Regulation of exocytosis in chromaffin cells by phosducin-like protein, a protein interacting with G protein betagamma subunits.
Fiche publication
Date publication
septembre 2000
Journal
FEBS letters
Auteurs
Membres identifiés du Cancéropôle Est :
Dr BADER Marie-France, Dr CHASSEROT-GOLAZ Sylvette, Dr VITALE Nicolas
Tous les auteurs :
Gensse M, Vitale N, Chasserot-Golaz S, Bader MF
Lien Pubmed
Résumé
Phosducin and related proteins have been identified as ubiquitous regulators of signalling mediated by betagamma subunits of trimeric G proteins. To explore a role for phosducin in regulated exocytosis, we have examined the distribution and putative function of phosducin-like protein (PhLP) in adrenal medullary chromaffin cells. The full-length cDNA encoding the short splice variant of PhLP (PhLPs) was cloned from cultured chromaffin cells. Native PhLPs was found associated with plasma membranes and detected in the subplasmalemmal area of resting chromaffin cells by confocal immunofluorescence analysis. Stimulation with secretagogues triggered a massive redistribution of PhLPs into the cytoplasm. When microinjected into individual chromaffin cells, recombinant PhLPs inhibited catecholamine secretion evoked by a depolarizing concentration of K+ without affecting calcium mobilization. Thus, PhLPs may participate directly in the regulation of calcium-evoked exocytosis.
Mots clés
Amino Acid Sequence, Animals, Base Sequence, Carrier Proteins, biosynthesis, Cell Membrane, Cells, Cultured, Chromaffin Cells, cytology, Cytosol, metabolism, DNA, Complementary, Exocytosis, physiology, GTP-Binding Protein beta Subunits, GTP-Binding Protein gamma Subunits, Heterotrimeric GTP-Binding Proteins, metabolism, Humans, Molecular Sequence Data, Nerve Tissue Proteins, biosynthesis, Protein Transport, Rats, Recombinant Fusion Proteins, genetics
Référence
FEBS Lett.. 2000 Sep;480(2-3):184-8