Essential Cavβ modulatory properties are AID-independent
- 6 March 2005
- journal article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 12 (4), 372-377
- https://doi.org/10.1038/nsmb909
Abstract
Voltage-gated Ca(2+) channel beta (Ca(v)beta) subunits have a highly conserved core consisting of interacting Src homology 3 and guanylate kinase domains, and are postulated to exert their effects through AID, the major interaction site in the pore-forming alpha(1) subunit. This stereotypical interaction does not explain how individual Ca(v)beta subunits modulate alpha(1) subunits differentially. Here we show that AID is neither necessary nor sufficient for critical Ca(v)beta regulatory properties. Complete modulation depends on additional contacts that are exclusive of AID and not revealed in recent crystal structures. These data offer a new context for understanding Ca(v)beta modulation, suggesting that the AID interaction orients the Ca(v)beta core so as to permit additional isoform-specific Ca(v)alpha(1)-Ca(v)beta interactions that underlie the particular regulation seen with each Ca(v)alpha(1)-Ca(v)beta pair, rather than as the main site of regulation.Keywords
This publication has 22 references indexed in Scilit:
- Structural basis of the α1–β subunit interaction of voltage-gated Ca2+ channelsNature, 2004
- Structure of a complex between a voltage-gated calcium channel β-subunit and an α-subunit domainNature, 2004
- Structural Analysis of the Voltage-Dependent Calcium Channel β Subunit Functional Core and Its Complex with the α1 Interaction DomainNeuron, 2004
- Membrane-associated guanylate kinase-like properties of β-subunits required for modulation of voltage-dependent Ca 2+ channelsProceedings of the National Academy of Sciences, 2004
- Calcium Channel Function Regulated by the SH3-GK Module in β SubunitsNeuron, 2004
- The Voltage-dependent Calcium Channel β Subunit Contains Two Stable Interacting DomainsPublished by Elsevier ,2003
- Subunits of Voltage-Gated Calcium ChannelsJournal of Bioenergetics and Biomembranes, 2003
- Structure and Regulation of Voltage-Gated Ca2+ ChannelsAnnual Review of Cell and Developmental Biology, 2000
- Complexes of the α1C and β Subunits Generate the Necessary Signal for Membrane Targeting of Class C L-type Calcium ChannelsPublished by Elsevier ,1999
- Calcium channel β-subunit binds to a conserved motif in the I–II cytoplasmic linker of the α1-subunitNature, 1994