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A new study explains Pseudomonas aeruginosa’s strong resistance to osmotic down-shock.


Noebels highlights the importance of cellular and circuit-level context for understanding channelopathies of the brain.


Bohner and Venkataraman propose a link between the sensitivity of allosteric macromolecules to their underlying biophysical parameters, the interrelationships between these parameters, and macromolecular adaptability. They argue that “emergent” combinations of parameters yield mechanistic insight that individual parameters cannot.

The pore-forming unit of ATP-sensitive K channels is composed of four Kir6.2 subunits. Borschel et al. show that salt bridges between the cytoplasmic domain of adjacent Kir6.2 subunits determine the degree to which channels inactivate after removal of ATP.

A linker that connects the voltage-sensing domain and pore domain in voltage-gated K+ channels is thought to provide coupling during gating, but this view has been challenged in KCNH channels. Tomczak et al. investigate gating in KV10.1 channels with disrupted linkers and reveal multiple mechanisms.

Pseudomonas aeruginosa is resistant to drastic osmotic changes because of its ability to quickly jettison small osmolytes through osmotic release channels. Çetiner et al. reveal that it uses one MscL-like and at least two types of MscS-like channels during its osmotic response.

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