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Retinoic acid inhibits inducible nitric oxide synthase expression in 3T3-L1 adipocytes
양정예,구본선,강미경,노혜원,손희숙,지은청,박진우 생화학분자생물학회 2002 Experimental and molecular medicine Vol.34 No.5
The release of neurotransmiter is regulated in the processes of membrane docking and membrane fusion between synaptic vesicles and presynaptic plasma membranes. Synaptic vesicles contain a diverse set of proteins that participate in these processes. Small GTP-binding proteins exist in the synaptic vesicles and are sugested to play roles for the regulation of neurotransmiter release. We have examined a possible role of GTP-binding proteins in the regulation of protein phosphory-lation in the synaptic vesicles. GTPγS stimulated the phosphorylation of 46 kDa protein (p46) with pI value of 5.0-5.2, but GDPβS did not. The p46 was identified as protein interacting with C-kinase 1 (PICK-1) by MALDI-TOF mass spectroscopy an-alysis, and anti-PICK-1 antibody recognized the p46 spot on 2-dimensional gel electrophoresis. Rab guanine nucleotide dissociation inhibitor (RabGDI), which dissociates Rab proteins from SVs, did not affect phosphorylation of p46. Ca2+/ calmodulin (CaM), which causes the smal GTP- binding proteins like Rab3A and RalA to diso-ciate from the membranes and stimulates CaM- dependnet protein kinase(s) and phosphatase, the presence of cyclosporin A and cyclophylin. However, RhoGDI, which dissociates Rho proteins from membranes, reduced the phosphorylation of p46 to the extent of about 50%. These results support that p46 was PICK-1, and its phosphory-lation was stimulated by GTP and Ca2+/CaM di-rectly or indirectly through GTP-binding protein(s) and Ca2+/CaM efector protein(s). The phosphoryl-ation of p46 (PICK-1) by GTP and Ca2+/CaM may be important for the regulation of transporters and neurosecretion.calcium; calmodulin; guanosine triphos-phate; phosphorylation; rho GTP-binding proteins; syn-aptic vesicles