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• W2893174243 abstract "Significance Voltage-gated Ca 2+ (Ca V ) channels have an α1-α2δ core complexed with one of several alternative β subunits. Contradictory evidence says that, once bound, ( i ) a β subunit is permanently associated with the α1-α2δ core or ( ii ) that it is free to be exchanged for other β subunits. We designed rapamycin-translocatable Ca V β subunits that allow drug-induced sequestration of free β subunits to several organelle anchors. Sequestering free subunits does not dissociate bound subunits from channels except when the binding site is mutated to weaken the interaction. Nevertheless, our rapamycin constructs show that, when nontranslocatable β subunits are coexpressed with a translocatable subunit, sequestering the translocatable subunit changes the channel properties, revealing a quick replacement by the nontranslocatable subunit in the channel complex." @default.
• W2893174243 created "2018-10-05" @default.
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• W2893174243 date "2018-09-26" @default.
• W2893174243 modified "2023-09-23" @default.
• W2893174243 title "Translocatable voltage-gated Ca ²⁺ channel β subunits in α1–β complexes reveal competitive replacement yet no spontaneous dissociation" @default.
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• W2893174243 doi "https://doi.org/10.1073/pnas.1809762115" @default.
• W2893174243 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6196550" @default.
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• W2893174243 hasPublicationYear "2018" @default.
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