| pubmed-article:12482583 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12482583 | lifeskim:mentions | umls-concept:C0521390 | lld:lifeskim |
| pubmed-article:12482583 | lifeskim:mentions | umls-concept:C0752274 | lld:lifeskim |
| pubmed-article:12482583 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
| pubmed-article:12482583 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
| pubmed-article:12482583 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:12482583 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:12482583 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:12482583 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:12482583 | pubmed:dateCreated | 2002-12-16 | lld:pubmed |
| pubmed-article:12482583 | pubmed:abstractText | We characterized the neuronal two-domain (95kD-alpha(1)2.1) form of the alpha(1)2.1 subunit of the voltage-gated calcium channels using genetic and molecular analysis. The 95kD-alpha(1)2.1 is absent in neuronal preparations from CACNA1A null mouse demonstrating that alpha(1)2.1 and 95kD-alpha(1)2.1 arise from the same gene. A recombinant two-domain form (alpha(1AI-II)) of alpha(1)2.1 associates with the beta subunit and is trafficked to the plasma membrane. Translocation of the alpha(1AI-II) to the plasma membrane requires association with the beta subunit, since a mutation in the alpha(1AI-II) that inhibits beta subunit association reduces membrane trafficking. Though the alpha(1AI-II) protein does not conduct any voltage-gated currents, we have previously shown that it generates a high density of non-linear charge movements [Ahern et al., Proc. Natl. Acad. Sci. USA 98 (2001) 6935-6940]. In this study, we demonstrate that co-expression of the alpha(1AI-II) significantly reduces the current amplitude of alpha(1)2.1/beta(1a)/alpha(2)delta channels, via competition for the beta subunit. Taken together, our results demonstrate a dual functional role for the alpha(1AI-II) protein, both as a voltage sensor and modulator of P/Q-type currents in recombinant systems. These studies suggest an in vivo role for the 95kD-alpha(1)2.1 in altering synaptic activity via protein-protein interactions and/or regulation of P/Q-type currents. | lld:pubmed |
| pubmed-article:12482583 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12482583 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12482583 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12482583 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12482583 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12482583 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12482583 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12482583 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12482583 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12482583 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12482583 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12482583 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12482583 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12482583 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:12482583 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:12482583 | pubmed:author | pubmed-author:MoriYasuoY | lld:pubmed |
| pubmed-article:12482583 | pubmed:author | pubmed-author:ShinHee-SupHS | lld:pubmed |
| pubmed-article:12482583 | pubmed:author | pubmed-author:CampbellKevin... | lld:pubmed |
| pubmed-article:12482583 | pubmed:author | pubmed-author:FelixRicardoR | lld:pubmed |
| pubmed-article:12482583 | pubmed:author | pubmed-author:ArikkathJyoth... | lld:pubmed |
| pubmed-article:12482583 | pubmed:author | pubmed-author:AhernChristop... | lld:pubmed |
| pubmed-article:12482583 | pubmed:author | pubmed-author:ChenChien-Cha... | lld:pubmed |
| pubmed-article:12482583 | pubmed:author | pubmed-author:CoronadoRober... | lld:pubmed |
| pubmed-article:12482583 | pubmed:author | pubmed-author:SongInseonI | lld:pubmed |
| pubmed-article:12482583 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12482583 | pubmed:day | 18 | lld:pubmed |
| pubmed-article:12482583 | pubmed:volume | 532 | lld:pubmed |
| pubmed-article:12482583 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12482583 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12482583 | pubmed:pagination | 300-8 | lld:pubmed |
| pubmed-article:12482583 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:12482583 | pubmed:meshHeading | pubmed-meshheading:12482583... | lld:pubmed |
| pubmed-article:12482583 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12482583 | pubmed:articleTitle | Molecular characterization of a two-domain form of the neuronal voltage-gated P/Q-type calcium channel alpha(1)2.1 subunit. | lld:pubmed |
| pubmed-article:12482583 | pubmed:affiliation | Howard Hughes Medical Institute, Department of Physiology, University of Iowa College of Medicine, 400 Eckstein Medical Research Building, Iowa City, IA 52242-1101, USA. | lld:pubmed |
| pubmed-article:12482583 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12482583 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12482583 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
