| pubmed-article:11296298 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11296298 | lifeskim:mentions | umls-concept:C0330390 | lld:lifeskim |
| pubmed-article:11296298 | lifeskim:mentions | umls-concept:C0033634 | lld:lifeskim |
| pubmed-article:11296298 | lifeskim:mentions | umls-concept:C0086376 | lld:lifeskim |
| pubmed-article:11296298 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:11296298 | lifeskim:mentions | umls-concept:C1709059 | lld:lifeskim |
| pubmed-article:11296298 | lifeskim:mentions | umls-concept:C0234112 | lld:lifeskim |
| pubmed-article:11296298 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
| pubmed-article:11296298 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:11296298 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:11296298 | pubmed:dateCreated | 2001-4-11 | lld:pubmed |
| pubmed-article:11296298 | pubmed:abstractText | N-type and P/Q-type Ca(2+) channels are inhibited by neurotransmitters acting through G protein-coupled receptors in a membrane-delimited pathway involving Gbetagamma subunits. Inhibition is caused by a shift from an easily activated "willing" (W) state to a more-difficult-to-activate "reluctant" (R) state. This inhibition can be reversed by strong depolarization, resulting in prepulse facilitation, or by protein kinase C (PKC) phosphorylation. Comparison of regulation of N-type Ca(2+) channels containing Cav2.2a alpha(1) subunits and P/Q-type Ca(2+) channels containing Ca(v)2.1 alpha(1) subunits revealed substantial differences. In the absence of G protein modulation, Ca(v)2.1 channels containing Ca(v)beta subunits were tonically in the W state, whereas Ca(v)2.1 channels without beta subunits and Ca(v)2.2a channels with beta subunits were tonically in the R state. Both Ca(v)2.1 and Ca(v)2.2a channels could be shifted back toward the W state by strong depolarization or PKC phosphorylation. Our results show that the R state and its modulation by prepulse facilitation, PKC phosphorylation, and Ca(v)beta subunits are intrinsic properties of the Ca(2+) channel itself in the absence of G protein modulation. A common allosteric model of G protein modulation of Ca(2+)-channel activity incorporating an intrinsic equilibrium between the W and R states of the alpha(1) subunits and modulation of that equilibrium by G proteins, Ca(v)beta subunits, membrane depolarization, and phosphorylation by PKC accommodates our findings. Such regulation will modulate transmission at synapses that use N-type and P/Q-type Ca(2+) channels to initiate neurotransmitter release. | lld:pubmed |
| pubmed-article:11296298 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11296298 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11296298 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296298 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11296298 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:11296298 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:11296298 | pubmed:author | pubmed-author:CatterallW... | lld:pubmed |
| pubmed-article:11296298 | pubmed:author | pubmed-author:HerlitzeSS | lld:pubmed |
| pubmed-article:11296298 | pubmed:author | pubmed-author:ScheuerTT | lld:pubmed |
| pubmed-article:11296298 | pubmed:author | pubmed-author:ZhongHH | lld:pubmed |
| pubmed-article:11296298 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11296298 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:11296298 | pubmed:volume | 98 | lld:pubmed |
| pubmed-article:11296298 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11296298 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11296298 | pubmed:pagination | 4699-704 | lld:pubmed |
| pubmed-article:11296298 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:11296298 | pubmed:meshHeading | pubmed-meshheading:11296298... | lld:pubmed |
| pubmed-article:11296298 | pubmed:meshHeading | pubmed-meshheading:11296298... | lld:pubmed |
| pubmed-article:11296298 | pubmed:meshHeading | pubmed-meshheading:11296298... | lld:pubmed |
| pubmed-article:11296298 | pubmed:meshHeading | pubmed-meshheading:11296298... | lld:pubmed |
| pubmed-article:11296298 | pubmed:meshHeading | pubmed-meshheading:11296298... | lld:pubmed |
| pubmed-article:11296298 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11296298 | pubmed:articleTitle | Allosteric modulation of Ca2+ channels by G proteins, voltage-dependent facilitation, protein kinase C, and Ca(v)beta subunits. | lld:pubmed |
| pubmed-article:11296298 | pubmed:affiliation | Department of Pharmacology, University of Washington, Seattle, WA 98195-7280, USA. | lld:pubmed |
| pubmed-article:11296298 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11296298 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11296298 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11296298 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11296298 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11296298 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11296298 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11296298 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11296298 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11296298 | lld:pubmed |
