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Publication Detail
Keeping G proteins at bay: a complex between G protein-coupled receptor kinase 2 and Gbetagamma.
  • Publication Type:
    Journal article
  • Publication Sub Type:
  • Authors:
    Lodowski DT, Pitcher JA, Capel WD, Lefkowitz RJ, Tesmer JJ
  • Publisher:
    American Association for the Advancement of Science
  • Publication date:
  • Pagination:
    1256, 1262
  • Journal:
  • Volume:
  • Issue:
  • Print ISSN:
  • Addresses:
    Institute for Cellular and Molecular Biology, Department of Chemistry and Biochemistry, University of Texas at Austin, Austin, TX 78712, USA.
The phosphorylation of heptahelical receptors by heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptor kinases (GRKs) is a universal regulatory mechanism that leads to desensitization of G protein signaling and to the activation of alternative signaling pathways.We determined the crystallographic structure of bovine GRK2 in complex with G protein beta1gamma2 subunits.Our results show how the three domains of GRK2-the RGS (regulator of G protein signaling) homology, protein kinase, and pleckstrin homology domains-integrate their respective activities and recruit the enzyme to the cell membrane in an orientation that not only facilitates receptor phosphorylation, but also allows for the simultaneous inhibition of signaling by Galpha and Gbetagamma subunits.
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