Journal
SCIENCE
Volume 310, Issue 5754, Pages 1686-1690Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1118890
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Funding
- NHLBI NIH HHS [HL071818] Funding Source: Medline
- NIA NIH HHS [AG006093] Funding Source: Medline
- NIGMS NIH HHS [GM61454] Funding Source: Medline
- NINDS NIH HHS [NS41441] Funding Source: Medline
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G protein-coupled receptor kinase 2 (GRK2) plays a key role in the desensitization of G protein-coupled receptor signaling by phosphorylating activated heptahelical receptors and by sequestering heterotrimeric G proteins. We report the atomic structure of GRK2 in complex with G alpha(q) and G beta gamma, in which the activated G alpha subunit of G(q) is fully dissociated from G beta gamma and dramatically reoriented from its position in the inactive G alpha beta gamma heterotrimer. G alpha(q) forms an effector-like interaction with the GRK2 regulator of G protein signaling (RGS) homology domain that is distinct from and does not overlap with that used to bind RGS proteins such as RGS4.
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