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Biochem Biophys Res Commun. 2015 Jan 2;456(1):238-44. doi: 10.1016/j.bbrc.2014.11.065. Epub 2014 Nov 22.

Arabidopsis dynamin-related proteins, DRP2A and DRP2B, function coordinately in post-Golgi trafficking.

Author information

1
Laboratory of Plant Molecular Genetics, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
2
Plant Global Education Project, Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan.
3
Laboratory of Plant Molecular Genetics, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan; Japan Science and Technology Agency (JST), PRESTO, 4-1-8 Honcho, Kawaguchi, Saitama 332-0012, Japan.
4
Laboratory of Plant Molecular Genetics, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan; Japan Science and Technology Agency (JST), CREST, 4-1-8 Honcho, Kawaguchi, Saitama 332-0012, Japan. Electronic address: atsutsu@mail.ecc.u-tokyo.ac.jp.

Abstract

Dynamin-related proteins (DRPs) are large GTPases involved in a wide range of cellular membrane remodeling processes. In Arabidopsis thaliana, two paralogous land plant-specific type DRPs, DRP2A and DRP2B, are thought to participate in the regulation of post-Golgi trafficking. Here, we examined their molecular properties and functional relationships. qRT-PCR and GUS assays showed that DRP2A and DRP2B were expressed ubiquitously, although their expressions were strongest around root apical meristems and vascular bundles. Yeast two-hybrid, bi-molecular fluorescent complementation, and co-immunoprecipitation mass spectrometry analyses revealed that DRP2A and DRP2B interacted with each other. In observations with confocal laser scanning microscopy and variable incidence angle fluorescent microscopy, fluorescent fusions of DRP2A and DRP2B almost completely co-localized and were mainly localized to endocytic vesicle formation sites of the plasma membrane, clathrin-enriched trans-Golgi network and the cell plate in root epidermal cells. Treatments with wortmannin, an inhibitor of phosphatidylinositol 3-/4-kinases, latrunculin B, an inhibitor of actin polymerization, and oryzalin, an inhibitor of microtubule polymerization, increased the resident time of DRP2A and DRP2B on the plasma membrane. These results show that DRP2A and DRP2B function coordinately in multiple pathways of post-Golgi trafficking in phosphatidylinositol 3- or 4-kinase and cytoskeleton polymerization-dependent manners.

KEYWORDS:

Arabidopsis; DRP2; Dynamin-related protein; Post-Golgi trafficking

PMID:
25462567
DOI:
10.1016/j.bbrc.2014.11.065
[Indexed for MEDLINE]

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