EpsinR: an AP1/clathrin interacting protein involved in vesicle trafficking

被引：196

作者：

Mills, IG ^{[1
]}

Praefcke, GJK ^{[1
]}

Vallis, Y ^{[1
]}

Peter, BJ ^{[1
]}

Olesen, LE ^{[1
]}

Gallop, JL ^{[1
]}

Butler, PJG ^{[1
]}

Evans, PR ^{[1
]}

McMahon, HT ^{[1
]}

机构：

[1] MRC, Mol Biol Lab, Cambridge CB2 2QH, England

来源：

JOURNAL OF CELL BIOLOGY | 2003年 / 160卷 / 02期

关键词：

epsin; GGA; TGN; endocytosis; ENTH;

D O I：

10.1083/jcb.200208023

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

EpsinR is a clathrin-coated vesicle (CCV) enriched 70-kD protein that binds to phosphaticlylinositol-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 muM, 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.

引用

页码：213 / 222

页数：10

共 41 条

[1] RECONSTITUTION OF THE TRANSPORT OF PROTEIN BETWEEN SUCCESSIVE COMPARTMENTS OF THE GOLGI MEASURED BY THE COUPLED INCORPORATION OF N-ACETYLGLUCOSAMINE [J].