◀ Back to RHO

GRK4 — RHO

Text-mined interactions from Literome

Gan et al., J Biol Chem 2000 : In addition, the recombinant proteins that represent the C-terminal domain and the conserved region of GRK2 could inhibit GRK2 mediated phosphorylation of rhodopsin and receptor mediated activation of GRK2 but not GRK2 mediated phosphorylation of the peptide substrate
Eichmann et al., J Biol Chem 2003 : And indeed, the amino terminus of GRK2 ( GRK2 ( 1-185 ) ) inhibited a Gbetagamma stimulated inositol phosphate signal in cells, purified GRK2 ( 1-185 ) suppressed the Gbetagamma stimulated phosphorylation of rhodopsin , and GRK2 ( 1-185 ) bound directly to purified Gbetagamma subunits ... In addition to the Gbetagamma regulatory activity, the amino-terminal Gbetagamma binding site of GRK2 affects the kinase activity of GRK2 because antibodies specifically cross reacting with the amino terminus of GRK2 suppressed the GRK2 dependent phosphorylation of rhodopsin
Gan et al., J Biol Chem 2004 : The CC regions of GRK-1, GRK-2, and GRK-5, representatives of the three subfamilies of GRKs, could bind rhodopsin in vitro and inhibit GRK-2 mediated phosphorylation of rhodopsin , but not a peptide GRK substrate