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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Biological Factors / genetics
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Biological Factors / physiology*
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Cell Adhesion Molecules / genetics
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Cluster Analysis
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Computational Biology
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Conserved Sequence
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Drosophila melanogaster
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Humans
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Ligands
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Mice
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Microfilament Proteins
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Models, Molecular
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Molecular Sequence Data
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Phosphoproteins / genetics
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Protein Binding
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Protein Structure, Tertiary / physiology
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Proteins / genetics
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Rats
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Saccharomyces cerevisiae
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Sequence Alignment
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Sequence Homology, Amino Acid
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Signal Transduction / physiology*
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Transforming Growth Factor beta / physiology*
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Wiskott-Aldrich Syndrome Protein
Substances
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Biological Factors
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Cell Adhesion Molecules
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Ligands
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Microfilament Proteins
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Phosphoproteins
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Proteins
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Transforming Growth Factor beta
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WAS protein, human
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Was protein, mouse
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Was protein, rat
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Wiskott-Aldrich Syndrome Protein
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vasodilator-stimulated phosphoprotein
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smooth muscle inhibitory factor