Characterization of the GRK2 binding site of Galphaq.

@article{Day2004CharacterizationOT,
  title={Characterization of the GRK2 binding site of Galphaq.},
  author={Peter W. Day and John J G Tesmer and Rachel Sterne-Marr and Leslie C Freeman and Jeffrey L. Benovic and Philip B. Wedegaertner},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 51},
  pages={
          53643-52
        }
}
Heterotrimeric guanine nucleotide-binding proteins (G proteins) transmit signals from membrane bound G protein-coupled receptors (GPCRs) to intracellular effector proteins. The G(q) subfamily of Galpha subunits couples GPCR activation to the enzymatic activity of phospholipase C-beta (PLC-beta). Regulators of G protein signaling (RGS) proteins bind to activated Galpha subunits, including Galpha(q), and regulate Galpha signaling by acting as GTPase activating proteins (GAPs), increasing the rate… CONTINUE READING
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