ProtModification Grk5 ---| Adrb2

URN urn:agi-ProtModification:inout-urn:agi-llid:2869:out-urn:agi-llid:154::unknown
References 7
Connectivity 2
Effect unknown

TextRef info:pmid/8662852#abs:4
MedLine Reference 8662852:3
Sentence Here we report the identification of the sites of GRK2- and GRK5-mediated beta2AR phosphorylation.

TextRef info:pmid/8170959#abs:8
CellLineName Sf9
MedLine Reference 8170959:7
Sentence While phosphorylation of the beta 2-AR by GRK2, -3, and -5 is similar, the activity of GRK2 and -3 is enhanced by G beta gamma whereas that of GRK5 is not.

TextRef info:pmid/8120045#abs:6
CellLineName Sf9
MedLine Reference 8120045:5
Sentence Purified GRK5 phosphorylates rhodopsin in a light-dependent manner and beta 2-adrenergic receptor in an agonist-dependent manner and phosphorylates the C-terminal tail regions of both receptor proteins.

TextRef info:pmid/10499588#abs:6
MedLine Reference 10499588:5
Sentence A serine residue at position 411 in the tail of the beta2-adrenergic receptor is a substrate for phosphorylation by GRK-5 (for G-protein-coupled-receptor kinase-5) and is required for interaction with EBP50 and for proper recycling of the receptor.

TextRef info:pmid/8144599#abs:5
MedLine Reference 8144599:4
Sentence Expression and characterization of a mutant GRK5 that does not autophosphorylate (S484A and T485A) reveals that the mutant has a approximately 15-20-fold reduced ability to phosphorylate the beta 2-adrenergic receptor and rhodopsin compared to wild type GRK5.

TextRef info:pmid/19092051#abs:5
MedLine Reference 19092051:4
Sentence However, tyrosyl phosphorylation of GRK5 was not necessary for GRK5-mediated phosphorylation of the beta(2)-adrenergic receptor, even though beta(2)-adrenergic receptor activation promoted tyrosyl phosphorylation of GRK5 in smooth muscle cells.
Tissue smooth muscle

TextRef info:pmid/8288567#abs:4
MedLine Reference 8288567:3
Sentence GRK5 phosphorylates the beta 2-adrenergic receptor (beta 2AR), m2 muscarinic cholinergic receptor, and rhodopsin in an agonist-dependent manner to maximal stoichiometries of approximately 2.5, 1.5, and 1 mol of phosphate/mol of receptor, respectively, with Km values of approximately 0.5 microM for the beta 2AR, approximately 16 microM for rhodopsin, and approximately 24 microM for ATP.