The ENTH domain

被引：119

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

[1] Regulation of nucleocytoplasmic trafficking by cell adhesion receptors and the cytoskeleton
Aplin, AE
Juliano, RL
[J]. JOURNAL OF CELL BIOLOGY, 2001, 155 (02) : 187 - 191
[2] Hrs-2 regulates receptor-mediated endocytosis via interactions with Eps15
Bean, AJ
Davanger, S
Chou, MF
Gerhardt, B
Tsujimoto, S
Chang, YC
[J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (20) : 15271 - 15278
[3] Adaptins - The final recount
Boehm, M
Bonifacino, JS
[J]. MOLECULAR BIOLOGY OF THE CELL, 2001, 12 (10) : 2907 - 2920
[4] Cadavid ALM, 2000, DEVELOPMENT, V127, P1727
[5] Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis
Chen, H
Fre, S
Slepnev, VI
Capua, MR
Takei, K
Butler, MH
Di Fiore, PP
De Camilli, P
[J]. NATURE, 1998, 394 (6695) : 793 - 797
[6] The interaction of epsin and Eps15 with the clathrin adaptor AP-2 is inhibited by mitotic phosphorylation and enhanced by stimulation-dependent dephosphorylation in nerve terminals
Chen, H
Slepnev, VI
Di Fiore, PP
De Camilli, P
[J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (06) : 3257 - 3260
[7] Structure of the nuclear transport complex karyopherin-β2-Ran•GppNHp
Chook, YM
Blobel, G
[J]. NATURE, 1999, 399 (6733) : 230 - 237
[8] Structure of importin-β bound to tbe IBB domain of importin-α
Cingolani, G
Petosa, C
Weis, K
Müller, CW
[J]. NATURE, 1999, 399 (6733) : 221 - 229
[9] The Eps15 homology (EH) domain
Confalonieri, S
Di Fiore, PP
[J]. FEBS LETTERS, 2002, 513 (01) : 24 - 29
[10] Novel protein kinases Ark1p and Prk1p associate with and regulate the cortical actin cytoskeleton in budding yeast
Cope, MJTV
Yang, S
Shang, C
Drubin, DG
[J]. JOURNAL OF CELL BIOLOGY, 1999, 144 (06) : 1203 - 1218

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