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An EVH1/WH1 domain as a key actor in TGFβ signalling

被引：15
作者：
Callebaut, I
机构：
[1] Univ Paris 06, CNRS UMR 7590, LMCP, F-75252 Paris 05, France
[2] Univ Paris 07, CNRS UMR 7590, LMCP, F-75252 Paris 05, France
来源：
FEBS LETTERS | 2002年 / 519卷 / 1-3期
关键词：
SMIF; Smad4; sequence analysis; PSI-BLAST; hydrophobic cluster analysis;
D O I：
10.1016/S0014-5793(02)02751-5
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：
EVH1 (enabled VASP (vasodilator-stimulated protein) homology 1)/WH1 (WASP (Wiskott-Aldrich syndrome protein) homology 1) domains, present in Ena VASP and WASP, are protein interaction modules specialised in binding proline-rich ligands. An EVH1/WH1 domain is here identified in the recently cloned SMIF protein, a key protein in transforming growth factor-beta (TGFbeta) signalling which was not yet related to defined domains. The SMIF EVH1/WH1 domain interacts with the proline-rich Smad4 activation domain, leading to translocation of so-formed complex to the nucleus where SMIF possesses strong intrinsic TGFbeta-inducible transcriptional activity. This finding highlights the pivotal role that the EVH1/WH1 family of domains play in multiple eukaryotic signal transduction pathways. (C) 2002 Federation of European Biochemical Societies. Published by Else-tier Science B.V. All rights reserved.
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页码：178 / 180
页数：3
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