Function and interactions of the Ysc84/SH3yl1 family of actin- and lipid-binding proteins.
Function and interactions of the Ysc84/SH3yl1 family of actin- and lipid-binding proteins.
复制标题
肌动蛋白和脂质结合蛋白 Ysc84/SH3yl1 家族的功能和相互作用。
DOI：
10.1042/bst20140221
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发表时间：
2015
影响因子：
3.9
通讯作者：
Urbanek AN
中科院分区：
文献类型：
--
作者：
Urbanek AN
了解肌动蛋白丝是如何在细胞膜附近成核、聚合和分解的是一个越来越感兴趣的领域。质膜的突起是细胞运动所必需的，而向内弯曲或内陷是细胞内吞所必需的。这些膜的形态变化通常与肌动蛋白的重排有关，但真核生物的许多肌动蛋白结合蛋白如何以协调的方式发挥作用以产生所需的反应仍然没有很好的理解。鉴定和分析在质膜和肌动蛋白调节网络之间的界面处起作用的蛋白质是增加我们对肌动蛋白聚合力与膜形态变化之间关系的机制的认识的核心。Ysc 84/SH 3 yl 1蛋白尚未被广泛研究，但在酵母和哺乳动物细胞中的工作表明，这些蛋白在整合丝状肌动蛋白（F-肌动蛋白）的调节与膜形态变化的网络中心发挥作用。
Understanding how actin filaments are nucleated, polymerized and disassembled in close proximity to cell membranes is an area of growing interest. Protrusion of the plasma membrane is required for cell motility, whereas inward curvature or invagination is required for endocytic events. These morphological changes in membrane are often associated with rearrangements of actin, but how the many actin-binding proteins of eukaryotes function in a co-ordinated way to generate the required responses is still not well understood. Identification and analysis of proteins that function at the interface between the plasma membrane and actin-regulatory networks is central to increasing our knowledge of the mechanisms required to transduce the force of actin polymerization to changes in membrane morphology. The Ysc84/SH3yl1 proteins have not been extensively studied, but work in both yeast and mammalian cells indicate that these proteins function at the hub of networks integrating regulation of filamentous actin (F-actin) with changes in membrane morphology.
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影响因子：
3.3
作者：
Dewar, H;Warren, DT;Ayscough, KR
通讯作者：
Ayscough, KR
影响因子：
64.8
作者：
Uetz, P;Giot, L;Rothberg, JM
通讯作者：
Rothberg, JM
影响因子：
3.3
作者：
Robertson, Alastair S.;Allwood, Ellen G.;Ayscough, Kathryn R.
通讯作者：
Ayscough, Kathryn R.
DOI：
10.1083/jcb.201005141
发表时间：
2010-08-09
期刊：
The Journal of cell biology
影响因子：
--
作者：
Hiramoto-Yamaki N;Takeuchi S;Ueda S;Harada K;Fujimoto S;Negishi M;Katoh H
通讯作者：
Katoh H