and Martin Loose. “Single-Molecule Measurements to Study
Polymerization Dynamics of FtsZ-FtsA Copolymers.” Cytokinesis, edited by
Arnaud Echard, vol. 137, Academic Press, 2017, pp. 355–70, doi:10.1016/bs.mcb.2016.03.036.
short: N.S. Baranova, M. Loose, in:, A. Echard (Ed.), Cytokinesis, Academic Press,
2017, pp. 355–370.
date_created: 2018-12-11T11:50:45Z
date_published: 2017-12-01T00:00:00Z
date_updated: 2025-07-10T11:50:24Z
day: '01'
department:
- _id: MaLo
doi: 10.1016/bs.mcb.2016.03.036
ec_funded: 1
editor:
- first_name: 'Arnaud '
full_name: 'Echard, Arnaud '
last_name: Echard
external_id:
isi:
- '000403542900022'
intvolume: ' 137'
isi: 1
language:
- iso: eng
month: '12'
oa_version: None
page: 355 - 370
project:
- _id: 2596EAB6-B435-11E9-9278-68D0E5697425
grant_number: ALTF 2015-1163
name: Synthesis of bacterial cell wall
- _id: 25681D80-B435-11E9-9278-68D0E5697425
call_identifier: FP7
grant_number: '291734'
name: International IST Postdoc Fellowship Programme
publication: Cytokinesis
publication_identifier:
issn:
- 0091-679X
publication_status: published
publisher: Academic Press
publist_id: '6134'
quality_controlled: '1'
scopus_import: '1'
status: public
title: Single-molecule measurements to study polymerization dynamics of FtsZ-FtsA
copolymers
type: book_chapter
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 137
year: '2017'
...
---
_id: '629'
abstract:
- lang: eng
text: Even simple cells like bacteria have precisely regulated cellular anatomies,
which allow them to grow, divide and to respond to internal or external cues with
high fidelity. How spatial and temporal intracellular organization in prokaryotic
cells is achieved and maintained on the basis of locally interacting proteins
still remains largely a mystery. Bulk biochemical assays with purified components
and in vivo experiments help us to approach key cellular processes from two opposite
ends, in terms of minimal and maximal complexity. However, to understand how cellular
phenomena emerge, that are more than the sum of their parts, we have to assemble
cellular subsystems step by step from the bottom up. Here, we review recent in
vitro reconstitution experiments with proteins of the bacterial cell division
machinery and illustrate how they help to shed light on fundamental cellular mechanisms
that constitute spatiotemporal order and regulate cell division.
author:
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Katja
full_name: Zieske, Katja
last_name: Zieske
- first_name: Petra
full_name: Schwille, Petra
last_name: Schwille
citation:
ama: 'Loose M, Zieske K, Schwille P. Reconstitution of protein dynamics involved
in bacterial cell division. In: Prokaryotic Cytoskeletons. Vol 84. Sub-Cellular
Biochemistry. Springer; 2017:419-444. doi:10.1007/978-3-319-53047-5_15'
apa: Loose, M., Zieske, K., & Schwille, P. (2017). Reconstitution of protein
dynamics involved in bacterial cell division. In Prokaryotic Cytoskeletons
(Vol. 84, pp. 419–444). Springer. https://doi.org/10.1007/978-3-319-53047-5_15
chicago: Loose, Martin, Katja Zieske, and Petra Schwille. “Reconstitution of Protein
Dynamics Involved in Bacterial Cell Division.” In Prokaryotic Cytoskeletons,
84:419–44. Sub-Cellular Biochemistry. Springer, 2017. https://doi.org/10.1007/978-3-319-53047-5_15.
ieee: M. Loose, K. Zieske, and P. Schwille, “Reconstitution of protein dynamics
involved in bacterial cell division,” in Prokaryotic Cytoskeletons, vol.
