Key result
Phosphoprotein phosphatases 1, 2A, and calcineurin selectively dephosphorylate different phosphorylation sites on the alpha 1 and beta subunits of skeletal muscle calcium channels.
The study demonstrates that the three principal serine/threonine phosphoprotein phosphatases selectively dephosphorylate different sites on the alpha 1 and beta subunits of skeletal muscle calcium channels.
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No immediate clinical implications; leaves open phosphatase selectivity as a regulatory mechanism pending in vivo validation.
Lai et al. (1993) studied this question. Phosphoprotein phosphatases (PP1, PP2A, calcineurin) was evaluated on Dephosphorylation rates and selectivity of alpha 1 and beta subunits. Phosphoprotein phosphatases 1, 2A, and calcineurin selectively dephosphorylate different phosphorylation sites on the alpha 1 and beta subunits of skeletal muscle calcium channels.
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