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Phosducin-like protein is a putative modulator of heterotrimeric G proteins. Additionally we are shipping Phosducin-Like Proteins (7) and many more products for this protein.
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Human Polyclonal PDCL Primary Antibody for WB - ABIN1944777
Wiemann, Weil, Wellenreuther, Gassenhuber, Glassl, Ansorge, Böcher, Blöcker, Bauersachs, Blum, Lauber, Düsterhöft, Beyer, Köhrer, Strack, Mewes, Ottenwälder, Obermaier, Tampe, Heubner, Wambutt, Korn et al.: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. ... in Genome research 2001
Show all 3 references for ABIN1944777
Phosducin (show PDC Antibodies) regulates secretory activity in TT line of thyroid parafollicular C cells.
PhLP1 binding stabilizes the Gbeta (show SUCLG2 Antibodies) fold, disrupting interactions with CCT (show FLVCR2 Antibodies) and releasing a PhLP1-Gbeta (show SUCLG2 Antibodies) dimer for assembly with Ggamma.
evidence of a generic mechanism, whereby the splicing of the PhLP gene could potentially and efficiently regulate the cellular levels of heterotrimeric G proteins.
Data suggest that phosducin (show PDC Antibodies) rs12402521 polymorphism is an important genetic predictor of obesity-related hypertension.
identification of Pdc (show PNKD Antibodies) as a gene for stress-induced hypertension offers new insights into the relationship between sympathetic nervous system activation, blood pressure regulation and genetic factors
Data suggest that the existence of a common epitope on the molecules of phosducin (show PDC Antibodies) and beta-actin (show ACTB Antibodies) may reflect a topological similarity of a small region of their surfaces.
Candidate gene-based association studies in 2 different populations revealed several SNPs in the PDC (show PNKD Antibodies) gene to be associated with stress-dependent blood pressure phenotypes.
physiological control of G-protein regulation by PhLP seems to involve phosphorylation by CK2 (show CSNK2A1 Antibodies) and alternative splicing of the regulator
the strong inhibitory action of PhLP(S) on Gbetagamma signaling is the result of a previously unrecognized mechanism of Gbetagamma-regulation, inhibition of Gbetagamma-folding by interference with TCP-1alpha (show TCP1 Antibodies)
PhLP phosphorylation permits the release of a PhLP x Gbeta (show SUCLG2 Antibodies) intermediate from cytosolic chaperonin (show HSPD1 Antibodies) complex, allowing Ggamma to associate with Gbeta (show SUCLG2 Antibodies) in this intermediate complex.
findings reveal a common mechanism of Gbetagamma and RGS9-Gbeta5 assembly in rods and cones, highlighting the importance of PhLP1 and CCT-mediated Gbeta complex formation in G protein signaling.
this study demonstrated in vivo that PhLP1 is required for the folding and assembly of both Gbetagamma and Gbeta5-RGS9.
These data are consistent with the hypothesis that PhLP is a widely expressed modulator of Gbetagamma function.
These results suggest a mechanism for Gbetagamma assembly in which PhLP stabilizes the nascent Gbeta (show SUCLG2 Antibodies) polypeptide until Ggamma can associate, resulting in membrane binding of Gbetagamma and release of PhLP to catalyze another round of assembly.
N-glycosylated phosducin-like protein long (PhLP(L)) is expressed in all structures of the central nervous system and regulates opioid receptor function in the brain.
identification of novel germ-like specific form in phosducin-like protein family
antagonistic actions of PhLP3 and prefoldin serve to modulate CCT activity and play a key role in establishing a functional cytoskeleton in vivo
Phosducin-like protein is a putative modulator of heterotrimeric G proteins. The protein shares extensive amino acid sequence homology with phosducin, a phosphoprotein expressed in retina and pineal gland. Both phosducin-like protein and phosphoducin have been shown to regulate G-protein signaling by binding to the beta-gamma subunits of G proteins.
, 33 kDa phototransducing protein
, G beta gamma binding protein
, phosducin-like orphan protein
, phosducin-like protein