Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5059
pubmed:dateCreated
1992-6-19
pubmed:abstractText
Neurons release neurotransmitters by calcium-dependent exocytosis of synaptic vesicles. However, the molecular steps transducing the calcium signal into membrane fusion are still an enigma. It is reported here that synaptotagmin, a highly conserved synaptic vesicle protein, binds calcium at physiological concentrations in a complex with negatively charged phospholipids. This binding is specific for calcium and involves the cytoplasmic domain of synaptotagmin. Calcium binding is dependent on the intact oligomeric structure of synaptotagmin (it is abolished by proteolytic cleavage at a single site). These results suggest that synaptotagmin acts as a cooperative calcium receptor in exocytosis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
256
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1021-5
pubmed:dateRevised
2007-3-19
pubmed:meshHeading
pubmed-meshheading:1589771-Animals, pubmed-meshheading:1589771-Brain Chemistry, pubmed-meshheading:1589771-Calcium, pubmed-meshheading:1589771-Calcium-Binding Proteins, pubmed-meshheading:1589771-Cell Membrane, pubmed-meshheading:1589771-Cytoplasmic Granules, pubmed-meshheading:1589771-Dansyl Compounds, pubmed-meshheading:1589771-Energy Transfer, pubmed-meshheading:1589771-Exocytosis, pubmed-meshheading:1589771-Fluorescent Dyes, pubmed-meshheading:1589771-Liposomes, pubmed-meshheading:1589771-Macromolecular Substances, pubmed-meshheading:1589771-Membrane Glycoproteins, pubmed-meshheading:1589771-Nerve Tissue Proteins, pubmed-meshheading:1589771-Phosphatidylethanolamines, pubmed-meshheading:1589771-Rats, pubmed-meshheading:1589771-Synaptic Vesicles, pubmed-meshheading:1589771-Synaptotagmins
pubmed:year
1992
pubmed:articleTitle
Synaptotagmin: a calcium sensor on the synaptic vesicle surface.
pubmed:affiliation
Department of Neurochemistry, Max-Planck-Institute for Psychiatry, Martinsried, Germany.
pubmed:publicationType
Journal Article