Abstract
We describe a novel protein that contains a verprolin-homology (V) region, through which several actin-regulating proteins, including Wiskott-Aldrich syndrome protein (WASP) family members, bind directly to actin. The amino acid sequence is homologous to the sequences of WASP-interacting protein (WIP) and CR16, both of which associate with WASP and/or N-WASP, and thus these three proteins constitute a new protein family. We named the protein WICH (WIP- and CR16-homologous protein). WICH associates strongly with N-WASP but only weakly with WASP via its C-terminal WASP-interacting (W) region. Ectopic expression of WICH induces actin-microspike formation through cooperation with N-WASP. In addition, expression of the W fragment of WICH suppresses microspike formation induced by N-WASP, indicating an essential role for WICH in N-WASP-induced microspike formation.
©2002 Elsevier Science (USA).
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Actins / metabolism*
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Blotting, Western
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Carrier Proteins / genetics
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Cloning, Molecular
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Cytoskeletal Proteins
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Fungal Proteins / genetics*
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Humans
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Intracellular Signaling Peptides and Proteins
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Microfilament Proteins / chemistry
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Microfilament Proteins / genetics*
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Microfilament Proteins / metabolism*
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Molecular Sequence Data
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Nerve Tissue Proteins / genetics
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Nerve Tissue Proteins / metabolism*
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Organ Specificity
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Phosphoproteins*
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Protein Binding
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Protein Structure, Tertiary / genetics
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Pseudopodia / metabolism*
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RNA, Messenger / biosynthesis
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Saccharomyces cerevisiae Proteins*
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Sequence Analysis, DNA
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Sequence Homology, Amino Acid
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Wiskott-Aldrich Syndrome Protein, Neuronal
Substances
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Actins
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Carrier Proteins
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Cytoskeletal Proteins
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Fungal Proteins
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Intracellular Signaling Peptides and Proteins
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Microfilament Proteins
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Nerve Tissue Proteins
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Phosphoproteins
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RNA, Messenger
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Saccharomyces cerevisiae Proteins
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VRP1 protein, S cerevisiae
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WASL protein, human
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WIPF1 protein, human
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WIPF2 protein, human
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Wipf1 protein, rat
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Wipf3 protein, rat
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Wiskott-Aldrich Syndrome Protein, Neuronal