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XB-ART-8552
Biophys J September 1, 2001; 81 (3): 1439-51.

Evidence for two concentration-dependent processes for beta-subunit effects on alpha1B calcium channels.

Cantí C , Davies A , Berrow NS , Butcher AJ , Page KM , Dolphin AC .


Abstract
beta-Subunits of voltage-dependent Ca(2+) channels regulate both their expression and biophysical properties. We have injected a range of concentrations of beta3-cDNA into Xenopus oocytes, with a fixed concentration of alpha1B (Ca(V)2.2) cDNA, and have quantified the corresponding linear increase of beta3 protein. The concentration dependence of a number of beta3-dependent processes has been studied. First, the dependence of the a1B maximum conductance on beta3-protein occurs with a midpoint around the endogenous concentration of beta3 (approximately 17 nM). This may represent the interaction of the beta-subunit, responsible for trafficking, with the I-II linker of the nascent channel. Second, the effect of beta3-subunits on the voltage dependence of steady-state inactivation provides evidence for two channel populations, interpreted as representing alpha1B without or with a beta3-subunit, bound with a lower affinity of 120 nM. Third, the effect of beta3 on the facilitation rate of G-protein-modulated alpha1B currents during a depolarizing prepulse to +100 mV provides evidence for the same two populations, with the rapid facilitation rate being attributed to Gbetagamma dissociation from the beta-subunit-bound alpha1B channels. The data are discussed in terms of two hypotheses, either binding of two beta-subunits to the alpha1B channel or a state-dependent alteration in affinity of the channel for the beta-subunit.

PubMed ID: 11509358
PMC ID: PMC1301623
Article link: Biophys J

Genes referenced: cacna1b

References [+] :
Baylor, Calcium release and sarcoplasmic reticulum membrane potential in frog skeletal muscle fibres. 1984, Pubmed


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