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Issues

ISSN 0022-1295
EISSN 1540-7748
In this Issue

Editorial

Welcome from new Editor-in-Chief

Research News

JGP study suggests how the regulatory protein γ8 reopens AMPA receptor channels in the continued presence of glutamate.

Commentaries

Grabe et al. celebrate a new mathematical model of the multidrug transporter EmrE, constructed from NMR and stop flow kinetic data.

Moss considers recent work describing the effect of low temperature on force development in skeletal muscle.

Viewpoint

Ion transporters can be strongly regulated by autoinhibitory reactions that depend on ion binding within their transport sites.

Research Articles

Secondary active transport mechanisms often depict a limited number of states and transitions, although recent research suggests that alternative “leak” pathways are not always minor. Hussey et al. numerically simulate a fully unrestricted model for the bacterial transporter EmrE and demonstrate that highly efficient transport can be achieved despite the existence of multiple leak pathways.

Molecular bases of pathogenic enhancement of Ca2+ release channel activities in RYR1 carrying disease-associated mutations at the N-terminal region were studied. Functional studies and MD simulation revealed that the interactions between domains have a strong correlation with channel activity.

CRAC channels contain a cluster of positively charged residues in the inner pore whose function is not understood. Here, we show that these positive charges promote pore opening by enhancing hydration of the hydrophobic gate located at the outer end of the pore.

This paper presents the crystal structure of a forced open inward rectifier Kir2.2 channel. Molecular dynamics reveals the details of ion permeation through the open channel.

Using single-channel recordings and single-molecule FRET, Carrillo et al. show that resensitization of α-amino-5-methyl-3-hydroxy-4-isoxazole propionate receptors by the regulatory protein γ8 is characterized by transitions to high conductance levels associated with tighter conformational coupling similar to those seen in the presence of cyclothiazide.

Correction

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