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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0086376,
umls-concept:C0330390,
umls-concept:C0439799,
umls-concept:C0443199,
umls-concept:C0521390,
umls-concept:C0521449,
umls-concept:C0596235,
umls-concept:C0680730,
umls-concept:C1148554,
umls-concept:C1521991,
umls-concept:C1552644,
umls-concept:C1704675,
umls-concept:C1711351,
umls-concept:C1823153,
umls-concept:C2003941,
umls-concept:C2349976
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pubmed:issue |
28
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pubmed:dateCreated |
1998-8-6
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pubmed:abstractText |
Interactions of G-protein alpha (Galpha) and beta gamma subunits (Gbeta gamma) with N- (alpha1B) and P/Q-type (alpha1A) Ca2+ channels were investigated using the Xenopus oocyte expression system. Gi3alpha was found to inhibit both N- and P/Q-type channels by receptor agonists, whereas Gbeta1 gamma2 was responsible for prepulse facilitation of N-type channels. L-type channels (alpha1C) were not regulated by Galpha or Gbeta gamma. For N-type, prepulse facilitation mediated via Gbeta gamma was impaired when the cytoplasmic I-II loop (loop 1) was deleted or replaced with the alpha1C loop 1. Galpha-mediated inhibitions were also impaired by substitution of the alpha1C loop 1, but only when the C terminus was deleted. For P/Q-type, by contrast, deletion of the C terminus alone diminished Galpha-mediated inhibition. Moreover, a chimera of L-type with the alpha1B loop 1 gained Gbeta gamma-dependent facilitation, whereas an L-type chimera with the N- or P/Q-type C terminus gained Galpha-mediated inhibition. These findings provide evidence that loop 1 of N-type channels is a regulatory site for Gbeta gamma and the C termini of P/Q- and N-types for Galpha.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
273
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
17585-94
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9651353-Animals,
pubmed-meshheading:9651353-Base Sequence,
pubmed-meshheading:9651353-Calcium Channels,
pubmed-meshheading:9651353-Cytoplasm,
pubmed-meshheading:9651353-GTP-Binding Proteins,
pubmed-meshheading:9651353-Neurons,
pubmed-meshheading:9651353-Oligodeoxyribonucleotides,
pubmed-meshheading:9651353-Rabbits,
pubmed-meshheading:9651353-Recombinant Proteins,
pubmed-meshheading:9651353-Xenopus
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pubmed:year |
1998
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pubmed:articleTitle |
Differential interactions of the C terminus and the cytoplasmic I-II loop of neuronal Ca2+ channels with G-protein alpha and beta gamma subunits. I. Molecular determination.
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pubmed:affiliation |
Department of Neurochemistry, Tokyo Institute of Psychiatry, 2-1-8 Kamikitazawa, Setagaya-ku, Tokyo 156, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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