84, Springer, 2017, pp. 419–444.
ista: 'Loose M, Zieske K, Schwille P. 2017.Reconstitution of protein dynamics involved
in bacterial cell division. In: Prokaryotic Cytoskeletons. vol. 84, 419–444.'
mla: Loose, Martin, et al. “Reconstitution of Protein Dynamics Involved in Bacterial
Cell Division.” Prokaryotic Cytoskeletons, vol. 84, Springer, 2017, pp.
419–44, doi:10.1007/978-3-319-53047-5_15.
short: M. Loose, K. Zieske, P. Schwille, in:, Prokaryotic Cytoskeletons, Springer,
2017, pp. 419–444.
corr_author: '1'
date_created: 2018-12-11T11:47:35Z
date_published: 2017-05-13T00:00:00Z
date_updated: 2024-10-09T20:58:00Z
day: '13'
department:
- _id: MaLo
doi: 10.1007/978-3-319-53047-5_15
external_id:
pmid:
- '28500535'
intvolume: ' 84'
language:
- iso: eng
month: '05'
oa_version: None
page: 419 - 444
pmid: 1
publication: Prokaryotic Cytoskeletons
publication_identifier:
eisbn:
- 978-3-319-53047-5
publication_status: published
publisher: Springer
publist_id: '7165'
quality_controlled: '1'
scopus_import: 1
series_title: Sub-Cellular Biochemistry
status: public
title: Reconstitution of protein dynamics involved in bacterial cell division
type: book_chapter
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 84
year: '2017'
...
---
_id: '660'
abstract:
- lang: eng
text: Growing microtubules are protected from depolymerization by the presence of
a GTP or GDP/Pi cap. End-binding proteins of the EB1 family bind to the stabilizing
cap, allowing monitoring of its size in real time. The cap size has been shown
to correlate with instantaneous microtubule stability. Here we have quantitatively
characterized the properties of cap size fluctuations during steadystate growth
and have developed a theory predicting their timescale and amplitude from the
kinetics of microtubule growth and cap maturation. In contrast to growth speed
fluctuations, cap size fluctuations show a characteristic timescale, which is
defined by the lifetime of the cap sites. Growth fluctuations affect the amplitude
of cap size fluctuations; however, cap size does not affect growth speed, indicating
that microtubules are far from instability during most of their time of growth.
Our theory provides the basis for a quantitative understanding of microtubule
stability fluctuations during steady-state growth.
acknowledgement: We thank Philippe Cluzel for helpful discussions and Gunnar Pruessner
for data analysis advice. This work was supported by the Francis Crick Institute,
which receives its core funding from Cancer Research UK Grant FC001163, Medical
Research Council Grant FC001163, and Wellcome Trust Grant FC001163. This work was
also supported by European Research Council Advanced Grant Project 323042 (to C.D.
and T.S.).
article_processing_charge: No
author:
- first_name: Jamie
full_name: Rickman, Jamie
last_name: Rickman
- first_name: Christian F
full_name: Düllberg, Christian F
id: 459064DC-F248-11E8-B48F-1D18A9856A87
last_name: Düllberg
orcid: 0000-0001-6335-9748
- first_name: Nicholas
full_name: Cade, Nicholas
last_name: Cade
- first_name: Lewis
full_name: Griffin, Lewis
last_name: Griffin
- first_name: Thomas
full_name: Surrey, Thomas
last_name: Surrey
citation:
ama: Rickman J, Düllberg CF, Cade N, Griffin L, Surrey T. Steady state EB cap size
fluctuations are determined by stochastic microtubule growth and maturation. PNAS.
2017;114(13):3427-3432. doi:10.1073/pnas.1620274114
apa: Rickman, J., Düllberg, C. F., Cade, N., Griffin, L., & Surrey, T. (2017).
