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• W2016528031 abstract "N-type Ca 2+ channels can be inhibited by neurotransmitter-induced release of G protein βγ subunits. Two isoforms of Ca v 2.2 α1 subunits of N-type calcium channels from rat brain (Ca v 2.2a and Ca v 2.2b; initially termed rbB-I and rbB-II) have different functional properties. Unmodulated Ca v 2.2b channels are in an easily activated “willing” ( W ) state with fast activation kinetics and no prepulse facilitation. Activating G proteins shifts Ca v 2.2b channels to a difficult to activate “reluctant” ( R ) state with slow activation kinetics; they can be returned to the W state by strong depolarization resulting in prepulse facilitation. This contrasts with Ca v 2.2a channels, which are tonically in the R state and exhibit strong prepulse facilitation. Activating or inhibiting G proteins has no effect. Thus, the R state of Ca v 2.2a and its reversal by prepulse facilitation are intrinsic to the channel and independent of G protein modulation. Mutating G177 in segment IS3 of Ca v 2.2b to E as in Ca v 2.2a converts Ca v 2.2b tonically to the R state, insensitive to further G protein modulation. The converse substitution in Ca v 2.2a, E177G, converts it to the W state and restores G protein modulation. We propose that negatively charged E177 in IS3 interacts with a positive charge in the IS4 voltage sensor when the channel is closed and produces the R state of Ca v 2.2a by a voltage sensor-trapping mechanism. G protein βγ subunits may produce reluctant channels by a similar molecular mechanism." @default.
• W2016528031 created "2016-06-24" @default.
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• W2016528031 date "2001-04-10" @default.
• W2016528031 modified "2023-10-17" @default.
• W2016528031 title "Control of gating mode by a single amino acid residue in transmembrane segment IS3 of the N-type Ca ²⁺ channel" @default.
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• W2016528031 doi "https://doi.org/10.1073/pnas.051629098" @default.
• W2016528031 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/31898" @default.
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