Chongyuan Wang, Agata Jacewicz ... Stephen Barstow Long
Cryo-EM structures reveal that MICU1-MICU2 operates like a regulatable toxin to block the pore of the mitochondrial calcium uniporter and confer Ca2+-dependent control.
Katherine E Huffer, Antoniya A Aleksandrova ... Kenton J Swartz
Structure-based alignment of TRP channels enables comparison of structural changes, ion permeation pathways and ligand-binding sites and reveals over-representation of structures that represent non-conducting states.
Tone Bengtsen, Viktor L Holm ... Kresten Lindorff-Larsen
Molecular simulations, small-angle X-ray and neutron scattering experiments and previously measured NMR experiments were combined to study the structure and dynamics of the proteins and lipids in a nanodisc.
Structure of the Mrp antiporter, an ancestor of respiratory complex I, suggests a mechanism of coupling between cation and proton translocation, applicable to a large family of related membrane proteins.
Sigrid Noreng, Richard Posert ... Isabelle Baconguis
The in-depth structural and functional work provide a deeper understanding as to how the epithelial sodium channel is a heteromeric ion channel that is regulated by Na+ and proteolysis.
Changes to cellular protein homeostasis reveal widespread advantageous effects of destabilizing mutations, opening the possibility to switch mutational landscapes back-and-forth from permissive to restrictive.
Efficient nuclear transport of very large biomolecules, relevant for viral transport, scales non-linearly with size and its kinetics can be explained by a simple two-parameter energetic model.
Computation and experiment together demonstrate that nonspecific membrane–protein interactions could regulate transmembrane protein function and suggest that covalent linkers can be an integral component of the sensing apparatus.