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PMID: 2122258 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review

The GTPase superfamily: a conserved switch for diverse cell functions.

Nature ·Vol. 348 ·No. 6297 ·1990-11-08 ·Pages 125-32

Bourne HR, Sanders DA, McCormick F

Abstract

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.

MeSH Terms
Animals Biological Transport Cysteine/physiology Endocytosis Exocytosis GTP Phosphohydrolase-Linked Elongation Factors/physiology GTP-Binding Proteins/physiology Guanosine Triphosphate/physiology Humans Neurofibromatosis 1/physiopathology Peptide Elongation Factors/physiology Peptide Initiation Factors/physiology Pheromones/physiology Protein Processing, Post-Translational Proto-Oncogene Proteins p21(ras)/physiology Saccharomyces cerevisiae/physiology Signal Transduction
Chemicals
Peptide Elongation Factors Peptide Initiation Factors Pheromones Guanosine Triphosphate GTP Phosphohydrolase-Linked Elongation Factors GTP-Binding Proteins HRAS protein, human Proto-Oncogene Proteins p21(ras) Cysteine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Bourne H R
Department of Pharmacology, University of California, San Francisco 94143.
Sanders D A
McCormick F
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
DOI
10.1038/348125a0
Published
1990-11-08
Pages
125-32
Language
English
Region
England
NLM ID
0410462
Subset
IM
External Links
PubMed source DOI: 10.1038/348125a0 View journal details
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