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Cover Image
Cover Image
Cover picture: The ellipse represents the values of two biophysical parameters that fit available data equally well. This implies large uncertainties in individual parameters (brackets). Despite this uncertainty, combinations of parameters in some directions (stiff) are much more constrained than others (sloppy). This observation can be used to construct new “emergent” parameters that provide insights and predictions not available from the individual parameters (see Research Article by Bohner and Venkataraman, 547–560).
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Research News
Pseudomonas doesn’t mind a dunking
A new study explains Pseudomonas aeruginosa’s strong resistance to osmotic down-shock.
Review
Precision physiology and rescue of brain ion channel disorders
Noebels highlights the importance of cellular and circuit-level context for understanding channelopathies of the brain.
Article
Identifiability, reducibility, and adaptability in allosteric macromolecules
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.
Control of Kir channel gating by cytoplasmic domain interface interactions
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 new mechanism of voltage-dependent gating exposed by KV10.1 channels interrupted between voltage sensor and pore
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.
Tension-activated channels in the mechanism of osmotic fitness in Pseudomonas aeruginosa
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.
