Uniform diameter and curvature of the outer membrane extensions and vesicles of Shewanella oneidensis are maintained by a bacterial Bin/Amphiphysin/Rvs (BAR) domain-like protein BdpA.

Compared to other isoforms of RAS, KRAS4b has unique membrane diffusion behavior related to its biology, and the two major domains of the protein both contribute to this diffusion behavior.

Two domains of the peripheral membrane protein Tim44 interact with two different sectors of a translocase to coordinate the translocation of proteins across the inner mitochondrial membrane.

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.

When the Ca²⁺-binding loops of the C2B domain insert into a membrane, interactions with a phospholipid and the SNARE complex allow synaptotagmin-1 to bend the membrane.

Combination of actin and curly on lipid membranes constitutes a new, minimalistic system to generate high curvature actin rings that can contract upon the action of myosin II filaments.

The nanoscopic landscape of the membrane has a direct impact on the spatiotemporal, and likely also the signaling, dynamics of Ras proteins.

A new structure reveals two Arf-GEF regulatory domains form a single structural unit that stimulates Arf-GEF activity.

Direct measurements of trafficking kinetics between organelles of the secretory pathway suggest that lipid-driven membrane domains laterally sort proteins during membrane traffic.

The dynamic structure of respiratory complex I from mesophilic bacterium is revealed and demonstrates existence of uncoupled conformations in the bacterial complex.