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- W2106670791 abstract "Two processes dominate voltage-gated calcium channel (CaV) inactivation: voltage-dependent inactivation (VDI) and calcium-dependent inactivation (CDI). The CaVβ/CaVα1-I-II loop and Ca2+/calmodulin (CaM)/CaVα1–C-terminal tail complexes have been shown to modulate each, respectively. Nevertheless, how each complex couples to the pore and whether each affects inactivation independently have remained unresolved. Here, we demonstrate that the IS6–α-interaction domain (AID) linker provides a rigid connection between the pore and CaVβ/I-II loop complex by showing that IS6-AID linker polyglycine mutations accelerate CaV1.2 (L-type) and CaV2.1 (P/Q-type) VDI. Remarkably, mutations that either break the rigid IS6-AID linker connection or disrupt CaVβ/I-II association sharply decelerate CDI and reduce a second Ca2+/CaM/CaVα1–C-terminal–mediated process known as calcium-dependent facilitation. Collectively, the data strongly suggest that components traditionally associated solely with VDI, CaVβ and the IS6-AID linker, are essential for calcium-dependent modulation, and that both CaVβ-dependent and CaM-dependent components couple to the pore by a common mechanism requiring CaVβ and an intact IS6-AID linker." @default.
- W2106670791 created "2016-06-24" @default.
- W2106670791 creator A5045437602 @default.
- W2106670791 creator A5075337100 @default.
- W2106670791 date "2009-02-23" @default.
- W2106670791 modified "2023-10-03" @default.
- W2106670791 title "Disruption of the IS6-AID Linker Affects Voltage-gated Calcium Channel Inactivation and Facilitation" @default.
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- W2106670791 doi "https://doi.org/10.1085/jgp.200810143" @default.
- W2106670791 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2812501" @default.
- W2106670791 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19237593" @default.
- W2106670791 hasPublicationYear "2009" @default.
- W2106670791 type Work @default.