WIP, a protein associated with wiskott-aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cells.

Wiskott-Aldrich syndrome (WAS) is an X-linked immunodeficiency caused by mutations that affect the WAS protein (WASP) and characterized by cytoskeletal abnormalities in hematopoietic cells. By using the yeast two-hybrid system we have identified a proline-rich WASP-interacting protein (WIP), which coimmunoprecipitated with WASP from lymphocytes. WIP binds to WASP at a ...
site distinct from the Cdc42 binding site and has actin as well as profilin binding motifs. Expression of WIP in human B cells, but not of a WIP truncation mutant that lacks the actin binding motif, increased polymerized actin content and induced the appearance of actin-containing cerebriform projections on the cell surface. These results suggest that WIP plays a role in cortical actin assembly that may be important for lymphocyte function.
Mesh Terms:
Actins, Amino Acid Sequence, Carrier Proteins, Cells, Cultured, Cytoskeletal Proteins, Dimerization, Humans, Intracellular Signaling Peptides and Proteins, Lymphocytes, Molecular Sequence Data, Proteins, Wiskott-Aldrich Syndrome, Wiskott-Aldrich Syndrome Protein
Proc. Natl. Acad. Sci. U.S.A.
Date: Dec. 23, 1997
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