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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.
Showing 10 out of 43 products:
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 Pubmed References
Human Polyclonal PDCL Primary Antibody for ICC, IF - ABIN4344392
Stadler, Rexhepaj, Singan, Murphy, Pepperkok, Uhlén, Simpson, Lundberg: Immunofluorescence and fluorescent-protein tagging show high correlation for protein localization in mammalian cells. in Nature methods 2013
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.
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.
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
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 (show GNB5 Antibodies)-RGS9 (show RGS Antibodies).
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.