Steady state EB cap size fluctuations are determined by stochastic microtubule
growth and maturation. PNAS. National Academy of Sciences. https://doi.org/10.1073/pnas.1620274114
chicago: Rickman, Jamie, Christian F Düllberg, Nicholas Cade, Lewis Griffin, and
Thomas Surrey. “Steady State EB Cap Size Fluctuations Are Determined by Stochastic
Microtubule Growth and Maturation.” PNAS. National Academy of Sciences,
2017. https://doi.org/10.1073/pnas.1620274114.
ieee: J. Rickman, C. F. Düllberg, N. Cade, L. Griffin, and T. Surrey, “Steady state
EB cap size fluctuations are determined by stochastic microtubule growth and maturation,”
PNAS, vol. 114, no. 13. National Academy of Sciences, pp. 3427–3432, 2017.
ista: Rickman J, Düllberg CF, Cade N, Griffin L, Surrey T. 2017. Steady state EB
cap size fluctuations are determined by stochastic microtubule growth and maturation.
PNAS. 114(13), 3427–3432.
mla: Rickman, Jamie, et al. “Steady State EB Cap Size Fluctuations Are Determined
by Stochastic Microtubule Growth and Maturation.” PNAS, vol. 114, no. 13,
National Academy of Sciences, 2017, pp. 3427–32, doi:10.1073/pnas.1620274114.
short: J. Rickman, C.F. Düllberg, N. Cade, L. Griffin, T. Surrey, PNAS 114 (2017)
3427–3432.
date_created: 2018-12-11T11:47:46Z
date_published: 2017-03-28T00:00:00Z
date_updated: 2025-09-11T07:08:20Z
day: '28'
department:
- _id: MaLo
doi: 10.1073/pnas.1620274114
external_id:
isi:
- '000397607300065'
pmid:
- '28280102'
intvolume: ' 114'
isi: 1
issue: '13'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5380103/
month: '03'
oa: 1
oa_version: Submitted Version
page: 3427 - 3432
pmid: 1
publication: PNAS
publication_identifier:
issn:
- 0027-8424
publication_status: published
publisher: National Academy of Sciences
publist_id: '7073'
quality_controlled: '1'
scopus_import: '1'
status: public
title: Steady state EB cap size fluctuations are determined by stochastic microtubule
growth and maturation
type: journal_article
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 114
year: '2017'
...
---
_id: '7360'
abstract:
- lang: eng
text: Inflammation, which is a highly regulated host response against danger signals,
may be harmful if it is excessive and deregulated. Ideally, anti-inflammatory
therapy should autonomously commence as soon as possible after the onset of inflammation,
should be controllable by a physician, and should not systemically block beneficial
immune response in the long term. We describe a genetically encoded anti-inflammatory
mammalian cell device based on a modular engineered genetic circuit comprising
a sensor, an amplifier, a “thresholder” to restrict activation of a positive-feedback
loop, a combination of advanced clinically used biopharmaceutical proteins, and
orthogonal regulatory elements that linked modules into the functional device.
This genetic circuit was autonomously activated by inflammatory signals, including
endogenous cecal ligation and puncture (CLP)-induced inflammation in mice and
serum from a systemic juvenile idiopathic arthritis (sIJA) patient, and could
be reset externally by a chemical signal. The microencapsulated anti-inflammatory
device significantly reduced the pathology in dextran sodium sulfate (DSS)-induced
acute murine colitis, demonstrating a synthetic immunological approach for autonomous
anti-inflammatory therapy.
article_processing_charge: No
article_type: original
author:
- first_name: Anže
full_name: Smole, Anže
last_name: Smole
- first_name: Duško
full_name: Lainšček, Duško
last_name: Lainšček
- first_name: Urban
full_name: Bezeljak, Urban
id: 2A58201A-F248-11E8-B48F-1D18A9856A87
last_name: Bezeljak
orcid: 0000-0003-1365-5631
- first_name: Simon
full_name: Horvat, Simon
last_name: Horvat
- first_name: Roman
full_name: Jerala, Roman
last_name: Jerala
citation:
ama: Smole A, Lainšček D, Bezeljak U, Horvat S, Jerala R. A synthetic mammalian
therapeutic gene circuit for sensing and suppressing inflammation. Molecular
Therapy. 2017;25(1):102-119. doi:10.1016/j.ymthe.2016.10.005
apa: Smole, A., Lainšček, D., Bezeljak, U., Horvat, S., & Jerala, R. (2017).
