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Yeast epsin-related proteins required for Golgi-endosome traffic define a gamma-adaptin ear-binding motif.

Abstract：

:Clathrin-coated vesicles (CCVs) are a central component of endocytosis and traffic between the trans-Golgi network (TGN) and endosomes. Although endocytic CCV formation is well characterized, much less is known about CCV formation at internal membranes. Here we describe two epsin amino-terminal homology (ENTH) domain-containing proteins, Ent3p and Ent5p, that are intimately involved in clathrin function at the Golgi. Both proteins associate with the clathrin adaptor Gga2p in vivo; Ent5p also interacts with the clathrin adaptor complex AP-1 and clathrin. A novel, conserved motif that mediates the interaction of Ent3p and Ent5p with gamma-ear domains of Gga2p and AP-1 is defined. Ent3p and Ent5p colocalize with clathrin, and cells lacking both Ent proteins exhibit defects in clathrin localization and traffic between the Golgi and endosomes. The findings suggest that Ent3p and Ent5p constitute a functionally related pair that co-operate with Gga proteins and AP-1 to recruit clathrin and promote formation of clathrin coats at the Golgi/endosomes. On the basis of our results and the established roles of epsin and epsin-related proteins in endocytosis, we propose that ENTH-domain-containing proteins are a universal component of CCV formation.

journal_name

Nat Cell Biol

journal_title

Nature cell biology

authors

Duncan MC,Costaguta G,Payne GS

doi

10.1038/ncb901

keywords:

subject

Has Abstract

pub_date

2003-01-01 00:00:00

pages

77-81

issue

1

eissn

1465-7392

issn

1476-4679

pii

ncb901

journal_volume

5

pub_type

杂志文章

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