Phosducin-like protein (PDCL) is a putative modulator of heterotrimeric G proteins. It was initially isolated as the product of an ethanol-responsive gene in neural cell cultures . PDCL shares extensive amino acid sequence homology with phosducin (PDC; OMIM 171490), a phosphoprotein expressed in retina and pineal gland that inhibits several G protein-coupled signaling pathways by binding to the beta-gamma subunits of G proteins.
NCBI Summary:
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.
General function
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Cellular localization
Cytoplasmic
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Ovarian function
Oogenesis
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Expression regulated by
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Ovarian localization
Oocyte
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Lopez P, et al 2002 reported a novel germ line specific gene of the phosducin-like (PhLP) family has a meiotic function conserved from yeast to mice.
They identified a new member of the phosducin-like (PhLP) protein family, predominantly, if not exclusively expressed in male and female germ cells. In situ analysis on testis sections and analysis of purified spermatogenic cell fractions evidenced a stage-specific expression, with high levels of RNA and protein in pachytene spermatocytes and round spermatids. Three mRNA species were detected, which correspond to different polyadenylation sites and vary in abundance during germ cell maturation. Only low levels of RNA were detected in whole ovary extracts, but expression of the protein became detectable within hours after hormonal induction of superovulation. The gene (Mgcphlp) is located on mouse chromosome 5 in the immediate vicinity of the Clock locus. The predicted aminoacid sequence shows extensive similarities not only with the known mammalian PhLP proteins, but also with the yeast phosducin-like protein Plp2, required for the production and growth of haploid cells. Expression of the murine protein was found to complement the defect of a yeast plp2D mutant. We propose that the MgcPhLP/PLP2 proteins exert in germ cell maturation a function conserved from yeast to mammals.