During Drosophila phototransduction, the G protein coupled receptor (GPCR) Rhodopsin (Rh1) transduces photon absorption into electrical signal via G-protein coupled activation of phospholipase C (PLC).
Sudipta Ashe, Shweta Yadav
doaj +1 more source
The Role of G Protein-Coupled Receptor Kinase 6 Regulation in Inflammation and Pain. [PDF]
Stegen M, Frey UH.
europepmc +1 more source
Downregulation of G protein-coupled receptor kinase 4 protects against kidney ischemia-reperfusion injury. [PDF]
Yang D +20 more
europepmc +1 more source
G protein-coupled receptor kinases (GRKs) are essential regulators of signaling pathways mediated by G protein-coupled receptors. Recent research suggests that GRK-mediated phosphorylation patterns dictate functional selectivity, leading to biased ...
Min Jae Seo, Wookyung Yu
doaj +1 more source
G Protein-Coupled Receptor Kinase 2 Selectively Enhances β-Arrestin Recruitment to the D2 Dopamine Receptor through Mechanisms That Are Independent of Receptor Phosphorylation. [PDF]
Sánchez-Soto M +12 more
europepmc +1 more source
Kinase Activity Is Not Required for G Protein-Coupled Receptor Kinase 4 Restraining mTOR Signaling during Cilia and Kidney Development. [PDF]
Gerhards J +8 more
europepmc +1 more source
G Protein-Coupled Receptor Kinase 4 Is a Novel Prognostic Factor in Hepatocellular Carcinoma. [PDF]
Luo Y, Wang Z, Xiao S, Li R, Jiang X.
europepmc +1 more source
A novel octopamine receptor with preferential expression in Drosophila mushroom bodies [PDF]
Octopamine is a neuromodulator that mediates diverse physiological processes in invertebrates. In some insects, such as honeybees and fruit flies, octopamine has been shown to be a major stimulator of adenylyl cyclase and to function in associative ...
Han, K-A, Millar, NS
core
Dopamine-induced arrestin recruitment and desensitization of the dopamine D4 receptor is regulated by G protein-coupled receptor kinase-2. [PDF]
Burström V +6 more
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Structures of rhodopsin in complex with G-protein-coupled receptor kinase 1. [PDF]
Chen Q +11 more
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