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膜联蛋白II四聚体:结构与功能

Annexin II tetramer: structure and function.

作者信息

Waisman D M

机构信息

Department of Medical Biochemistry, Faculty of Medicine, University of Calgary, Alberta, Canada.

出版信息

Mol Cell Biochem. 1995 Aug-Sep;149-150:301-22. doi: 10.1007/BF01076592.

Abstract

The annexins are a family of proteins that bind acidic phospholipids in the presence of Ca2+. The interaction of these proteins with biological membranes has led to the suggestion that these proteins may play a role in membrane trafficking events such as exocytosis, endocytosis and cell-cell adhesion. One member of the annexin family, annexin II, has been shown to exist as a monomer, heterodimer or heterotetramer. The ability of annexin II tetramer to bridge secretory granules to plasma membrane has suggested that this protein may play a role in Ca(2+)-dependent exocytosis. Annexin II tetramer has also been demonstrated on the extracellular face of some metastatic cells where it mediates the binding of certain metastatic cells to normal cells. Annexin II tetramer is a major cellular substrate of protein kinase C and pp60src. Phosphorylation of annexin II tetramer is a negative modulator of protein function.

摘要

膜联蛋白是一类在Ca2+存在下能结合酸性磷脂的蛋白质家族。这些蛋白质与生物膜的相互作用表明,它们可能在诸如胞吐作用、胞吞作用和细胞间黏附等膜运输事件中发挥作用。膜联蛋白家族的一个成员,膜联蛋白II,已被证明以单体、异二聚体或异四聚体的形式存在。膜联蛋白II四聚体将分泌颗粒与质膜连接起来的能力表明,这种蛋白质可能在Ca(2+)依赖的胞吐作用中发挥作用。在一些转移细胞的细胞外表面也发现了膜联蛋白II四聚体,它介导某些转移细胞与正常细胞的结合。膜联蛋白II四聚体是蛋白激酶C和pp60src的主要细胞底物。膜联蛋白II四聚体的磷酸化是蛋白质功能的负调节剂。

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