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WIP, a Protein Associated with Wiskott-Aldrich Syndrome Protein, Induces Actin Polymerization and Redistribution in Lymphoid Cells

Narayanaswamy Ramesh, Ines M. Anton, John H. Hartwig and Raif S. Geha
Proceedings of the National Academy of Sciences of the United States of America
Vol. 94, No. 26 (Dec. 23, 1997), pp. 14671-14676
Stable URL: http://www.jstor.org/stable/43676
Page Count: 6
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
WIP, a Protein Associated with Wiskott-Aldrich Syndrome Protein, Induces Actin Polymerization and Redistribution in Lymphoid Cells
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Abstract

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.

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