PMID- 19004783
OWN - NLM
STAT- MEDLINE
DCOM- 20081217
LR  - 20211020
IS  - 1091-6490 (Electronic)
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 105
IP  - 46
DP  - 2008 Nov 18
TI  - Differential degradation of PIN2 auxin efflux carrier by retromer-dependent 
      vacuolar targeting.
PG  - 17812-7
LID - 10.1073/pnas.0808073105 [doi]
AB  - 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.
FAU - Kleine-Vehn, Jurgen
AU  - Kleine-Vehn J
AD  - Department of Plant Systems Biology, Flanders Institute for Biotechnology, 
      Technologiepark 927, 9052 Ghent, Belgium.
FAU - Leitner, Johannes
AU  - Leitner J
FAU - Zwiewka, Marta
AU  - Zwiewka M
FAU - Sauer, Michael
AU  - Sauer M
FAU - Abas, Lindy
AU  - Abas L
FAU - Luschnig, Christian
AU  - Luschnig C
FAU - Friml, Jiri
AU  - Friml J
LA  - eng
GR  - P 19585/FWF_/Austrian Science Fund FWF/Austria
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20081112
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Arabidopsis Proteins)
RN  - 0 (Guanine Nucleotide Exchange Factors)
RN  - 0 (Indoleacetic Acids)
RN  - 0 (Mag1 protein, Arabidopsis)
RN  - 0 (PIN2 protein, Arabidopsis)
RN  - 0 (Phosphatidylinositols)
RN  - 0 (Vesicular Transport Proteins)
RN  - EC 3.6.5.2 (ADP-Ribosylation Factors)
SB  - IM
MH  - ADP-Ribosylation Factors/metabolism
MH  - Arabidopsis/cytology/growth & development/*metabolism
MH  - Arabidopsis Proteins/*metabolism
MH  - Cell Membrane/metabolism
MH  - Gravitropism
MH  - Guanine Nucleotide Exchange Factors/metabolism
MH  - Indoleacetic Acids/*metabolism
MH  - Mutation/genetics
MH  - Phenotype
MH  - Phosphatidylinositols/metabolism
MH  - *Protein Processing, Post-Translational
MH  - Protein Transport
MH  - Time Factors
MH  - Vacuoles/*metabolism
MH  - Vesicular Transport Proteins/metabolism
PMC - PMC2584678
COIS- The authors declare no conflict of interest.
EDAT- 2008/11/14 09:00
MHDA- 2008/12/18 09:00
PMCR- 2009/05/18
CRDT- 2008/11/14 09:00
PHST- 2008/11/14 09:00 [pubmed]
PHST- 2008/12/18 09:00 [medline]
PHST- 2008/11/14 09:00 [entrez]
PHST- 2009/05/18 00:00 [pmc-release]
AID - 0808073105 [pii]
AID - 5454 [pii]
AID - 10.1073/pnas.0808073105 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 2008 Nov 18;105(46):17812-7. doi: 
      10.1073/pnas.0808073105. Epub 2008 Nov 12.