Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2001-1-16
pubmed:abstractText
Chemical synaptic transmission serves as the main form of cell to cell communication in the nervous system. Neurotransmitter release occurs through the process of regulated exocytosis, in which a synaptic vesicle releases its contents in response to an increase in calcium. The use of genetic, biochemical, structural, and functional studies has led to the identification of factors important in the synaptic vesicle life cycle. Here we focus on the prominent role of SNARE (soluble NSF attachment protein receptor) proteins during membrane fusion and the regulation of SNARE function by Rab3a, nSec1, and NSF. Many of the proteins important for transmitter release have homologs involved in intracellular vesicle transport, and all forms of vesicle trafficking share common basic principles. Finally, modifications to the synaptic exocytosis pathway are very likely to underlie certain forms of synaptic plasticity and therefore contribute to learning and memory.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Calcium, http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/EXOC3 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/EXOC4 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Munc18 Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins, http://linkedlifedata.com/resource/pubmed/chemical/SNARE Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Synaptotagmins, http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/rab3A GTP-Binding Protein
pubmed:status
MEDLINE
pubmed:issn
1081-0706
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
19-49
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:11031229-Animals, pubmed-meshheading:11031229-Calcium, pubmed-meshheading:11031229-Calcium-Binding Proteins, pubmed-meshheading:11031229-Carrier Proteins, pubmed-meshheading:11031229-Exocytosis, pubmed-meshheading:11031229-Humans, pubmed-meshheading:11031229-Membrane Fusion, pubmed-meshheading:11031229-Membrane Glycoproteins, pubmed-meshheading:11031229-Membrane Proteins, pubmed-meshheading:11031229-Munc18 Proteins, pubmed-meshheading:11031229-Nerve Tissue Proteins, pubmed-meshheading:11031229-Phosphorylation, pubmed-meshheading:11031229-SNARE Proteins, pubmed-meshheading:11031229-Signal Transduction, pubmed-meshheading:11031229-Synaptic Vesicles, pubmed-meshheading:11031229-Synaptotagmins, pubmed-meshheading:11031229-Vesicular Transport Proteins, pubmed-meshheading:11031229-rab3A GTP-Binding Protein
pubmed:year
2000
pubmed:articleTitle
Mechanisms of synaptic vesicle exocytosis.
pubmed:affiliation
Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, California 94305-5428, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review