The GTPase superfamily: a conserved switch for diverse cell functions

Nature. 1990 Nov 8;348(6297):125-32. doi: 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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

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*

Substances

  • 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