A synthetic mammalian therapeutic gene circuit for sensing and suppressing inflammation.
Molecular Therapy. Elsevier. https://doi.org/10.1016/j.ymthe.2016.10.005
chicago: Smole, Anže, Duško Lainšček, Urban Bezeljak, Simon Horvat, and Roman Jerala.
“A Synthetic Mammalian Therapeutic Gene Circuit for Sensing and Suppressing Inflammation.”
Molecular Therapy. Elsevier, 2017. https://doi.org/10.1016/j.ymthe.2016.10.005.
ieee: A. Smole, D. Lainšček, U. Bezeljak, S. Horvat, and R. Jerala, “A synthetic
mammalian therapeutic gene circuit for sensing and suppressing inflammation,”
Molecular Therapy, vol. 25, no. 1. Elsevier, pp. 102–119, 2017.
ista: Smole A, Lainšček D, Bezeljak U, Horvat S, Jerala R. 2017. A synthetic mammalian
therapeutic gene circuit for sensing and suppressing inflammation. Molecular Therapy.
25(1), 102–119.
mla: Smole, Anže, et al. “A Synthetic Mammalian Therapeutic Gene Circuit for Sensing
and Suppressing Inflammation.” Molecular Therapy, vol. 25, no. 1, Elsevier,
2017, pp. 102–19, doi:10.1016/j.ymthe.2016.10.005.
short: A. Smole, D. Lainšček, U. Bezeljak, S. Horvat, R. Jerala, Molecular Therapy
25 (2017) 102–119.
date_created: 2020-01-25T15:55:39Z
date_published: 2017-01-01T00:00:00Z
date_updated: 2025-09-18T10:41:35Z
day: '01'
ddc:
- '570'
department:
- _id: MaLo
doi: 10.1016/j.ymthe.2016.10.005
external_id:
isi:
- '000391901600013'
pmid:
- '28129106'
file:
- access_level: open_access
checksum: ea8b1b28606dd1edab7379ba4fa3641f
content_type: application/pdf
creator: dernst
date_created: 2020-03-03T10:55:13Z
date_updated: 2020-07-14T12:47:56Z
file_id: '7561'
file_name: 2017_MolecularTherapy_Smole.pdf
file_size: 3404806
relation: main_file
file_date_updated: 2020-07-14T12:47:56Z
has_accepted_license: '1'
intvolume: ' 25'
isi: 1
issue: '1'
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc-nd/4.0/
month: '01'
oa: 1
oa_version: Published Version
page: 102-119
pmid: 1
publication: Molecular Therapy
publication_identifier:
issn:
- 1525-0016
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: A synthetic mammalian therapeutic gene circuit for sensing and suppressing
inflammation
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: 25
year: '2017'
...
---
OA_place: publisher
OA_type: hybrid
_id: '453'
abstract:
- lang: eng
text: Most kinesin motors move in only one direction along microtubules. Members
of the kinesin-5 subfamily were initially described as unidirectional plus-end-directed
motors and shown to produce piconewton forces. However, some fungal kinesin-5
motors are bidirectional. The force production of a bidirectional kinesin-5 has
not yet been measured. Therefore, it remains unknown whether the mechanism of
the unconventional minus-end-directed motility differs fundamentally from that
of plus-end-directed stepping. Using force spectroscopy, we have measured here
the forces that ensembles of purified budding yeast kinesin-5 Cin8 produce in
microtubule gliding assays in both plus- and minus-end direction. Correlation
analysis of pause forces demonstrated that individual Cin8 molecules produce additive
forces in both directions of movement. In ensembles, Cin8 motors were able to
produce single-motor forces up to a magnitude of ∼1.5 pN. Hence, these properties
appear to be conserved within the kinesin-5 subfamily. Force production was largely
independent of the directionality of movement, indicating similarities between
the motility mechanisms for both directions. These results provide constraints
for the development of models for the bidirectional motility mechanism of fission
yeast kinesin-5 and provide insight into the function of this mitotic motor.
