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异戊二烯化的类Ras GTP酶的膜结合与靶向定位

Membrane association and targeting of prenylated Ras-like GTPases.

作者信息

Seabra M C

机构信息

Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas 75235, USA.

出版信息

Cell Signal. 1998 Mar;10(3):167-72. doi: 10.1016/s0898-6568(97)00120-4.

Abstract

The regulatory function of the Ras-like GTPases in diverse cellular processes, such as growth, cell movement, and protein trafficking, is critically dependent on targeting to the proper cellular membrane. Prenylation of Ras, Rho/Rac, and Rab GTPases, defined as the covalent addition of isoprenyl groups to cysteine residues near or at their carboxyl terminus, is the first and necessary step that leads to membrane binding and targeting of these proteins. Recent progress on the molecular mechanisms of prenylation, membrane association, and targeting of Ras, Rho/Rac, and Rab proteins will be reviewed here. The detailed understanding of these targeting mechanisms may allow future development of specific therapeutic agents that interfere with the function of each one of these proteins.

摘要

类Ras GTP酶在多种细胞过程(如生长、细胞运动和蛋白质运输)中的调节功能,严重依赖于定位于适当的细胞膜。Ras、Rho/Rac和Rab GTP酶的异戊二烯化,定义为在其羧基末端附近或末端的半胱氨酸残基上共价添加异戊二烯基团,是导致这些蛋白质膜结合和定位的第一步也是必要步骤。本文将综述Ras、Rho/Rac和Rab蛋白异戊二烯化、膜结合和定位的分子机制的最新进展。对这些定位机制的详细了解可能有助于未来开发干扰这些蛋白质各自功能的特异性治疗药物。

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