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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >WIP, a protein associated with Wiskott-Aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cells
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WIP, a protein associated with Wiskott-Aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cells

机译:WIP是一种与Wiskott-Aldrich综合征蛋白相关的蛋白,可诱导肌动蛋白聚合并在淋巴样细胞中重新分布

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摘要

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.
机译: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,并以造血细胞的细胞骨架异常为特征。通过使用酵母双杂交系统,我们鉴定了富含脯氨酸的WASP相互作用蛋白(WIP),该蛋白与淋巴细胞中的WASP共免疫沉淀。 WIP在与Cdc42结合位点不同的位点与WASP结合,并具有肌动蛋白和蛋白原结合蛋白。 WIP在人B细胞中的表达,但不是缺少肌动蛋白结合基序的WIP截断突变体,不会增加聚合肌动蛋白的含量,并诱导细胞表面上含肌动蛋白的脑形突起的出现。这些结果表明,WIP在可能对淋巴细胞功能重要的皮质肌动蛋白组装中发挥作用。

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