膜联蛋白1通过蛋白质核心结构域与质膜驻留及内化的表皮生长因子受体特异性结合。

Specific association of annexin 1 with plasma membrane-resident and internalized EGF receptors mediated through the protein core domain.

作者信息

Radke Susanne, Austermann Judith, Russo-Marie Francoise, Gerke Volker, Rescher Ursula

机构信息

Institute for Medical Biochemistry, Centre for Molecular Biology of Inflammation, ZMBE, IZKF Münster, University of Münster, von-Esmarch-Str. 56, 48149 Münster, Germany.

出版信息

FEBS Lett. 2004 Dec 3;578(1-2):95-8. doi: 10.1016/j.febslet.2004.10.078.

DOI:10.1016/j.febslet.2004.10.078

PMID:15581623

Abstract

Phosphorylation of the Ca2+ and membrane-binding protein annexin 1 by epidermal growth factor (EGF) receptor tyrosine kinase has been thought to be involved in regulation of the EGF receptor trafficking. To elucidate the interaction of annexin 1 during EGF receptor internalization, we followed the distribution of annexin 1-GFP fusion proteins at sites of internalizing EGF receptors. The observed association of annexin 1 with EGF receptors was confirmed by immunoprecipitation. We found that this interaction was independent of a functional phosphorylation site in the annexin 1 N-terminal domain but mediated through the Ca2+ binding core domain.

摘要

表皮生长因子（EGF）受体酪氨酸激酶对钙离子和膜结合蛋白膜联蛋白1的磷酸化作用，被认为参与了EGF受体运输的调控。为了阐明膜联蛋白1在EGF受体内化过程中的相互作用，我们追踪了膜联蛋白1-绿色荧光蛋白（GFP）融合蛋白在EGF受体内化位点的分布情况。通过免疫沉淀证实了观察到的膜联蛋白1与EGF受体的关联。我们发现这种相互作用不依赖于膜联蛋白1 N端结构域中的功能性磷酸化位点，而是通过钙离子结合核心结构域介导的。