The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
WIP, a protein associated with Wiskott–Aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cells
Open accessAbstract
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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Metadata
- Authors
- Ramesh, N., Antón, I. M., Hartwig, J. H., & Geha, R. S.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1997-12-23
- Volume
- 94
- Issue
- 26
- Pages
- 14671-14676
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2113249117
- Cited by
- 373
- References
- 26
- FWCI
- 9.03
- Type
- journal article
- Language
- en
- Open access
- green
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- Ramesh, N., Antón, I. M., Hartwig, J. H., & Geha, R. S. (1997). WIP, a protein associated with Wiskott–Aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cells. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.94.26.14671
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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