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EpsinR2 Interacts with Clathrin, Adaptor Protein-3, AtVTI12, and Phosphatidylinositol-3-Phosphate. Implications for EpsinR2 Function in Protein Trafficking in Plant Cells
Gil-Je Lee, Hyeran Kim, Hyangju Kang, Mihue Jang, Dong Wook Lee, Sookjin Lee and Inhwan Hwang
Vol. 143, No. 4 (Apr., 2007), pp. 1561-1575
Published by: American Society of Plant Biologists (ASPB)
Stable URL: http://www.jstor.org/stable/40065372
Page Count: 15
You can always find the topics here!Topics: Proteins, Plant cells, Protoplasts, Antibodies, Endocytosis, Golgi apparatus, Yeasts, Vacuoles, Western blotting, Cell membranes
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Members of the epsin family of proteins (epsins) are characterized by the presence of an epsin N-terminal homology (ENTH) domain. Epsins have been implicated in various protein-trafficking pathways in animal and yeast (Saccharomyces cerevisiae) cells. Plant cells also contain multiple epsin-related proteins. In Arabidopsis (Arabidopsis thaliana), EPSIN1 is involved in vacuolar trafficking of soluble proteins. In this study, we investigated the role of Arabidopsis EpsinR2 in protein trafficking in plant cells. EpsinR2 contains a highly conserved ENTH domain but a fairly divergent C-terminal sequence. We found that the N-terminal ENTH domain specifically binds to phosphatidylinositol-3-P in vitro and has a critical role in the targeting of EpsinR2. Upon transient expression in protoplasts, hemagglutinin epitope-tagged EpsinR2 was translocated primarily to a novel cellular compartment, while a minor portion localized to the Golgi complex. Protein-binding experiments showed that EpsinR2 interacts with clathrin, AtVTI12, and the Arabidopsis homologs of adaptor protein-3 δ-adaptin and adaptor protein-2 α-adaptin. Localization experiments revealed that hemagglutinin epitope-tagged EpsinR2 colocalizes primarily with δ-adaptin and partially colocalizes with clathrin and AtVTI12. Based on these findings, we propose that EpsinR2 plays an important role in protein trafficking through interactions with δ-adaptin, AtVTI12, clathrin, and phosphatidylinositol-3-P.
Plant Physiology © 2007 American Society of Plant Biologists (ASPB)