The ENTH domain

被引：120

作者：

De Camilli, P

Chen, H

Hyman, J

Panepucci, E

Bateman, A

Brunger, AT

机构：

[1] Yale Univ, Sch Med, Howard Hughes Med Inst, New Haven, CT 06510 USA

[2] Yale Univ, Sch Med, Dept Cell Biol, New Haven, CT 06510 USA

[3] Stanford Univ, Dept Mol & Cellular Physiol, Stanford, CA 94305 USA

[4] Stanford Univ, Dept Neurol & Neurol Sci, Stanford, CA 94305 USA

[5] Stanford Univ, Stanford Synchrotron Radiat Lab, Stanford, CA 94305 USA

[6] Sanger Ctr, Cambridge CB10 1SA, England

来源：

FEBS LETTERS | 2002年 / 513卷 / 01期

关键词：

VHS domain; ubiquitin; clathrin; AP-2; endocytosis; EH domain;

D O I：

10.1016/S0014-5793(01)03306-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The epsin NH2-terminal homology (ENTH) domain is a membrane interacting module composed by a superhelix of alpha-helices. It is present at the NH2-terminus of proteins that often contain consensus sequences for binding to clathrin coat components and their accessory factors, and therefore function as endocytic adaptors. ENTH domain containing proteins have additional roles in signaling and actin regulation and may have yet other actions in the nucleus. The ENTH domain is structurally similar to the VIIS domain. These domains define two families of adaptor proteins which function in membrane traffic and whose interaction with membranes is regulated, in part, by phosphoinositides. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：11 / 18

页数：8

共 79 条

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