acknowledgement: 'The plasmid for full-length kinesin-1 was a gift from G. Holzwarth
and J. Macosko with permission from J. Howard. We thank I. Lueke and N. I. Cade
for technical assistance. G.P. thanks the Francis Crick Institute, and in particular
the Surrey and Salbreux groups, for their hospitality during his sabbatical stay,
as well as Imperial College London for making it possible. This work was supported
by the Francis Crick Institute, which receives its core funding from Cancer Research
UK (FC001163), the United Kingdom Medical Research Council (FC001163), and the Wellcome
Trust (FC001163), and by Imperial College London. J.R. was also supported by a Sir
Henry Wellcome Postdoctoral Fellowship (100145/Z/12/Z) and T.S. by the European
Research Council (Advanced Grant, project 323042). '
article_processing_charge: No
article_type: original
author:
- first_name: Todd
full_name: Fallesen, Todd
last_name: Fallesen
- first_name: Johanna
full_name: Roostalu, Johanna
last_name: Roostalu
- first_name: Christian F
full_name: Düllberg, Christian F
id: 459064DC-F248-11E8-B48F-1D18A9856A87
last_name: Düllberg
orcid: 0000-0001-6335-9748
- first_name: Gunnar
full_name: Pruessner, Gunnar
last_name: Pruessner
- first_name: Thomas
full_name: Surrey, Thomas
last_name: Surrey
citation:
ama: Fallesen T, Roostalu J, Düllberg CF, Pruessner G, Surrey T. Ensembles of bidirectional
kinesin Cin8 produce additive forces in both directions of movement. Biophysical
Journal. 2017;113(9):2055-2067. doi:10.1016/j.bpj.2017.09.006
apa: Fallesen, T., Roostalu, J., Düllberg, C. F., Pruessner, G., & Surrey, T.
(2017). Ensembles of bidirectional kinesin Cin8 produce additive forces in both
directions of movement. Biophysical Journal. Biophysical Society. https://doi.org/10.1016/j.bpj.2017.09.006
chicago: Fallesen, Todd, Johanna Roostalu, Christian F Düllberg, Gunnar Pruessner,
and Thomas Surrey. “Ensembles of Bidirectional Kinesin Cin8 Produce Additive Forces
in Both Directions of Movement.” Biophysical Journal. Biophysical Society,
2017. https://doi.org/10.1016/j.bpj.2017.09.006.
ieee: T. Fallesen, J. Roostalu, C. F. Düllberg, G. Pruessner, and T. Surrey, “Ensembles
of bidirectional kinesin Cin8 produce additive forces in both directions of movement,”
Biophysical Journal, vol. 113, no. 9. Biophysical Society, pp. 2055–2067,
2017.
ista: Fallesen T, Roostalu J, Düllberg CF, Pruessner G, Surrey T. 2017. Ensembles
of bidirectional kinesin Cin8 produce additive forces in both directions of movement.
