The GTPase superfamily: a conserved switch for diverse cell functions
Open Access
- 8 November 1990
- journal article
- review article
- Published by Springer Nature in Nature
- Vol. 348 (6297) , 125-132
- https://doi.org/10.1038/348125a0
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.Keywords
This publication has 123 references indexed in Scilit:
- S. cerevisiae genes IRA1 and IRA2 encode proteins that may be functionally equivalent to mammalian ras GTPase activating proteinCell, 1990
- How does the nose know?Cell, 1990
- A novel membrane factor stimulates guanine nucleotide exchange reaction of ras proteinsFEBS Letters, 1990
- The GTP-binding protein Ypt1 is required for transport in vitro: the Golgi apparatus is defective in ypt1 mutants.The Journal of cell biology, 1989
- Reconstitution of protein transport from the endoplasmic reticulum to the Golgi complex in yeast: the acceptor Golgi compartment is defective in the sec23 mutant.The Journal of cell biology, 1988
- A GTP-binding protein required for secretion rapidly associates with secretory vesicles and the plasma membrane in yeastCell, 1988
- Study of a temperature-sensitive mutant of the ras-related YPT1 gene product in yeast suggests a role in the regulation of intracellular calciumCell, 1988
- Topology of signal recognition particle receptor in endoplasmic reticulum membraneNature, 1985
- Differential activation of yeast adenylate cyclase by wild type and mutant RAS proteinsCell, 1985
- The role of guanosine 5′-triphosphate in polypeptide chain elongationBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1978