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    Cover picture: Fluorescence of skeletal muscle fibers expressing cDNA for either CFP-YFP-CaV1.1 (top row) or YFP-CaV1.1-CFP (middle and bottom rows). CaV1.1, the “voltage sensor” for excitation–contraction coupling, was localized in transverse tubular membranes (YFP fluorescence indicated in red). Colocalization was observed for CFP (indicated in green) attached to the N terminus but not to the C terminus, consistent with the idea that the C terminus was cleaved and lost from the transverse tubules (see research article by Ohrtman et al., 303–314).

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ISSN 0022-1295
EISSN 1540-7748
In this Issue

Generally Physiological

Commentary

Research Articles

Both the catalytically active and inactive interfacial ATP-binding sites open at least 8 Å during CFTR channel closure.

TMEM16A is an essential component of Ca2+-activated Cl currents in mouse vomeronasal sensory neurons.

The distal C-terminal domain of CaV1.1 is not required for depolarization-induced potentiation of L-type Ca2+ current in skeletal muscle.

Transverse tubule PIP2 modulates Ca2+ release from the SR during EC coupling.

The effects of PIP2 on Slo1 BK channels depend on subunit composition.

Kv1.2’s gating charge is less than Shaker’s, and the specific contributions of charged S4 residues differ, suggesting that the electric field distribution in the Kv1.2 voltage-sensing domain is different than Shaker’s.

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