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The G protein-coupled receptor kinases (GRKs) phosphorylate agonist occupied G protein-coupled receptors (GPCR) and desensitize GPCR-mediated signaling.A proteomic approach was used to screen interacting proteins of GRK in MDA-MB-231 cells and HUVEC cells, and reveals several proteins in the GRK immunocomplex including damaged DNA-binding protein 1 (DDB1), an adaptor subunit of E3 ubiquitin ligase complex.We further found that the depletion of DDB1 decreased Hsp90 inhibitor-induced and UV irradiation-induced GRK degradation.Thus, our study identified potential GRK interacting proteins and revealed the regulation of GRK level by DDB1 containing ubiquitin ligase complex-dependent proteolysis pathway.