FEBS Lett. 2002 May 22;519(1-3):178-80.

An EVH1/WH1 domain as a key actor in TGFbeta signalling.

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Systèmes Moléculaires and Biologie Structurale, LMCP, CNRS UMR 7590, Universités Paris 6 and Paris 7, Case 115, 4 place Jussieu, Paris, France. isabelle.callebaut@lmcp.jussieu.fr

Abstract

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.

PMID:: 12023040; [PubMed - indexed for MEDLINE]

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The WH1 and EVH1 domains of WASP and Ena/VASP family members bind distinct sequence motifs. [Curr Biol. 2002]
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An EVH1/WH1 domain as a key actor in TGFbeta signalling.
An EVH1/WH1 domain as a key actor in TGFbeta signalling.
FEBS Lett. 2002 May 22 ;519(1-3):178-80.

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