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GRK6 — PDGFRB

Text-mined interactions from Literome

Hildreth et al., J Biol Chem 2004 : To determine whether GRK2 regulates the PDGFRbeta in physiologic systems, we examined PDGFRbeta signaling in mouse embryonic fibroblasts from GRK2-null and cognate wild type mice ... This effect was reproduced by S1104D mutation of the PDGFRbeta, which also diminished PDGFRbeta activation and signaling ( like the S1104A mutation ) to an extent equivalent to that achieved by GRK2 mediated PDGFRbeta phosphorylation ... We conclude that GRK2 mediated PDGFRbeta seryl phosphorylation plays an important role in desensitizing the PDGFRbeta in physiologic systems
Wu et al., J Biol Chem 2005 : This PDGFRbeta mediated GRK2 tyrosyl phosphorylation enhanced GRK2 activity : GRK2 mediated seryl phosphorylation of the PDGFRbeta was 9-fold greater for the WT than for the Y857F in response to PDGF, but equivalent when GRK2 was activated by sequential stimulation of beta2-adrenergic and PDGF-beta receptors ... Furthermore, both PDGFRbeta mediated GRK2 tyrosyl phosphorylation and GRK2 mediated PDGFRbeta seryl phosphorylation were reduced approximately 50 % in intact cells by mutation to phenylalanine of three tyrosines in the N-terminal domain of GRK2