Abstract
Different post-translational modifications of Ca channel beta subunits have been identified. Recent studies have characterized the palmitoylation of the Ca channel beta2a subunit, as well as one effect of this modification on channel function. The potential importance of palmitoylation on other channel properties is discussed. Other studies have addressed the role of phosphorylation of beta subunits in the regulation of voltage-dependent Ca channels. Phosphorylation of beta subunits by second messenger-activated protein kinases, as well as by unidentified protein kinases, may affect interactions between channel subunits and other aspects of channel function. The differential modification of Ca channel beta subunit isoforms by post-translational events likely results in diversely regulated channels with unique properties.
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