A role for synaptotagmin (p65) in regulated exocytosis
Article Abstract:
The role of synaptotagmin, an abundant synaptic vesicle protein, in the translocation of synaptic vesicles to the plasma membrane and the subsequent fusion of these membranes was investigated. Direct microinjection of antibodies raised against synaptotagmin as well as bacterially expressed forms of the protein in PC12 cells altered the regulated secretion in these cells. The results provide additional evidence that synaptotagmin plays an important role in regulating synaptic vesicle membrane flow.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1993
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Synaptotagmin: a calcium-sensitive inhibitor of exocytosis?
Article Abstract:
Synaptotagmin, a synaptic vesicle protein that is present in large numbers in certain endocrine cells and neurons, binds directly or indirectly through syntaxin. It docks synaptic vesicles near Ca2+ channels, and the local elevation of cytosolic Ca2+ often enhances exocytotic fusion. Synaptic vesicle proteins may inhibit exocytosis at dormant Ca2+ levels. Investigations of nonneuronal cells indicate that Ca2+ dependent exocytotic fusion is evident in all eukaryotes.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1993
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SNARE complex formation is triggered by Ca2+ and drives membrane fusion
Article Abstract:
The presence of a group of proteins from the VAMP, SNAP-25 and syntaxin families is essential to the process of membrane fusion. Collectively known as SNAREs, these proteins form a helical bundle that bridge apposed membranes. Research into clostridial proteins that cleave SNAREs suggests that the mechanism by which Ca2+ regulates transmitter release is linked to the action of the 65 aa C-terminal fragment of SNAP-25.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1999
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