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Differential degradation of PIN2 auxin efflux carrier by retromer-dependent vacuolar targeting

Jürgen Kleine-Vehn UGent, Johannes Leitner, Marta Zwiewka UGent, Michael Sauer, Lindy Abas, Christian Luschnig and Jiri Friml UGent (2008) PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 105(46). p.17812-17817
abstract
All eukaryotic cells present at the cell surface a specific set of plasma membrane proteins that modulate responses to internal and external cues and whose activity is also regulated by protein degradation. We characterized the lytic vacuole-dependent degradation of membrane proteins in Arabidopsis thaliana by means of in vivo visualization of vacuolar targeting combined with quantitative protein analysis. We show that the vacuolar targeting pathway is used by multiple cargos including PIN-FORMED (PIN) efflux carriers for the phytohormone auxin. In vivo visualization of PIN2 vacuolar targeting revealed its differential degradation in response to environmental signals, such as gravity. In contrast to polar PIN delivery to the basal plasma membrane, which depends on the vesicle trafficking regulator ARF-GEF GNOM, PIN sorting to the lytic vacuolar pathway requires additional brefeldin A-sensitive ARF-GEF activity. Furthermore, we identified putative retromer components SORTING NEXIN1 (SNX1) and VACUOLAR PROTEIN SORTING29 (VPS29) as important factors in this pathway and propose that the retromer complex acts to retrieve PIN proteins from a late/pre-vacuolar compartment back to the recycling pathways. Our data suggest that ARF GEF- and retromer-dependent processes regulate PIN sorting to the vacuole in an antagonistic manner and illustrate instrumentalization of this mechanism for fine-tuning the auxin fluxes during gravitropic response.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
CELL POLARITY, PLANT DEVELOPMENT, ARABIDOPSIS-THALIANA, PREVACUOLAR COMPARTMENT, posttranslational regulation, vesicle trafficking, gravitropism, polar auxin transport, TRANSPORT, RECEPTOR KINASE, PROTEINS, TRAFFICKING, FLOW, GRADIENTS
journal title
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Proc. Natl. Acad. Sci. USA
volume
105
issue
46
pages
17812 - 17817
Web of Science type
Article
Web of Science id
000261225600045
ISSN
0027-8424
DOI
10.1073/pnas.0808073105
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
509304
handle
http://hdl.handle.net/1854/LU-509304
date created
2009-02-27 14:36:05
date last changed
2012-12-06 16:13:32
@article{509304,
  abstract     = {All eukaryotic cells present at the cell surface a specific set of plasma membrane proteins that modulate responses to internal and external cues and whose activity is also regulated by protein degradation. We characterized the lytic vacuole-dependent degradation of membrane proteins in Arabidopsis thaliana by means of in vivo visualization of vacuolar targeting combined with quantitative protein analysis. We show that the vacuolar targeting pathway is used by multiple cargos including PIN-FORMED (PIN) efflux carriers for the phytohormone auxin. In vivo visualization of PIN2 vacuolar targeting revealed its differential degradation in response to environmental signals, such as gravity. In contrast to polar PIN delivery to the basal plasma membrane, which depends on the vesicle trafficking regulator ARF-GEF GNOM, PIN sorting to the lytic vacuolar pathway requires additional brefeldin A-sensitive ARF-GEF activity. Furthermore, we identified putative retromer components SORTING NEXIN1 (SNX1) and VACUOLAR PROTEIN SORTING29 (VPS29) as important factors in this pathway and propose that the retromer complex acts to retrieve PIN proteins from a late/pre-vacuolar compartment back to the recycling pathways. Our data suggest that ARF GEF- and retromer-dependent processes regulate PIN sorting to the vacuole in an antagonistic manner and illustrate instrumentalization of this mechanism for fine-tuning the auxin fluxes during gravitropic response.},
  author       = {Kleine-Vehn, J{\"u}rgen and Leitner, Johannes and Zwiewka, Marta and Sauer, Michael and Abas, Lindy and Luschnig, Christian and Friml, Jiri},
  issn         = {0027-8424},
  journal      = {PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA},
  keyword      = {CELL POLARITY,PLANT DEVELOPMENT,ARABIDOPSIS-THALIANA,PREVACUOLAR COMPARTMENT,posttranslational regulation,vesicle trafficking,gravitropism,polar auxin transport,TRANSPORT,RECEPTOR KINASE,PROTEINS,TRAFFICKING,FLOW,GRADIENTS},
  language     = {eng},
  number       = {46},
  pages        = {17812--17817},
  title        = {Differential degradation of PIN2 auxin efflux carrier by retromer-dependent vacuolar targeting},
  url          = {http://dx.doi.org/10.1073/pnas.0808073105},
  volume       = {105},
  year         = {2008},
}

Chicago
Kleine-Vehn, Jürgen, Johannes Leitner, Marta Zwiewka, Michael Sauer, Lindy Abas, Christian Luschnig, and Jiri Friml. 2008. “Differential Degradation of PIN2 Auxin Efflux Carrier by Retromer-dependent Vacuolar Targeting.” Proceedings of the National Academy of Sciences of the United States of America 105 (46): 17812–17817.
APA
Kleine-Vehn, J., Leitner, J., Zwiewka, M., Sauer, M., Abas, L., Luschnig, C., & Friml, J. (2008). Differential degradation of PIN2 auxin efflux carrier by retromer-dependent vacuolar targeting. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 105(46), 17812–17817.
Vancouver
1.
Kleine-Vehn J, Leitner J, Zwiewka M, Sauer M, Abas L, Luschnig C, et al. Differential degradation of PIN2 auxin efflux carrier by retromer-dependent vacuolar targeting. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 2008;105(46):17812–7.
MLA
Kleine-Vehn, Jürgen, Johannes Leitner, Marta Zwiewka, et al. “Differential Degradation of PIN2 Auxin Efflux Carrier by Retromer-dependent Vacuolar Targeting.” PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 105.46 (2008): 17812–17817. Print.