| pubmed-article:1328883 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1328883 | lifeskim:mentions | umls-concept:C0248868 | lld:lifeskim |
| pubmed-article:1328883 | lifeskim:mentions | umls-concept:C0242210 | lld:lifeskim |
| pubmed-article:1328883 | lifeskim:mentions | umls-concept:C0087044 | lld:lifeskim |
| pubmed-article:1328883 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:1328883 | pubmed:issue | 6394 | lld:pubmed |
| pubmed-article:1328883 | pubmed:dateCreated | 1992-11-16 | lld:pubmed |
| pubmed-article:1328883 | pubmed:abstractText | Synapsin I is a synaptic vesicle-associated phosphoprotein that is involved in the modulation of neurotransmitter release. Ca2+/calmodulin-dependent protein kinase II, which phosphorylates two sites in the carboxy-terminal region of synapsin I, causes synapsin I to dissociate from synaptic vesicles and increases neurotransmitter release. Conversely, the dephosphorylated form of synapsin I, but not the form phosphorylated by Ca2+/calmodulin-dependent protein kinase II, inhibits neurotransmitter release. The amino-terminal region of synapsin I interacts with membrane phospholipids, whereas the C-terminal region binds to a protein component of synaptic vesicles. Here we demonstrate that the binding of the C-terminal region of synapsin I involves the regulatory domain of a synaptic vesicle-associated form of Ca2+/calmodulin-dependent protein kinase II. Our results indicate that this form of the kinase functions both as a binding protein for synapsin I, and as an enzyme that phosphorylates synapsin I and promotes its dissociation from the vesicles. | lld:pubmed |
| pubmed-article:1328883 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1328883 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1328883 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1328883 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1328883 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1328883 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1328883 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1328883 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1328883 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:1328883 | pubmed:issn | 0028-0836 | lld:pubmed |
| pubmed-article:1328883 | pubmed:author | pubmed-author:GreengardPP | lld:pubmed |
| pubmed-article:1328883 | pubmed:author | pubmed-author:CzernikA JAJ | lld:pubmed |
| pubmed-article:1328883 | pubmed:author | pubmed-author:BenfenatiFF | lld:pubmed |
| pubmed-article:1328883 | pubmed:author | pubmed-author:RubensteinJ... | lld:pubmed |
| pubmed-article:1328883 | pubmed:author | pubmed-author:GorelickF SFS | lld:pubmed |
| pubmed-article:1328883 | pubmed:author | pubmed-author:ValtortaFF | lld:pubmed |
| pubmed-article:1328883 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1328883 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:1328883 | pubmed:volume | 359 | lld:pubmed |
| pubmed-article:1328883 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1328883 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1328883 | pubmed:pagination | 417-20 | lld:pubmed |
| pubmed-article:1328883 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:1328883 | pubmed:meshHeading | pubmed-meshheading:1328883-... | lld:pubmed |
| pubmed-article:1328883 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1328883 | pubmed:articleTitle | Synaptic vesicle-associated Ca2+/calmodulin-dependent protein kinase II is a binding protein for synapsin I. | lld:pubmed |
| pubmed-article:1328883 | pubmed:affiliation | Institute of Human Physiology, University of Modena, Italy. | lld:pubmed |
| pubmed-article:1328883 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1328883 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1328883 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:25400 | entrezgene:pubmed | pubmed-article:1328883 | lld:entrezgene |
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