RGS9-1 phosphorylation and Ca2+

Adv Exp Med Biol. 2002:514:125-9. doi: 10.1007/978-1-4615-0121-3_8.

Abstract

The duration of photoresponses in vertebrate rods and cones is controlled at the level of GTP hydrolysis by a GTPase accelerating protein (GAP) whose catalytic core is provided by RGS9-1. RGS9-1 is in turn regulated by phosphorylation on serine 475, in a reaction that is dependent on Ca2+. In living mice, the level of phosphorylation at this site is reduced by light. Thus RGS9-1 phosphorylation provides a potential mechanism by which light-regulated changes in intracellular [Ca2+] may feed back on phototransduction through effects on the lifetime of activated G protein and cGMP phosphodiesterase.

Publication types

  • Review

MeSH terms

  • Animals
  • Calcium / metabolism*
  • Guanosine Triphosphate / metabolism
  • Humans
  • Hydrolysis
  • Kinetics
  • Light
  • Models, Biological
  • Phosphorylation
  • Protein Structure, Tertiary
  • RGS Proteins / chemistry
  • RGS Proteins / metabolism*
  • Signal Transduction

Substances

  • RGS Proteins
  • regulator of g-protein signaling 9
  • Guanosine Triphosphate
  • Calcium