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帽蛋白:对机制与调控的新见解

Capping protein: new insights into mechanism and regulation.

作者信息

Wear Martin A, Cooper John A

机构信息

Department of Cell Biology and Physiology, Washington University School of Medicine, St Louis, MI 63110, USA.

出版信息

Trends Biochem Sci. 2004 Aug;29(8):418-28. doi: 10.1016/j.tibs.2004.06.003.

Abstract

Temporal and spatial control of the actin cytoskeleton are crucial for a range of eukaryotic cellular processes. Capping protein (CP), a ubiquitous highly conserved heterodimer, tightly caps the barbed (fast-growing) end of the actin filament and is an important component in the assembly of various actin structures, including the dynamic branched filament network at the leading edge of motile cells. New research into the molecular mechanism of how CP interacts with the actin filament in vitro and the function of CP in vivo, including discoveries of novel interactions of CP with other proteins, has greatly enhanced our understanding of the role of CP in regulating the actin cytoskeleton.

摘要

肌动蛋白细胞骨架的时空控制对于一系列真核细胞过程至关重要。帽蛋白(CP)是一种普遍存在的高度保守异二聚体,紧密封闭肌动蛋白丝的带刺(快速生长)末端,是各种肌动蛋白结构组装的重要组成部分,包括运动细胞前缘的动态分支丝网络。关于CP在体外如何与肌动蛋白丝相互作用以及CP在体内功能的分子机制的新研究,包括CP与其他蛋白质新相互作用的发现,极大地增进了我们对CP在调节肌动蛋白细胞骨架中作用的理解。

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