Phosphorylation of 25-kDa synaptosome-associated protein - Possible involvement in protein kinase C-mediated regulation of neurotransmitter release

被引:215
作者
Shimazaki, Y
Nishiki, T
Omori, A
Sekiguchi, M
Kamata, Y
Kozaki, S
Takahashi, M
机构
[1] MITSUBISHI KASEI INST LIFE SCI,MACHIDA,TOKYO 194,JAPAN
[2] UNIV OSAKA PREFECTURE,COLL AGR,DEPT VET SCI,SAKAI,OSAKA 593,JAPAN
关键词
D O I
10.1074/jbc.271.24.14548
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Protein kinase C-mediated phosphorylation of a 25-kDa synaptosome-associated protein (SNAP-25) was examined in living PC12 cells, Phorbol 12-myristate 13 acetate treatment enhanced high potassium-induced [H-3]-norepinephrine release, and a 28-kDa protein recognized by an anti-SNAP-25 antibody was phosphorylated on Ser residues. The molecular size of the phosphorylated band decreased slightly following treatment with Clostridium botulinum type A neurotoxin, whereas the band disappeared after treatment with botulinum type E neurotoxin, indicating that the 28-kDa protein was SNAP-25, A phosphorylation is likely to occur at Ser(187), as this is the only Ser residue located between the cleavage sites of botulinum type A and E neurotoxins, SNAP-25 of PC12 cells was phosphorylated by purified protein kinase C in vitro, and the amount of syntaxin co immunoprecipitated with SNAP-25 was decreased by phosphorylation, These results suggest that the phosphorylation of SNAP-25 may be involved in protein kinase C-mediated regulation of catecholamine release from PC12 cells.
引用
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页码:14548 / 14553
页数:6
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