THE GTPASE SUPERFAMILY - A CONSERVED SWITCH FOR DIVERSE CELL FUNCTIONS

被引：2089

作者：

BOURNE, HR

SANDERS, DA

MCCORMICK, F

机构：

[1] UNIV CALIF SAN FRANCISCO, DEPT MED, SAN FRANCISCO, CA 94143 USA

[2] UNIV CALIF SAN FRANCISCO, CARDIOVASC RES INST, SAN FRANCISCO, CA 94143 USA

[3] CETUS CORP, DEPT MOLEC BIOL, EMERYVILLE, CA 94608 USA

来源：

NATURE | 1990年 / 348卷 / 6297期

关键词：

D O I：

10.1038/348125a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Proteins that bind and hydrolyse GTP are being discovered at a rapidly increasing rate. Each of these many GTPases acts as a molecular switch whose 'on' and 'off' states are triggered by binding and hydrolysis of GTP. Conserved structure and mechanism in myriad versions of the switch - in bacteria, yeast, flies and vertebrates - suggest that all derive from a single primordial protein, repeatedly modified in the course of evolution to perform a dazzling variety of functions. © 1990 Nature Publishing Group.

引用

页码：125 / 132

页数：8

共 129 条

[1]

ARAKI S, 1990, J BIOL CHEM, V265, P13007

[2]

BACKLUND PS, 1988, J BIOL CHEM, V263, P15864

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