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Human substance P receptor undergoes agonist‐dependent phosphorylation by G protein‐coupled receptor kinase 5 in vitro
Author(s) -
Warabi Kengo,
Richardson Mark D.,
Barry William T.,
Yamaguchi Keisuke,
Roush Eric D.,
Nishimura Kinya,
Kwatra Madan M.
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02858-2
Subject(s) - g protein coupled receptor kinase , phosphorylation , agonist , chemistry , receptor , g protein coupled receptor , kinase , biochemistry , beta adrenergic receptor kinase , arrestin , microbiology and biotechnology , biology
G protein‐coupled receptor kinases (GRKs) phosphorylate agonist‐occupied G protein‐coupled receptors, leading to receptor desensitization. Seven GRKs, designated GRK1 through 7, have been characterized. GRK5 is negatively regulated by protein kinase C. We investigated whether human substance P receptor (hSPR) is a substrate of GRK5. We report that membrane‐bound hSPR is phosphorylated by purified GRK5, and that both the rate and extent of phosphorylation increase dramatically in the presence of substance P. The phosphorylation has a high stoichiometry (20±4 mol phosphate/mol hSPR) and a low K m (1.7±0.1 nM). These data provide the first evidence that hSPR is a substrate of GRK5.