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Adaptin-like protein TPLATE and clathrin recruitment during plant somatic cytokinesis occurs via two distinct pathways

Daniël Van Damme UGent, Astrid Gadeyne UGent, Marleen Vanstraelen UGent, Dirk Inzé UGent, Marc Van Montagu UGent, Geert De Jaeger UGent, Eugenia Russinova UGent and Danny Geelen UGent (2011) PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 108(2). p.615-620
abstract
Plant cytokinesis deploys a transport system that centers cell plate-forming vesicles and fuses them to form a cell plate. Here we show that the adaptin-like protein TPLATE and clathrin light chain 2 (CLC2) are targeted to the expanding cell plate and to the equatorial subregion of the plasma membrane referred to as the cortical division zone (CDZ). Bimolecular fluorescence complementation and immunodetection indicates that TPLATE interacts with clathrin. Pharmacological tools as well as analysis of protein targeting in a mutant background affecting cell plate formation allowed to discriminate two recruitment pathways for TPLATE and CLC2. The cell plate recruitment pathway is dependent on phragmoplast microtubule organization and the formation and transport of secretory vesicles. The CDZ recruitment pathway, on the other hand, is activated at the end of cytokinesis and independent of trans-Golgi-derived vesicle trafficking. TPLATE and CLC2 do not accumulate at a narrow zone central of the CDZ. We have dubbed this subdomain the cortical division site and show that it corresponds precisely with the position where the cell plate merges with the parental wall. These data provide evidence that the plasma membrane is subject to localized endocytosis or membrane remodeling processes that are required for the fusion of the cell plate with a predefined region of the plasma membrane.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
tyrphostin, caffeine, plant cell divison, clathrin-mediated endocytosis, Adaptin
journal title
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Proc. Natl. Acad. Sci. U. S. A.
volume
108
issue
2
pages
615 - 620
Web of Science type
Article
Web of Science id
000286097700037
JCR category
MULTIDISCIPLINARY SCIENCES
JCR impact factor
9.681 (2011)
JCR rank
3/54 (2011)
JCR quartile
1 (2011)
ISSN
0027-8424
DOI
10.1073/pnas.1017890108
project
Biotechnology for a sustainable economy (Bio-Economy)
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
1209182
handle
http://hdl.handle.net/1854/LU-1209182
date created
2011-04-14 18:19:20
date last changed
2013-02-27 12:05:19
@article{1209182,
  abstract     = {Plant cytokinesis deploys a transport system that centers cell plate-forming vesicles and fuses them to form a cell plate. Here we show that the adaptin-like protein TPLATE and clathrin light chain 2 (CLC2) are targeted to the expanding cell plate and to the equatorial subregion of the plasma membrane referred to as the cortical division zone (CDZ). Bimolecular fluorescence complementation and immunodetection indicates that TPLATE interacts with clathrin. Pharmacological tools as well as analysis of protein targeting in a mutant background affecting cell plate formation allowed to discriminate two recruitment pathways for TPLATE and CLC2. The cell plate recruitment pathway is dependent on phragmoplast microtubule organization and the formation and transport of secretory vesicles. The CDZ recruitment pathway, on the other hand, is activated at the end of cytokinesis and independent of trans-Golgi-derived vesicle trafficking. TPLATE and CLC2 do not accumulate at a narrow zone central of the CDZ. We have dubbed this subdomain the cortical division site and show that it corresponds precisely with the position where the cell plate merges with the parental wall. These data provide evidence that the plasma membrane is subject to localized endocytosis or membrane remodeling processes that are required for the fusion of the cell plate with a predefined region of the plasma membrane.},
  author       = {Van Damme, Dani{\"e}l and Gadeyne, Astrid and Vanstraelen, Marleen and Inz{\'e}, Dirk and Van Montagu, Marc and De Jaeger, Geert and Russinova, Eugenia and Geelen, Danny},
  issn         = {0027-8424},
  journal      = {PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA},
  keyword      = {tyrphostin,caffeine,plant cell divison,clathrin-mediated endocytosis,Adaptin},
  language     = {eng},
  number       = {2},
  pages        = {615--620},
  title        = {Adaptin-like protein TPLATE and clathrin recruitment during plant somatic cytokinesis occurs via two distinct pathways},
  url          = {http://dx.doi.org/10.1073/pnas.1017890108},
  volume       = {108},
  year         = {2011},
}

Chicago
Van Damme, Daniël, Astrid Gadeyne, Marleen Vanstraelen, Dirk Inzé, Marc Van Montagu, Geert De Jaeger, Eugenia Russinova, and Danny Geelen. 2011. “Adaptin-like Protein TPLATE and Clathrin Recruitment During Plant Somatic Cytokinesis Occurs via Two Distinct Pathways.” Proceedings of the National Academy of Sciences of the United States of America 108 (2): 615–620.
APA
Van Damme, Daniël, Gadeyne, A., Vanstraelen, M., Inzé, D., Van Montagu, M., De Jaeger, G., Russinova, E., et al. (2011). Adaptin-like protein TPLATE and clathrin recruitment during plant somatic cytokinesis occurs via two distinct pathways. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 108(2), 615–620.
Vancouver
1.
Van Damme D, Gadeyne A, Vanstraelen M, Inzé D, Van Montagu M, De Jaeger G, et al. Adaptin-like protein TPLATE and clathrin recruitment during plant somatic cytokinesis occurs via two distinct pathways. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 2011;108(2):615–20.
MLA
Van Damme, Daniël, Astrid Gadeyne, Marleen Vanstraelen, et al. “Adaptin-like Protein TPLATE and Clathrin Recruitment During Plant Somatic Cytokinesis Occurs via Two Distinct Pathways.” PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 108.2 (2011): 615–620. Print.