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

FEBS Letters

Callebaut, Isabelle¹ 

[1] Systèmes Moléculaires and Biologie Structurale, LMCP, CNRS UMR 7590, Universités Paris 6 and Paris 7, Case 115, 4 place Jussieu, 75252 Paris cedex 05, France

关键词: SMIF;    Smad4;    Sequence analysis;    PSI-BLAST;    Hydrophobic cluster analysis;    BMP;    bone morphogenetic protein;    VASP;    vasodilator-stimulated protein;    EVH1;    enabled VASP homology 1;    TGFβ;    transforming growth factor-β;    SIF1;    still life protein type 1;    WASP;    Wiskott–Aldrich syndrome protein;    WH1;    WASP homology 1;    HCA;    hydrophobic cluster analysis;   

DOI  :  10.1016/S0014-5793(02)02751-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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-β (TGFβ) 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 TGFβ-inducible transcriptional activity. This finding highlights the pivotal role that the EVH1/WH1 family of domains play in multiple eukaryotic signal transduction pathways.

【 授权许可】

Unknown