Journal
SCIENCE
Volume 300, Issue 5623, Pages 1256-1262Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1082348
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- NHLBI NIH HHS [HL16037] Funding Source: Medline
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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 beta(1)gamma(2) 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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