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

Youji Shimazaki, Tei Ichi Nishiki, Akira Omori, Mariko Sekiguchi, Yoichi Kamata, Shunji Kozaki, Masami Takahashi

Research output: Contribution to journalArticle

212 Citations (Scopus)

Abstract

Protein kinase C-mediated phosphorylation of a 25-kDa synaptosome-associated protein (SNAP-25) was examined in living PC 12 cells. Phorbol 12-myristate 13-acetate treatment enhanced high potassium-induced [3H]-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 Ser187, 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.

Original languageEnglish
Pages (from-to)14548-14553
Number of pages6
JournalJournal of Biological Chemistry
Volume271
Issue number24
DOIs
Publication statusPublished - Jan 1 1996

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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