WIP, a protein associated with Wiskott-Aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cells
WIP, a protein associated with Wiskott-Aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cells
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DOI：
10.1073/pnas.94.26.14671
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发表时间：
1997-12-23
影响因子：
11.1
通讯作者：
Geha, RS
中科院分区：
文献类型：
--
作者：
Ramesh, N;Ant贸n, IM;Geha, RS
Wiskott-Aldrich综合征（WAS）是一种X-连锁免疫缺陷，由影响WAS蛋白（WASP）的突变引起，其特征是造血细胞中的细胞骨架异常。通过酵母双杂交系统，我们已经确定了一个富含脯氨酸的WASP相互作用蛋白（WASP），它与淋巴细胞的WASP免疫共沉淀。WASP在不同于Cdc 42结合位点的位点结合，并且具有肌动蛋白以及profilin结合基序。在人类B细胞中，但不是在一个没有肌动蛋白结合基序的α-肌动蛋白截短突变体的表达，增加了聚合肌动蛋白含量，并诱导细胞表面出现含肌动蛋白的脑状突起。这些结果表明，在皮质肌动蛋白组装，可能是重要的淋巴细胞功能，发挥了作用。
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.