Biophysical Journal. 113(9), 2055–2067.
mla: Fallesen, Todd, et al. “Ensembles of Bidirectional Kinesin Cin8 Produce Additive
Forces in Both Directions of Movement.” Biophysical Journal, vol. 113,
no. 9, Biophysical Society, 2017, pp. 2055–67, doi:10.1016/j.bpj.2017.09.006.
short: T. Fallesen, J. Roostalu, C.F. Düllberg, G. Pruessner, T. Surrey, Biophysical
Journal 113 (2017) 2055–2067.
date_created: 2018-12-11T11:46:33Z
date_published: 2017-11-07T00:00:00Z
date_updated: 2025-08-05T14:08:52Z
day: '07'
ddc:
- '570'
department:
- _id: MaLo
doi: 10.1016/j.bpj.2017.09.006
external_id:
pmid:
- '29117528'
file:
- access_level: open_access
checksum: 99a2474088e20ac74b1882c4fbbb45b1
content_type: application/pdf
creator: system
date_created: 2018-12-12T10:14:03Z
date_updated: 2020-07-14T12:46:31Z
file_id: '5052'
file_name: IST-2018-965-v1+1_2017_Duellberg_Ensembles_of.pdf
file_size: 977192
relation: main_file
file_date_updated: 2020-07-14T12:46:31Z
has_accepted_license: '1'
intvolume: ' 113'
issue: '9'
language:
- iso: eng
license: https://creativecommons.org/licenses/by/4.0/
month: '11'
oa: 1
oa_version: Published Version
page: 2055 - 2067
pmid: 1
publication: Biophysical Journal
publication_identifier:
eissn:
- 1542-0086
issn:
- 0006-3495
publication_status: published
publisher: Biophysical Society
publist_id: '7369'
pubrep_id: '965'
quality_controlled: '1'
scopus_import: '1'
status: public
title: Ensembles of bidirectional kinesin Cin8 produce additive forces in both directions
of movement
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: 113
year: '2017'
...
---
_id: '960'
abstract:
- lang: eng
text: The human cerebral cortex is the seat of our cognitive abilities and composed
of an extraordinary number of neurons, organized in six distinct layers. The establishment
of specific morphological and physiological features in individual neurons needs
to be regulated with high precision. Impairments in the sequential developmental
programs instructing corticogenesis lead to alterations in the cortical cytoarchitecture
which is thought to represent the major underlying cause for several neurological
disorders including neurodevelopmental and psychiatric diseases. In this review
we discuss the role of cell polarity at sequential stages during cortex development.
We first provide an overview of morphological cell polarity features in cortical
neural stem cells and newly-born postmitotic neurons. We then synthesize a conceptual
molecular and biochemical framework how cell polarity is established at the cellular
level through a break in symmetry in nascent cortical projection neurons. Lastly
we provide a perspective how the molecular mechanisms applying to single cells
could be probed and integrated in an in vivo and tissue-wide context.
article_number: '176'
article_processing_charge: Yes
author:
- first_name: Andi H
full_name: Hansen, Andi H
id: 38853E16-F248-11E8-B48F-1D18A9856A87
last_name: Hansen
- first_name: Christian F
full_name: Düllberg, Christian F
id: 459064DC-F248-11E8-B48F-1D18A9856A87
last_name: Düllberg
orcid: 0000-0001-6335-9748
- first_name: Christine
full_name: Mieck, Christine
id: 34CAE85C-F248-11E8-B48F-1D18A9856A87
last_name: Mieck
orcid: 0000-0003-1919-7416
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Simon
full_name: Hippenmeyer, Simon
id: 37B36620-F248-11E8-B48F-1D18A9856A87
last_name: Hippenmeyer
orcid: 0000-0003-2279-1061
citation:
ama: Hansen AH, Düllberg CF, Mieck C, Loose M, Hippenmeyer S. Cell polarity in cerebral
cortex development - cellular architecture shaped by biochemical networks. Frontiers
in Cellular Neuroscience. 2017;11. doi:10.3389/fncel.2017.00176
apa: Hansen, A. H., Düllberg, C. F., Mieck, C., Loose, M., & Hippenmeyer, S.
