Cryo-EM structures of actomyosin VI in multiple nucleotide states reveal a unique actin-myosin interface and a mechanism of force-sensitivity; furthermore, myosin VI remodels F-actin, suggesting a role for actin structural plasticity during force generation.

Analysis of the mechanism of action of cystic fibrosis corrector drugs reveals signalling pathways potently controlling the proteostasis of the main disease-relevant CFTR mutant.

Motivational coupling of action to reward and inhibition to punishment is subserved by dissociable learning and choice processes, and is modulated by dopamine/noradrenaline transporter blockade.

Using linked TOG domains that each bind a curved conformation of αβ-tubulin, a microtubule polymerase catalyzes fast elongation by concentrating αβ-tubulin near the polymer end.

Structural, computational and functional approaches reveal the role of an extended acidic chamber near the nucleotide binding site in activation of P2X3 receptor channels by divalent-bound ATP.

A common mechanism for computation of direction selectivity in the ON and OFF channel is demonstrated.

In potassium-dependent NTPases, insertion of the activating potassium ion into the active site leads to rotation of the gamma-phosphate yielding a near-eclipsed, catalytically productive conformation of the triphosphate chain.

Drugs called bisphosphonates are used to treat a range of bone diseases, but how do they reach the enzymes that are their target?

An unbiased genetic screen in human cells shows that the molecular target of a natural product with promising anticancer activity is a membrane phospholipid.

Identification of a transporter complex comprised of SLC37A3 and ATRAID is required for nitrogen-containing bisphosphonates to enter the cytosol from lysosomes and exert their therapeutic effects on bone.