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Structure-function analyses reveal the mechanistic underpinnings of inside-out transmembrane signaling that controls periplasmic proteolysis, and thereby biofilm formation, in bacteria and may be relevant in the context of other signaling proteins with similar control elements.

The ER membrane protein complex promotes the biogenesis of a subset multipass membrane proteins enriched for transporters and other proteins with destabilizing features in transmembrane domains.

A small molecule, cotransin, blocks transmembrane domains form integrating into cell membranes by allosterically ‘locking’ the lateral gate of the Sec61 translocation channel.

The sensory regulatory system of the cholera causative involves the detection of bile acids by direct interaction with the inner membrane protein complex formed by ToxR and ToxS, thereby inducing concentration-dependent structural changes.

The structure of a voltage-activated potassium channel in lipid nanodiscs solved using cryo-electron microscopy is similar to previous X-ray structures, and provides insights into the mechanism of C-type inactivation.

Structure-function characterization of the EMC's cytoplasmic, transmembrane, and lumenal domains reveal features critical for terminal helix insertion and a specialized role for the lumenal domain in polytopic membrane protein biogenesis.

A transport mechanism is uncovered in the major drug-efflux system in E. coli involving two remote alternating-access conformational cycles, which could provide the basis for the development of allosteric inhibitors against multidrug resistance.

Eutherian CD4 evolved counterbalancing motifs in the extracellular, transmembrane, and intracellular domains that regulate CD4⁺ T cell responses to peptide antigens presented by class II MHC (pMHCII).

Molecular dynamics simulation of the full-length TSH receptor, a major human autoantigen whose full structure remains uncertain, showed that its linker region is an intrinsically disordered protein, explaining the difficulty of obtaining an experimental structure.

Mutational analysis and biochemical experiments suggest that the conserved β-hairpin-like membrane-reentrant loop of RseP - an S2P family intramembrane cleaving protease - helps to discriminate substrates by directly interacting with their transmembrane segments.