Plant Physiology Preview
Published on February 2, 2007; 10.1104/pp.106.095349
OPEN ACCESS ARTICLE
Received December 29, 2006
Accepted January 18, 2007
EpsinR2 Interacts with Clathrin, AP-3, AtVTI12, and PtdIns(3)P. Implications for EpsinR2 Function in Protein Trafficking in Plant Cells
Gil-Je Lee , Hyeran Kim , Hyangju Kang , Meehee Jang , Dong Wook Lee , Sookjin Lee , and Inhwan Hwang *
Division of Molecules and Life Sciences and Center for Plant Intracellular Trafficking, Pohang University of Science and Technology, Pohang, 790-784, Korea
* Corresponding author; email: ihhwang{at}postech.ac.kr.
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 cells. Plant cells also contain multiple epsin-related proteins. In 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-phosphate (PtdIns(3)P) in vitro, and has a critical role in the targeting of EpsinR2. Upon transient expression in protoplasts, hemagglutinin (HA) epitope-tagged EpsinR2 (HA: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 homologues of adaptor protein (AP)-3  -adaptin and AP-2  -adaptin. Localization experiments revealed that HA:EpsinR2 co-localizes primarily with -adaptin, and partially co-localizes with clathrin and AtVTI12. Based on these findings, we propose that EpsinR2 plays an important role in protein trafficking through interactions with -adaptin, AtVTI12, clathrin, and PtdIns(3)P.
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