FEBS Lett 1993 Jul 12;3261-3:21-4.

A molecular basis for gating mode transitions in human skeletal muscle Na+ channels.

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Recombinant sodium channel alpha subunits expressed in Xenopus oocytes display an anomalously slow rate of inactivation that arises from channels that predominantly exist in a slow gating mode [1,2]. Co-expression of Na+ channel beta 1 subunit with the human skeletal muscle Na+ channel alpha subunit increases the Na+ current and induces normal gating behavior in Xenopus laevis oocytes. The effects of the beta 1 subunit can be explained by an allosterically induced conformational switch of the alpha subunit protein that occurs upon binding the beta 1 subunit. This binding alters the free energy barriers separating distinct conformational states of the channel. The results illustrate a fundamental modulation of ion channel gating at the molecular level, and specifically demonstrate the importance of the beta 1 subunit for gating mode changes of Na+ channels.

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