细丝蛋白（ABP-280）的磷酸化作用调节其与脂膜、整合素及肌动蛋白的结合。

Phosphorylation of filamin (ABP-280) regulates the binding to the lipid membrane, integrin, and actin.

作者信息

Goldmann W H

机构信息

Department of Pathology, Children's Hospital, Harvard Medical School, Boston, MA 02115, USA.

出版信息

Cell Biol Int. 2001;25(8):805-8. doi: 10.1006/cbir.2000.0710.

DOI:10.1006/cbir.2000.0710

PMID:11482904

Abstract

Actin-binding protein (ABP-280; filamin) is a phosphoprotein present in the periphery of the cytoplasm, where it can cross-link actin filaments, associate with lipid membranes, and bind to membrane surface receptors. Given its function and localization in the cell, the hypothesis that it serves as a substrate for p56lck, a lymphocyte-specific member of the src family of protein tyrosine kinases associated with cell surface glycoproteins is considered. The results suggest conformationally-induced regulation of filamin (ABP-280).

摘要

肌动蛋白结合蛋白（ABP - 280；细丝蛋白）是一种磷蛋白，存在于细胞质周边，在那里它可以交联肌动蛋白丝、与脂质膜结合并与膜表面受体结合。鉴于其在细胞中的功能和定位，有人提出假说，认为它是p56lck的底物，p56lck是src家族蛋白酪氨酸激酶的淋巴细胞特异性成员，与细胞表面糖蛋白相关。结果提示细丝蛋白（ABP - 280）存在构象诱导调节。