| pubmed-article:15953418 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15953418 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:15953418 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:15953418 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
| pubmed-article:15953418 | lifeskim:mentions | umls-concept:C1709061 | lld:lifeskim |
| pubmed-article:15953418 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:15953418 | pubmed:dateCreated | 2005-6-14 | lld:pubmed |
| pubmed-article:15953418 | pubmed:abstractText | Voltage-dependent G protein (Gbetagamma) inhibition of N-type (CaV2.2) channels supports presynaptic inhibition and represents a central paradigm of channel modulation. Still controversial are the proposed determinants for such modulation, which reside on the principal alpha1B channel subunit. These include the interdomain I-II loop (I-II), the carboxy tail (CT), and the amino terminus (NT). Here, we probed these determinants and related mechanisms, utilizing compound-state analysis with yeast two-hybrid and mammalian cell FRET assays of binding among channel segments and G proteins. Chimeric channels confirmed the unique importance of NT. Binding assays revealed selective interaction between NT and I-II elements. Coexpressing NT peptide with Gbetagamma induced constitutive channel inhibition, suggesting that the NT domain constitutes a G protein-gated inhibitory module. Such inhibition was limited to NT regions interacting with I-II, and G-protein inhibition was abolished within alpha1B channels lacking these NT regions. Thus, an NT module, acting via interactions with the I-II loop, appears fundamental to such modulation. | lld:pubmed |
| pubmed-article:15953418 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15953418 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15953418 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15953418 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15953418 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15953418 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15953418 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15953418 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15953418 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15953418 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15953418 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15953418 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15953418 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:15953418 | pubmed:issn | 0896-6273 | lld:pubmed |
| pubmed-article:15953418 | pubmed:author | pubmed-author:EvansJenaferJ | lld:pubmed |
| pubmed-article:15953418 | pubmed:author | pubmed-author:YueDavid TDT | lld:pubmed |
| pubmed-article:15953418 | pubmed:author | pubmed-author:ColecraftHenr... | lld:pubmed |
| pubmed-article:15953418 | pubmed:author | pubmed-author:AglerHeather... | lld:pubmed |
| pubmed-article:15953418 | pubmed:author | pubmed-author:TayLai HockLH | lld:pubmed |
| pubmed-article:15953418 | pubmed:author | pubmed-author:AndersonMolly... | lld:pubmed |
| pubmed-article:15953418 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15953418 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:15953418 | pubmed:volume | 46 | lld:pubmed |
| pubmed-article:15953418 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15953418 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15953418 | pubmed:pagination | 891-904 | lld:pubmed |
| pubmed-article:15953418 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:15953418 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15953418 | pubmed:articleTitle | G protein-gated inhibitory module of N-type (ca(v)2.2) ca2+ channels. | lld:pubmed |
| pubmed-article:15953418 | pubmed:affiliation | Department of Biomedical Engineering and Ca2+ Signals Laboratory, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA. | lld:pubmed |
| pubmed-article:15953418 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15953418 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:15953418 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15953418 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:15953418 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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