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Published 21 January 2003. doi:10.1083/jcb.200208023
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© The Rockefeller University Press, 0021-9525/2003/1/213 $5.00
The Journal of Cell Biology, Volume 160, Number 2, 213-222

Article

EpsinR

: an AP1/clathrin interacting protein involved in vesicle trafficking



Ian G. Mills, Gerrit J.K. Praefcke, Yvonne Vallis, Brian J. Peter, Lene E. Olesen, Jennifer L. Gallop, P. Jonathan G. Butler, Philip R. Evans and Harvey T. McMahon

Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 2QH, UK

Address correspondence to Harvey T. McMahon, MRC Laboratory of Molecular Biology, Hills Rd., Cambridge CB2 2QH, UK. Tel.: 44-1223-402311. Fax: 44-1223-402310. E-mail: hmm{at}mrc-lmb.cam.ac.uk

EpsinR is a clathrin-coated vesicle (CCV) enriched 70-kD protein that binds to phosphatidylinositol-4-phosphate, clathrin, and the gamma appendage domain of the adaptor protein complex 1 (AP1). In cells, its distribution overlaps with the perinuclear pool of clathrin and AP1 adaptors. Overexpression disrupts the CCV-dependent trafficking of cathepsin D from the trans-Golgi network to lysosomes and the incorporation of mannose-6-phosphate receptors into CCVs. These biochemical and cell biological data point to a role for epsinR in AP1/clathrin budding events in the cell, just as epsin1 is involved in the budding of AP2 CCVs. Furthermore, we show that two gamma appendage domains can simultaneously bind to epsinR with affinities of 0.7 and 45 µM, respectively. Thus, potentially, two AP1 complexes can bind to one epsinR. This high affinity binding allowed us to identify a consensus binding motif of the form DFxDF, which we also find in {gamma}-synergin and use to predict that an uncharacterized EF-hand–containing protein will be a new gamma binding partner.

Key Words: epsin; GGA; TGN; endocytosis; ENTH


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