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Validated All-in-One™ qPCR Primer for GRK2(NM_001619.4) Search again
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
The product of this gene phosphorylates the beta-2-adrenergic receptor and appears to mediate agonist-specific desensitization observed at high agonist concentrations. This protein is an ubiquitous cytosolic enzyme that specifically phosphorylates the activated form of the beta-adrenergic and related G-protein-coupled receptors. Abnormal coupling of beta-adrenergic receptor to G protein is involved in the pathogenesis of the failing heart. [provided by RefSeq].
Gene References into function
- GRK2-phosphorylated recombinant ribosomal protein P2 reconstitutes translational activity of 60S ribosomal subunits and represents a potential novel signaling pathway responsible for P2 phosphorylation.
- a direct correlation between the expression of GRK2 and the desensitization of natively expressed H2 receptors in U-937 cells
- GRK2 plays a negative feedback regulatory role on protein kinase C(PKC)beta 1 activity in interaction between GRK2 and PKCbeta 1.
- identification of the amino-terminal domain as a regulatory Gbeta gamma binding site
- GRK2 is potential marker for organ injury and survival after cardiopulmonary bypass
- PDEG functions to link c-Src and G-protein-coupled receptor kinase 2 in a signaling unit that regulates p42/p44 mitogen-activated protein kinase by epidermal growth factor
- The pleckstsrin homology domain of this protein binds to PKC and affects the activity of PKC kinase.
- GRK2 requires agonist-induced formation of opioid receptor-G protein-coupled receptor kinase (GRK)-G beta gamma complex on the membrane in order to function
- GRK2 (and also GRK3, GRK5, and GRK6) is stabilized by interaction with Hsp90; GRK2 degradation induced by geldanamycin was predominantly through the proteasome pathway
- The concentration of betaARK1 in lymphocytes is greater in hypertensive individuals with left ventricular hypertrophy than in those without it
- GPRK2-mediated PDGFRbeta seryl phosphorylation plays an important role in desensitizing PDGFRbeta; this desensitization involves GPRK2-mediated phosphorylation of PDGFRbeta Ser(1104), with consequent dissociation of the PDGFRbeta from NHERF
- analysis of the GRK2 binding site of Galphaq
- role in terminating histamine H1 receptor singnaling by the kinase activity and RGS function of GRK2
- beta-Arrestin 2 and GRK2 are potential mediators of signaling by activated Smoothened
- GRK2 binding is critical not only for alpha2A-adrenergic receptor phosphorylation but also for full activity of the kinase.
- in leukocytes from patients with active relapsing-remitting multiple sclerosis (MS) or with secondary progressive MS, GRK2 levels are significantly reduced
- Ezrin is a novel substrate of GRK2
- kinase binding to an mGluR1 domain involved in G protein-coupling is essential for the phosphorylation-independent attenuation of signaling by GRK2
- the uncoupling and endocytosis of 5-HT4R require different GRK2 concentrations and involve distinct molecular events
- Overall, these data suggest that GRK2 has a regulatory role in EGF-induced ERK/MAPK activation.
- GRK2-as5 has a role in membrane trafficking of the mu-opioid receptor
- identification of the protein G-coupled receptor kinase 2 (GRK2), a kinase involved in the desensitization of G protein-coupled receptors (GPCR), as a downstream target and regulator of the TGFbeta-signaling cascade
- The effect of PDE4 on the of action of PKA on GRK2 phosphorylation and transport is reported.
- The presence of the alpha(2C)AR within the heterodimer resulted in a marked reduction in the level of GRK2-mediated alpha(2A)AR phosphorylation, which was accompanied by a qualitative attenuation of beta-arrestin recruitment.
- Our results suggest a feedback mechanism by which phosphorylation of GRK2 by c-Src increases both GRK2 kinase activity towards GPCRs and its specific interaction with Galphaq subunits.
- High expression was detected in septic neutrophils and control cells treated with cytokines plus LPS.
- clathrin has a role in phosphorylation and internalization of beta2-adrenergic receptor by GRK2
- Decreased expression of GRK2 is associated with obstructed bladder
- Overexpression of GRK2 in Alzheimer disease.
- insulin-like growth factor-1 alters Mdm2-mediated GRK2 degradation, leading to enhanced GRK2 stability and increased kinase levels
- analysis of the G protein-coupled receptor kinase and beta-arrestin-mediated desensitization of the angiotensin II type 1A receptor
- Phosphorylation of p38 by GRK2 at the docking groove unveils a novel mechanism for inactivating p38MAPK.
- interaction of DREAM with GRK6 and GRK2, members of the G protein-coupled receptor kinase family of proteins, and their phosphorylation of DREAM
- Our studies indicate that GRK2 is a novel component of neuronal and glial fibrillary tau deposits with no preference in tau isoform binding. GRK2 may play a role in hyperphosphorylation of tau in tauopathies.
- Our data suggest that in cirrhosis-induced vasodilation, the AT1-R is desensitized by GRK-2 and beta-arrestin-2 and that changed patterns of phosphorylated Ca(2+) sensitizing proteins decrease Ca(2+) sensitivity.
- Our preliminary data suggest that GRK2 is involved in GPCRs coupling dysfunction observed in AD patients.
- findings show in tissues that S-nitrosothiols (SNOs) increase beta-adrenergic receptor (beta-AR) expression and prevent agonist-stimulated receptor
- GRK2 interacts not only with epithelial Na(+) channels, but also with both Nedd4 and Nedd4-2.
- Mechanical unloading leads to complete reversal in PI3Kgamma and betaARK1-associated PI3K activation. Furthermore, displacement of active PI3K from betaARK1 restores betaAR responsiveness in failing myocytes.
- Regulator of coordinated integrin and G-protein-coupled receptor-directed epithelial cell migration.
- EGF transregulates opioid receptors through EGFR-mediated tyrosyl phosphorylation and activation of GRK2; GRK2 may be a mediator of cross-talk from RTK to GPCR signaling pathway
- Histamine stimulates phospholipase C-signaling in myometrial smooth muscle cells through H(1) histamine receptors and that GRK2 recruitment is a key mechanism in the regulation of H(1) histamine receptor signaling in human uterine smooth muscle.