(2017). Cell polarity in cerebral cortex development - cellular architecture shaped
by biochemical networks. Frontiers in Cellular Neuroscience. Frontiers
Research Foundation. https://doi.org/10.3389/fncel.2017.00176
chicago: Hansen, Andi H, Christian F Düllberg, Christine Mieck, Martin Loose, and
Simon Hippenmeyer. “Cell Polarity in Cerebral Cortex Development - Cellular Architecture
Shaped by Biochemical Networks.” Frontiers in Cellular Neuroscience. Frontiers
Research Foundation, 2017. https://doi.org/10.3389/fncel.2017.00176.
ieee: A. H. Hansen, C. F. Düllberg, C. Mieck, M. Loose, and S. Hippenmeyer, “Cell
polarity in cerebral cortex development - cellular architecture shaped by biochemical
networks,” Frontiers in Cellular Neuroscience, vol. 11. Frontiers Research
Foundation, 2017.
ista: Hansen AH, Düllberg CF, Mieck C, Loose M, Hippenmeyer S. 2017. Cell polarity
in cerebral cortex development - cellular architecture shaped by biochemical networks.
Frontiers in Cellular Neuroscience. 11, 176.
mla: Hansen, Andi H., et al. “Cell Polarity in Cerebral Cortex Development - Cellular
Architecture Shaped by Biochemical Networks.” Frontiers in Cellular Neuroscience,
vol. 11, 176, Frontiers Research Foundation, 2017, doi:10.3389/fncel.2017.00176.
short: A.H. Hansen, C.F. Düllberg, C. Mieck, M. Loose, S. Hippenmeyer, Frontiers
in Cellular Neuroscience 11 (2017).
date_created: 2018-12-11T11:49:25Z
date_published: 2017-06-28T00:00:00Z
date_updated: 2026-04-30T22:30:42Z
day: '28'
ddc:
- '570'
department:
- _id: SiHi
- _id: MaLo
doi: 10.3389/fncel.2017.00176
ec_funded: 1
external_id:
isi:
- '000404486700001'
file:
- access_level: open_access
checksum: dc1f5a475b918d09a0f9f587400b1626
content_type: application/pdf
creator: system
date_created: 2018-12-12T10:09:40Z
date_updated: 2020-07-14T12:48:16Z
file_id: '4764'
file_name: IST-2017-830-v1+1_2017_Hansen_CellPolarity.pdf
file_size: 2153858
relation: main_file
file_date_updated: 2020-07-14T12:48:16Z
has_accepted_license: '1'
intvolume: ' 11'
isi: 1
language:
- iso: eng
month: '06'
oa: 1
oa_version: Published Version
project:
- _id: 25D61E48-B435-11E9-9278-68D0E5697425
call_identifier: FP7
grant_number: '618444'
name: Molecular Mechanisms of Cerebral Cortex Development
- _id: 25D7962E-B435-11E9-9278-68D0E5697425
grant_number: RGP0053/2014
name: Quantitative Structure-Function Analysis of Cerebral Cortex Assembly at Clonal
Level
- _id: 25681D80-B435-11E9-9278-68D0E5697425
call_identifier: FP7
grant_number: '291734'
name: International IST Postdoc Fellowship Programme
- _id: 25985A36-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: T00817-B21
name: The biochemical basis of PAR polarization
publication: Frontiers in Cellular Neuroscience
publication_identifier:
issn:
- 1662-5102
publication_status: published
publisher: Frontiers Research Foundation
publist_id: '6445'
pubrep_id: '830'
quality_controlled: '1'
related_material:
record:
- id: '9962'
relation: dissertation_contains
status: public
scopus_import: '1'
status: public
title: Cell polarity in cerebral cortex development - cellular architecture shaped
by biochemical networks
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: 11
year: '2017'
...
---
_id: '1544'
abstract:
- lang: eng
text: 'Cell division in prokaryotes and eukaryotes is commonly initiated by the
well-controlled binding of proteins to the cytoplasmic side of the cell membrane.
