Biochemical studies and molecular dynamics simulations indicate that dephosphroylation of F-BAR protein Cdc15 promotes cytokinesis ring assembly in yeast via conformation change of intrinsically disorder regions and condensate formation.

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.

PX-BAR Mvp1 and dynamin-like GTPase Vps1 drive retromer-independent endosomal recycling.

Single episodes of voluntary exercise induced a functional increase in hippocampal synapses mediated by activity-dependent expression of the BAR protein Mtss1L, acting as a novel early effector of synapse formation.

Ezrin, an important actin-membrane linker, can zip adjacent membranes, be enriched to positively-curved membranes when phosphorylated and to negatively-curved membranes through a direct interaction with membrane curvature sensor I-BAR domain proteins.

Cell stretch release generates plasma membrane (PM) evaginations of ≈100 nm, triggering a local event of actin polymerization that flattens and recovers PM shape.

The formation of HIV-1 particles requires a bending of the membrane that cannot be achieved by the Gag protein alone and thus there is need for the I-BAR protein IRSp53 to aid in the formation of HIV-1 buds.

The BAR protein endophilin spaces out turns of the dynamin helix, blocking its active conformational change and membrane fission.

A combination of light and electron microscopy data provide new insights into the dynamic architecture and the function of the endocytic protein machinery in relation to membrane shape changes in vivo.

The Time Point Selection (or TPS) method is a general protocol for determining sampling rates for high throughout time series biological studies, that is efficient, cheap, scalable and works well for several different types of molecular data.