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• W2006989095 abstract "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 Gβγ 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 α 1 subunits and P/Q-type Ca 2+ channels containing Ca v 2.1 α 1 subunits revealed substantial differences. In the absence of G protein modulation, Ca v 2.1 channels containing Ca v β subunits were tonically in the W state, whereas Ca v 2.1 channels without β subunits and Ca v 2.2a channels with β 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 β 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 α 1 subunits and modulation of that equilibrium by G proteins, Ca v β 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." @default.
• W2006989095 created "2016-06-24" @default.
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• W2006989095 date "2001-04-10" @default.
• W2006989095 modified "2023-09-30" @default.
• W2006989095 title "Allosteric modulation of Ca ²⁺ channels by G proteins, voltage-dependent facilitation, protein kinase C, and Ca _v β subunits" @default.
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• W2006989095 doi "https://doi.org/10.1073/pnas.051628998" @default.
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