A role for synaptotagmin (p65) in regulated exocytosis

Lisa A. Elferink, Michael R. Peterson, Richard H. Scheller

Research output: Contribution to journalArticlepeer-review

235 Scopus citations


Proteins that are specifically localized to synaptic vesicles in the nervous system have been proposed to mediate aspects of synaptic transmission. Antibodies raised against the cytoplasmic domains of five of these proteins, vamp, rab3A, synaptophysin, synaptotagmin, and SV2, were used to investigate their function. Microinjection of monoclonal and polyclonal antibodies raised against synaptotagmin (p65), but not the other vesicle proteins, decreases K+/Ca2+-mediated dopamine β-hydroxylase surface staining, a measure of regulated secretion in PC12 cells. Microinjection of a soluble fragment of synaptotagmin encompassing one of the domains homologous to the C2 regulatory region of protein kinase C, but lacking the membrane anchor, also inhibits evoked dopamine β-hydroxylase surface staining. These results provide support for the hypothesis that synaptotagmin, a Ca2+- and phospholipid-binding protein, is important for regulated exocytosis in neurons.

Original languageEnglish (US)
Pages (from-to)153-159
Number of pages7
Issue number1
StatePublished - Jan 15 1993
Externally publishedYes

ASJC Scopus subject areas

  • General Biochemistry, Genetics and Molecular Biology


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