Cyclin-dependent Kinase 5 Associated with p39 Promotes Munc18-1 Phosphorylation and Ca2+-dependent Exocytosis
作者： Lena Lilja , Jenny Ulrika Johansson , Jesper Gromada , Slavena Andrea Mandic , Gabriel Fried
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摘要: Cyclin-dependent kinase 5 (Cdk5) is a proline-directed serine/threonine protein that requires association with regulatory protein, p35 or p39, to form an active enzyme. Munc18-1 plays essential role in membrane fusion, and its function regulated by phosphorylation. We report here both p39 were expressed insulin-secreting β-cells, where they exhibited individual subcellular distributions associated membranous organelles of different densities. Overexpression Cdk5, p35, showed Cdk5 augmented Ca2+-induced insulin exocytosis. Suppression but not antisense oligonucleotides selectively inhibited Transient transfection primary β-cells templates mutated potential PKC phosphorylation sites, combination the activators, suggested Cdk5/p39-promoted Ca2+-dependent secretion from phosphorylating at biochemical step immediately prior vesicle fusion.
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