pubmed-article:15123626 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15123626 | lifeskim:mentions | umls-concept:C0249586 | lld:lifeskim |
pubmed-article:15123626 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
pubmed-article:15123626 | lifeskim:mentions | umls-concept:C0015283 | lld:lifeskim |
pubmed-article:15123626 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
pubmed-article:15123626 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
pubmed-article:15123626 | lifeskim:mentions | umls-concept:C1413286 | lld:lifeskim |
pubmed-article:15123626 | lifeskim:mentions | umls-concept:C1420506 | lld:lifeskim |
pubmed-article:15123626 | lifeskim:mentions | umls-concept:C0851827 | lld:lifeskim |
pubmed-article:15123626 | lifeskim:mentions | umls-concept:C1701901 | lld:lifeskim |
pubmed-article:15123626 | pubmed:issue | 28 | lld:pubmed |
pubmed-article:15123626 | pubmed:dateCreated | 2004-7-5 | lld:pubmed |
pubmed-article:15123626 | pubmed:abstractText | Cyclin-dependent kinase 5 (Cdk5) is a proline-directed serine/threonine protein kinase that requires association with a regulatory protein, p35 or p39, to form an active enzyme. Munc18-1 plays an essential role in membrane fusion, and its function is regulated by phosphorylation. We report here that both p35 and p39 were expressed in insulin-secreting beta-cells, where they exhibited individual subcellular distributions and associated with membranous organelles of different densities. Overexpression of Cdk5, p35, or p39 showed that Cdk5 and p39 augmented Ca(2+)-induced insulin exocytosis. Suppression of p39 and Cdk5, but not of p35, by antisense oligonucleotides selectively inhibited insulin exocytosis. Transient transfection of primary beta-cells with Munc18-1 templates mutated in potential Cdk5 or PKC phosphorylation sites, in combination with Cdk5 and the different Cdk5 activators, suggested that Cdk5/p39-promoted Ca(2+)-dependent insulin secretion from primary beta-cells by phosphorylating Munc18-1 at a biochemical step immediately prior to vesicle fusion. | lld:pubmed |
pubmed-article:15123626 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15123626 | pubmed:language | eng | lld:pubmed |
pubmed-article:15123626 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15123626 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:15123626 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15123626 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15123626 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15123626 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15123626 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15123626 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15123626 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15123626 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15123626 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15123626 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15123626 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15123626 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15123626 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15123626 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15123626 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15123626 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15123626 | pubmed:month | Jul | lld:pubmed |
pubmed-article:15123626 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:15123626 | pubmed:author | pubmed-author:BerggrenPer-O... | lld:pubmed |
pubmed-article:15123626 | pubmed:author | pubmed-author:GromadaJesper... | lld:pubmed |
pubmed-article:15123626 | pubmed:author | pubmed-author:FriedGabrielG | lld:pubmed |
pubmed-article:15123626 | pubmed:author | pubmed-author:LiljaLenaL | lld:pubmed |
pubmed-article:15123626 | pubmed:author | pubmed-author:JohanssonJenn... | lld:pubmed |
pubmed-article:15123626 | pubmed:author | pubmed-author:MandicSlavena... | lld:pubmed |
pubmed-article:15123626 | pubmed:author | pubmed-author:BarkChristina... | lld:pubmed |
pubmed-article:15123626 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:15123626 | pubmed:day | 9 | lld:pubmed |
pubmed-article:15123626 | pubmed:volume | 279 | lld:pubmed |
pubmed-article:15123626 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15123626 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15123626 | pubmed:pagination | 29534-41 | lld:pubmed |
pubmed-article:15123626 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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pubmed-article:15123626 | pubmed:year | 2004 | lld:pubmed |
pubmed-article:15123626 | pubmed:articleTitle | Cyclin-dependent kinase 5 associated with p39 promotes Munc18-1 phosphorylation and Ca(2+)-dependent exocytosis. | lld:pubmed |
pubmed-article:15123626 | pubmed:affiliation | Department of Molecular Medicine, Karolinska Institutet, Karolinska University Hospital, SE-171 76 Stockholm, Sweden. | lld:pubmed |
pubmed-article:15123626 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:15123626 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:15123626 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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