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桩蛋白、黏着斑激酶和p130CAS的酪氨酸磷酸化:对细胞铺展和迁移的影响。

Tyrosine phosphorylation of paxillin, FAK, and p130CAS: effects on cell spreading and migration.

作者信息

Panetti Tracee S

机构信息

Department of Microbiology and Immunology and Thrombosis Research Center, Temple University School of Medicine, Philadelphia, PA 19140, USA.

出版信息

Front Biosci. 2002 Jan 1;7:d143-50. doi: 10.2741/A771.

DOI:10.2741/A771
PMID:11779709
Abstract

Integrins are transmembrane receptors that mediate cell attachment to the substrate. At the cytoplasmic surface of the integrin, cytoskeletal proteins cluster into focal adhesions. The focal adhesions contain multiple proteins that provide a structural and signaling complex inside the cell. This review focuses on three of the cytoskeletal components of the focal adhesion, paxillin, FAK, and p130CAS, that are phosphorylated and play a regulatory role in cell spreading and cell migration. A brief discussion is included of tyrosine phosphorylation of the integrin in relation to localization and phosphorylation of these cytoskeletal proteins. The phosphorylation of integrins and cytoskeletal proteins regulates localization and downstream signaling with profound effects on cell movement.

摘要

整合素是介导细胞与底物附着的跨膜受体。在整合素的细胞质表面,细胞骨架蛋白聚集成粘着斑。粘着斑包含多种蛋白质,这些蛋白质在细胞内提供结构和信号复合体。本综述聚焦于粘着斑的三种细胞骨架成分,桩蛋白、粘着斑激酶和p130CAS,它们会发生磷酸化并在细胞铺展和细胞迁移中发挥调节作用。文中还简要讨论了整合素的酪氨酸磷酸化与这些细胞骨架蛋白的定位和磷酸化的关系。整合素和细胞骨架蛋白的磷酸化调节定位和下游信号传导,对细胞运动产生深远影响。

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