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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1991-2-28
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pubmed:abstractText |
Synapsin I is a neuron-specific phosphoprotein that binds to small synaptic vesicles and actin filaments in a phosphorylation-dependent fashion. It has been hypothesized that dephosphorylated synapsin I inhibits neurotransmitter release either by forming a cage around synaptic vesicles (cage model) or by anchoring them to the F-actin cytoskeleton of the nerve terminal (crosslinking model). Computer modeling was performed with the aim of testing the impact of phosphorylation on the molecular interactions of synapsin I within the nerve terminal. The results of the simulation experiments demonstrate that in the crosslinking model the phosphorylation of synapsin I causes a severalfold increase in the number of vesicles released from the cytoskeleton and that in the cage model the phosphorylation induces a 2-fold increase in the number of vesicles bearing one or more unsaturated synapsin I binding sites. These data are compatible with the view that the function of synapsin I in the short-term regulation of neurotransmitter release is to induce a phosphorylation-dependent transition of synaptic vesicles from a "reserve pool" to a readily "releasable pool" of vesicles.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1671174-13175199,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1671174-13320373,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1671174-14278410,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1671174-1978321,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1671174-1980418,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1671174-2160524,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1671174-2497104,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1671174-2497105,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1671174-2497106,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1671174-2510160,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1671174-2859595,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1671174-3087973,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1671174-3104800,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1671174-3276830,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1671174-42112,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1671174-5827910,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1671174-6278329,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1671174-6404911,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1671174-6404912,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1671174-6424121,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1671174-6809906,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1671174-6992165,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1671174-84386
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
88
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
575-9
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:1671174-Actins,
pubmed-meshheading:1671174-Animals,
pubmed-meshheading:1671174-Computer Simulation,
pubmed-meshheading:1671174-Kinetics,
pubmed-meshheading:1671174-Mathematics,
pubmed-meshheading:1671174-Models, Neurological,
pubmed-meshheading:1671174-Nerve Tissue Proteins,
pubmed-meshheading:1671174-Neurotransmitter Agents,
pubmed-meshheading:1671174-Phosphoproteins,
pubmed-meshheading:1671174-Protein Binding,
pubmed-meshheading:1671174-Synapsins,
pubmed-meshheading:1671174-Synaptic Vesicles
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pubmed:year |
1991
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pubmed:articleTitle |
Computer modeling of synapsin I binding to synaptic vesicles and F-actin: implications for regulation of neurotransmitter release.
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pubmed:affiliation |
Institute of Human Physiology, University of Modena, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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