|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
6
|
|
pubmed:dateCreated |
1995-1-18
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
At least four forms of synaptotagmin are expressed in neurons. Of these, synaptotagmin I has an essential function in mediating Ca(2+)-triggered neurotransmitter release at hippocampal synapses, but the functional implications of multiple synaptotagmins are unknown. Synaptotagmins I-III exhibit a strikingly differential distribution between synapses, with most neurons coexpressing either synaptotagmins I or II with III. Synaptotagmin IV is present uniformly throughout the brain at low levels. Synaptotagmins III and IV are both coexpressed with synaptotagmin I in hippocampal synapses, suggesting that these synaptotagmins are not functionally redundant. The first C2 domains of synaptotagmins I-III exhibit similar Ca2+ affinities in phospholipid-binding assays, whereas that of synaptotagmin IV is unable to bind Ca2+. All synaptotagmins tested bind the clathrin-adaptor protein AP-2 with high affinity. Our results suggest that different synaptotagmins serve distinct but overlapping functions in neuronal membrane traffic, with synaptotagmins I and II representing alternative Ca2+ sensors in exocytosis and all synaptotagmins functioning as AP-2 receptors in endocytosis.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Vesicular...,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligonucleotide Probes,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipids,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Synaptotagmin I,
http://linkedlifedata.com/resource/pubmed/chemical/Synaptotagmins,
http://linkedlifedata.com/resource/pubmed/chemical/Syt1 protein, rat
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Dec
|
|
pubmed:issn |
0896-6273
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
13
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
1281-91
|
|
pubmed:dateRevised |
2006-11-15
|
|
pubmed:meshHeading |
pubmed-meshheading:7993622-Adaptor Proteins, Vesicular Transport,
pubmed-meshheading:7993622-Animals,
pubmed-meshheading:7993622-Base Sequence,
pubmed-meshheading:7993622-Brain,
pubmed-meshheading:7993622-Calcium,
pubmed-meshheading:7993622-Calcium-Binding Proteins,
pubmed-meshheading:7993622-Gene Expression Regulation,
pubmed-meshheading:7993622-Membrane Glycoproteins,
pubmed-meshheading:7993622-Molecular Sequence Data,
pubmed-meshheading:7993622-Nerve Tissue Proteins,
pubmed-meshheading:7993622-Nucleic Acid Hybridization,
pubmed-meshheading:7993622-Oligonucleotide Probes,
pubmed-meshheading:7993622-Phospholipids,
pubmed-meshheading:7993622-Phosphoproteins,
pubmed-meshheading:7993622-Protein Binding,
pubmed-meshheading:7993622-RNA, Messenger,
pubmed-meshheading:7993622-Rats,
pubmed-meshheading:7993622-Synapses,
pubmed-meshheading:7993622-Synaptic Vesicles,
pubmed-meshheading:7993622-Synaptotagmin I,
pubmed-meshheading:7993622-Synaptotagmins
|
|
pubmed:year |
1994
|
|
pubmed:articleTitle |
Functional properties of multiple synaptotagmins in brain.
|
|
pubmed:affiliation |
Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas 75235.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
