Profiling the phospho-status of the BKCa channel alpha subunit in rat brain reveals unexpected patterns and complexity.

ABSTRACT: Molecular diversity of ion channel structure and function underlies variability in electrical signaling in nerve, muscle, and non-excitable cells. Protein phosphorylation and alternative splicing of pre-mRNA are two important mechanisms to generate structural and functional diversity of ion channels. However, systematic mass spectrometric analyses of in vivo phosphorylation and splice variants of ion channels in native tissues are largely lacking. Mammalian large-conductance calcium-activated potassium (BK(Ca)) channels are tetramers of alpha subunits (BKalpha) either alone or together with beta subunits, exhibit exceptionally large single channel conductance, and are dually activated by membrane depolarization and intracellular Ca(2+). The cytoplasmic C terminus of BKalpha is subjected to

SUBMITTER: Yan J 

PROVIDER: S-EPMC2577206 | biostudies-literature | 2008 Nov

REPOSITORIES: biostudies-literature