Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer).
Controlling liposome shape, arrangement and dynamics is important for biophysical studies and synthetic biology applications. Now, using a family of reconfigurable DNA nanocages as templates, spherical, tubular, toroidal and helical liposomes with predefined geometry have been produced. DNA-guided membrane fusion and bending is also demonstrated.
Circular dorsal ruffles (CDRs) are important for the vesicular uptake of extracellular matter, but the basis of their wave dynamics is not understood. Here, the authors propose and experimentally test a bistable reaction-diffusion system, which they show accounts for the typical CDR expansion and shrinkage and for aberrant formation of pinned waves and spirals.
Membrane protein diffusion is affected by distinct mechanisms such as molecular crowding and medium elasticity. Here the authors present an analytical approach to analyse single particle trajectories and distinguish mixed subdiffusive processes affecting membrane protein mobility in living cells.
Release of neurotransmitters occurs by opening of a fusion pore in a manner thought to be mediated by SNARE proteins, but whether the fusion pore is a lipidic or a proteinaceous structure is controversial. A new study using very small nanodiscs shows that it is both.
SecY and Sec61 translocons mediate the orderly insertion of transmembrane segments into the lipid bilayer during membrane-protein biogenesis. Reporting in this issue, Ismail et al. now use a SecM-based molecular force sensor to show that the translocon exerts a pulling force on the nascent chain that is capable of mechanical action at two distinct stages of the insertion process.
Single-molecule observations reveal that lipid- and protein-based interactions jointly contribute to the interactions among glycosylphosphatidylinositol-anchored proteins in membranes. Understanding these interactions will help to refine long-evolving (and still debated) models of 'raft' domains in biological membranes.
The extent to which ligand-free GPCRs exist in quasi-stable 'precoupled' complexes with G proteins in vivo is uncertain. New research, using fluorescence recovery after photobleaching (FRAP), reveals a structural requirement for and functional consequences of muscarinic acetylcholine receptor–Gq protein preassembly.