The AP-3 adaptor complex is required for vacuolar function in Arabidopsis
- Author
- Marta Zwiewka (UGent) , Elena Feraru (UGent) , Barbara Möller, Inhwan Hwang, Ioan Mugurel Feraru (UGent) , Jürgen Kleine-Vehn (UGent) , Dolf Weijers and Jiri Friml (UGent)
- Organization
- 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.
- Keywords
- 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
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Citation
Please use this url to cite or link to this publication: http://hdl.handle.net/1854/LU-1995985
- MLA
- Zwiewka, Marta, et al. “The AP-3 Adaptor Complex Is Required for Vacuolar Function in Arabidopsis.” CELL RESEARCH, vol. 21, no. 12, 2011, pp. 1711–22, doi:10.1038/cr.2011.99.
- APA
- Zwiewka, M., Feraru, E., Möller, B., Hwang, I., Feraru, I. M., Kleine-Vehn, J., … Friml, J. (2011). The AP-3 adaptor complex is required for vacuolar function in Arabidopsis. CELL RESEARCH, 21(12), 1711–1722. https://doi.org/10.1038/cr.2011.99
- Chicago author-date
- 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): 1711–22. https://doi.org/10.1038/cr.2011.99.
- Chicago author-date (all authors)
- 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. doi:10.1038/cr.2011.99.
- 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.
- IEEE
- [1]M. Zwiewka et al., “The AP-3 adaptor complex is required for vacuolar function in Arabidopsis,” CELL RESEARCH, vol. 21, no. 12, pp. 1711–1722, 2011.
@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 Möller, Barbara and Hwang, Inhwan and Feraru, Ioan Mugurel and Kleine-Vehn, Jürgen and Weijers, Dolf and Friml, Jiri}},
issn = {{1001-0602}},
journal = {{CELL RESEARCH}},
keywords = {{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://doi.org/10.1038/cr.2011.99}},
volume = {{21}},
year = {{2011}},
}
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