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Phosducin-like protein is a putative modulator of heterotrimeric G proteins. Zusätzlich bieten wir Ihnen Phosducin-Like Antikörper (49) und und viele weitere Produktgruppen zu diesem Protein an.
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PhLP1 binding stabilizes the Gbeta (zeige SUCLG2 Proteine) fold, disrupting interactions with CCT (zeige FLVCR2 Proteine) and releasing a PhLP1-Gbeta (zeige SUCLG2 Proteine) 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.
physiological control of G-protein regulation by PhLP seems to involve phosphorylation by CK2 (zeige CSNK2A1 Proteine) 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 (zeige TCP1 Proteine)
PhLP phosphorylation permits the release of a PhLP x Gbeta (zeige SUCLG2 Proteine) intermediate from cytosolic chaperonin (zeige HSPD1 Proteine) complex, allowing Ggamma to associate with Gbeta (zeige SUCLG2 Proteine) in this intermediate complex.
cytosolic chaperonin complex-dependent mechanism exists for Gbeta5-RGS7 assembly that utilizes the co-chaperone activity of PhLP1 in a unique way
PhLP-M1-G149, a Gbetagamma-interacting construct derived from phosducin-like protein 1 (PhLP) is a differential inhibitor of Gbetagamma
Pdcl has been implicated as a positive regulator of Hedgehog (zeige SHH Proteine) signaling that may control the trafficking of signaling receptors to primary cilia.
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 (zeige GNB5 Proteine)-RGS9 (zeige RGS Proteine).
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 (zeige SUCLG2 Proteine) 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.