| pubmed-article:9252412 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9252412 | lifeskim:mentions | umls-concept:C0015127 | lld:lifeskim |
| pubmed-article:9252412 | lifeskim:mentions | umls-concept:C0006772 | lld:lifeskim |
| pubmed-article:9252412 | lifeskim:mentions | umls-concept:C0039063 | lld:lifeskim |
| pubmed-article:9252412 | lifeskim:mentions | umls-concept:C1314792 | lld:lifeskim |
| pubmed-article:9252412 | lifeskim:mentions | umls-concept:C1419206 | lld:lifeskim |
| pubmed-article:9252412 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:9252412 | pubmed:issue | 33 | lld:pubmed |
| pubmed-article:9252412 | pubmed:dateCreated | 1997-9-4 | lld:pubmed |
| pubmed-article:9252412 | pubmed:abstractText | The GTPase Rab3A has been postulated to cycle on and off synaptic membranes during the course of neurotransmission. Moreover, a Rab guanine nucleotide dissociation inhibitor has been shown to cause Rab3A to dissociate from synaptic membranes in vitro. We demonstrate here that Ca2+/calmodulin also can cause Rab3A to dissociate from synaptic membranes in vitro. Like Rab guanine nucleotide dissociation inhibitor, it forms a 1:1 complex with Rab3A that requires both the lipidated C terminus of Rab3A and the presence of bound guanine nucleotide. In addition, a synthetic peptide corresponding to the Lys62-Arg85 sequence of Rab3A can prevent the dissociating effect of each protein and disrupt complexes between each protein and Rab3A. However, Ca2+/calmodulin's effect differs from that of Rab guanine nucleotide dissociation inhibitor not only in being Ca2+-dependent but also in having a less stringent requirement for GDP as opposed to GTP and in involving a less complete dissociation of Rab3A. The functional significance in vivo of Ca2+/calmodulin's effect remains to be determined; it may depend in part on the relative amounts of Ca2+/calmodulin and Rab guanine nucleotide dissociation inhibitor that are available for binding to Rab3A in individual, activated nerve termini. | lld:pubmed |
| pubmed-article:9252412 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9252412 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9252412 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9252412 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9252412 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9252412 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9252412 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9252412 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9252412 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9252412 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9252412 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9252412 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:9252412 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:9252412 | pubmed:author | pubmed-author:GlomsetJ AJA | lld:pubmed |
| pubmed-article:9252412 | pubmed:author | pubmed-author:ParkJ BJB | lld:pubmed |
| pubmed-article:9252412 | pubmed:author | pubmed-author:FarnsworthC... | lld:pubmed |
| pubmed-article:9252412 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9252412 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:9252412 | pubmed:volume | 272 | lld:pubmed |
| pubmed-article:9252412 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9252412 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9252412 | pubmed:pagination | 20857-65 | lld:pubmed |
| pubmed-article:9252412 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:9252412 | pubmed:meshHeading | pubmed-meshheading:9252412-... | lld:pubmed |
| pubmed-article:9252412 | pubmed:meshHeading | pubmed-meshheading:9252412-... | lld:pubmed |
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| pubmed-article:9252412 | pubmed:meshHeading | pubmed-meshheading:9252412-... | lld:pubmed |
| pubmed-article:9252412 | pubmed:meshHeading | pubmed-meshheading:9252412-... | lld:pubmed |
| pubmed-article:9252412 | pubmed:meshHeading | pubmed-meshheading:9252412-... | lld:pubmed |
| pubmed-article:9252412 | pubmed:meshHeading | pubmed-meshheading:9252412-... | lld:pubmed |
| pubmed-article:9252412 | pubmed:meshHeading | pubmed-meshheading:9252412-... | lld:pubmed |
| pubmed-article:9252412 | pubmed:meshHeading | pubmed-meshheading:9252412-... | lld:pubmed |
| pubmed-article:9252412 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9252412 | pubmed:articleTitle | Ca2+/calmodulin causes Rab3A to dissociate from synaptic membranes. | lld:pubmed |
| pubmed-article:9252412 | pubmed:affiliation | Howard Hughes Medical Institute, Department of Medicine, University of Washington, Seattle, Washington 98195-7370, USA. | lld:pubmed |
| pubmed-article:9252412 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9252412 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9252412 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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