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Cover Image
Cover Image
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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Generally Physiological
Commentary
Article
Cysteine accessibility probes timing and extent of NBD separation along the dimer interface in gating CFTR channels
Both the catalytically active and inactive interfacial ATP-binding sites open at least 8 Å during CFTR channel closure.
Conditional knockout of TMEM16A/anoctamin1 abolishes the calcium-activated chloride current in mouse vomeronasal sensory neurons
TMEM16A is an essential component of Ca2+-activated Cl− currents in mouse vomeronasal sensory neurons.
Apparent lack of physical or functional interaction between CaV1.1 and its distal C terminus
The distal C-terminal domain of CaV1.1 is not required for depolarization-induced potentiation of L-type Ca2+ current in skeletal muscle.
Depression of voltage-activated Ca2+ release in skeletal muscle by activation of a voltage-sensing phosphatase
Transverse tubule PIP2 modulates Ca2+ release from the SR during EC coupling.
Two distinct effects of PIP2 underlie auxiliary subunit-dependent modulation of Slo1 BK channels
The effects of PIP2 on Slo1 BK channels depend on subunit composition.
Voltage-dependent gating and gating charge measurements in the Kv1.2 potassium channel
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.
