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The AP-3 adaptor complex is required for vacuolar function in Arabidopsis

Marta Zwiewka UGent, Elena Feraru UGent, Barbara Möller, Inhwan Hwang, Ioan Mugurel Feraru UGent, Jürgen Kleine-Vehn UGent, Dolf Weijers and Jiri Friml UGent (2011) CELL RESEARCH. 21(12). p.1711-1722
abstract
Subcellular trafficking is required for a multitude of functions in eukaryotic cells. It involves regulation of cargo sorting, vesicle formation, trafficking and fusion processes at multiple levels. Adaptor protein (AP) complexes are key regulators of cargo sorting into vesicles in yeast and mammals but their existence and function in plants have not been demonstrated. Here we report the identification of the protein-affected trafficking 4 (pat4) mutant defective in the putative delta subunit of the AP-3 complex. pat4 and pat2, a mutant isolated from the same GFP imaging-based forward genetic screen that lacks a functional putative AP-3 beta, as well as dominant negative AP-3 mu transgenic lines display undistinguishable phenotypes characterized by largely normal morphology and development, but strong intracellular accumulation of membrane proteins in aberrant vacuolar structures. All mutants are defective in morphology and function of lytic and protein storage vacuoles (PSVs) but show normal sorting of reserve proteins to PSVs. Immunoprecipitation experiments and genetic studies revealed tight functional and physical associations of putative AP-3 beta and AP-3 delta subunits. Furthermore, both proteins are closely linked with putative AP-3 mu and sigma subunits and several components of the clathrin and dynamin machineries. Taken together, these results demonstrate that AP complexes, similar to those in other eukaryotes, exist in plants, and that AP-3 plays a specific role in the regulation of biogenesis and function of vacuoles in plant cells.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
vacuole biogenesis and function, AUXIN EFFLUX CARRIER, protein trafficking, PSVs, AP-3 complex, PROTEIN COMPLEX, PREVACUOLAR COMPARTMENT, ENDOCYTIC PATHWAY, VESICLE FORMATION, LYTIC VACUOLES, CELL POLARITY, PLANT-CELLS, TRAFFICKING, CLATHRIN
journal title
CELL RESEARCH
Cell Res.
volume
21
issue
12
pages
1711 - 1722
Web of Science type
Article
Web of Science id
000298156000011
JCR category
CELL BIOLOGY
JCR impact factor
8.19 (2011)
JCR rank
23/178 (2011)
JCR quartile
1 (2011)
ISSN
1001-0602
DOI
10.1038/cr.2011.99
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
1995985
handle
http://hdl.handle.net/1854/LU-1995985
date created
2012-01-19 10:44:13
date last changed
2012-02-10 11:38:47
@article{1995985,
  abstract     = {Subcellular trafficking is required for a multitude of functions in eukaryotic cells. It involves regulation of cargo sorting, vesicle formation, trafficking and fusion processes at multiple levels. Adaptor protein (AP) complexes are key regulators of cargo sorting into vesicles in yeast and mammals but their existence and function in plants have not been demonstrated. Here we report the identification of the protein-affected trafficking 4 (pat4) mutant defective in the putative delta subunit of the AP-3 complex. pat4 and pat2, a mutant isolated from the same GFP imaging-based forward genetic screen that lacks a functional putative AP-3 beta, as well as dominant negative AP-3 mu transgenic lines display undistinguishable phenotypes characterized by largely normal morphology and development, but strong intracellular accumulation of membrane proteins in aberrant vacuolar structures. All mutants are defective in morphology and function of lytic and protein storage vacuoles (PSVs) but show normal sorting of reserve proteins to PSVs. Immunoprecipitation experiments and genetic studies revealed tight functional and physical associations of putative AP-3 beta and AP-3 delta subunits. Furthermore, both proteins are closely linked with putative AP-3 mu and sigma subunits and several components of the clathrin and dynamin machineries. Taken together, these results demonstrate that AP complexes, similar to those in other eukaryotes, exist in plants, and that AP-3 plays a specific role in the regulation of biogenesis and function of vacuoles in plant cells.},
  author       = {Zwiewka, Marta and Feraru, Elena and M{\"o}ller, Barbara and Hwang, Inhwan and Feraru, Ioan Mugurel and Kleine-Vehn, J{\"u}rgen and Weijers, Dolf and Friml, Jiri},
  issn         = {1001-0602},
  journal      = {CELL RESEARCH},
  keyword      = {vacuole biogenesis and function,AUXIN EFFLUX CARRIER,protein trafficking,PSVs,AP-3 complex,PROTEIN COMPLEX,PREVACUOLAR COMPARTMENT,ENDOCYTIC PATHWAY,VESICLE FORMATION,LYTIC VACUOLES,CELL POLARITY,PLANT-CELLS,TRAFFICKING,CLATHRIN},
  language     = {eng},
  number       = {12},
  pages        = {1711--1722},
  title        = {The AP-3 adaptor complex is required for vacuolar function in Arabidopsis},
  url          = {http://dx.doi.org/10.1038/cr.2011.99},
  volume       = {21},
  year         = {2011},
}

Chicago
Zwiewka, Marta, Elena Feraru, Barbara Möller, Inhwan Hwang, Ioan Mugurel Feraru, Jürgen Kleine-Vehn, Dolf Weijers, and Jiri Friml. 2011. “The AP-3 Adaptor Complex Is Required for Vacuolar Function in Arabidopsis.” Cell Research 21 (12): 1711–1722.
APA
Zwiewka, M., Feraru, E., Möller, B., Hwang, I., Feraru, I. M., Kleine-Vehn, J., Weijers, D., et al. (2011). The AP-3 adaptor complex is required for vacuolar function in Arabidopsis. CELL RESEARCH, 21(12), 1711–1722.
Vancouver
1.
Zwiewka M, Feraru E, Möller B, Hwang I, Feraru IM, Kleine-Vehn J, et al. The AP-3 adaptor complex is required for vacuolar function in Arabidopsis. CELL RESEARCH. 2011;21(12):1711–22.
MLA
Zwiewka, Marta, Elena Feraru, Barbara Möller, et al. “The AP-3 Adaptor Complex Is Required for Vacuolar Function in Arabidopsis.” CELL RESEARCH 21.12 (2011): 1711–1722. Print.