However, a precise characterization of the spatiotemporal dynamics of membrane-bound
proteins is often difficult to achieve in vivo. Here, we present protocols for
the use of supported lipid bilayers to rebuild the cytokinetic machineries of
cells with greatly different dimensions: the bacterium Escherichia coli and eggs
of the vertebrate Xenopus laevis. Combined with total internal reflection fluorescence
microscopy, these experimental setups allow for precise quantitative analyses
of membrane-bound proteins. The protocols described to obtain glass-supported
membranes from bacterial and vertebrate lipids can be used as starting points
for other reconstitution experiments. We believe that similar biochemical assays
will be instrumental to study the biochemistry and biophysics underlying a variety
of complex cellular tasks, such as signaling, vesicle trafficking, and cell motility.'
article_processing_charge: No
author:
- first_name: Phuong
full_name: Nguyen, Phuong
last_name: Nguyen
- first_name: Christine
full_name: Field, Christine
last_name: Field
- first_name: Aaron
full_name: Groen, Aaron
last_name: Groen
- first_name: Timothy
full_name: Mitchison, Timothy
last_name: Mitchison
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
citation:
ama: 'Nguyen P, Field C, Groen A, Mitchison T, Loose M. Using supported bilayers
to study the spatiotemporal organization of membrane-bound proteins. In: Building
a Cell from Its Components Parts. Vol 128. Academic Press; 2015:223-241. doi:10.1016/bs.mcb.2015.01.007'
apa: Nguyen, P., Field, C., Groen, A., Mitchison, T., & Loose, M. (2015). Using
supported bilayers to study the spatiotemporal organization of membrane-bound
proteins. In Building a Cell from its Components Parts (Vol. 128, pp. 223–241).
Academic Press. https://doi.org/10.1016/bs.mcb.2015.01.007
chicago: Nguyen, Phuong, Christine Field, Aaron Groen, Timothy Mitchison, and Martin
Loose. “Using Supported Bilayers to Study the Spatiotemporal Organization of Membrane-Bound
Proteins.” In Building a Cell from Its Components Parts, 128:223–41. Academic
Press, 2015. https://doi.org/10.1016/bs.mcb.2015.01.007.
ieee: P. Nguyen, C. Field, A. Groen, T. Mitchison, and M. Loose, “Using supported
bilayers to study the spatiotemporal organization of membrane-bound proteins,”
in Building a Cell from its Components Parts, vol. 128, Academic Press,
2015, pp. 223–241.
ista: 'Nguyen P, Field C, Groen A, Mitchison T, Loose M. 2015.Using supported bilayers
to study the spatiotemporal organization of membrane-bound proteins. In: Building
a Cell from its Components Parts. vol. 128, 223–241.'
mla: Nguyen, Phuong, et al. “Using Supported Bilayers to Study the Spatiotemporal
Organization of Membrane-Bound Proteins.” Building a Cell from Its Components
Parts, vol. 128, Academic Press, 2015, pp. 223–41, doi:10.1016/bs.mcb.2015.01.007.
short: P. Nguyen, C. Field, A. Groen, T. Mitchison, M. Loose, in:, Building a Cell
from Its Components Parts, Academic Press, 2015, pp. 223–241.
corr_author: '1'
date_created: 2018-12-11T11:52:38Z
date_published: 2015-04-08T00:00:00Z
date_updated: 2025-09-29T11:03:06Z
day: '08'
department:
- _id: MaLo
doi: 10.1016/bs.mcb.2015.01.007
external_id:
isi:
- '000370490800013'
pmid:
- '25997350'
intvolume: ' 128'
isi: 1
language:
- iso: eng
main_file_link:
- open_access: '1'
url: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4578691/
month: '04'
oa: 1
oa_version: Submitted Version
page: 223 - 241
pmid: 1
publication: Building a Cell from its Components Parts
publication_status: published
publisher: Academic Press
publist_id: '5627'
quality_controlled: '1'
scopus_import: '1'
status: public
title: Using supported bilayers to study the spatiotemporal organization of membrane-bound
proteins
type: book_chapter
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 128
year: '2015'
...