Quantitative 3D lattice light sheet microscopy of unperturbed cells combined with electron tomography and acute loss of function experiments reveals how dynamic ESCRT-III/Vps4 assemblies succeed in reverse membrane budding on endosomes.
Single molecule microscopy combined with biochemical analyses show that a two-step lipid-binding mechanism of the SRP receptor balances the trade-off between speed and specificity during co-translational protein targeting.
Biophysical and functional data strongly support the notion that Munc18-1 acts as a template to assemble the neuronal SNARE complex, and that inhibition of this activity underlies diverse forms of regulation of neurotransmitter release.
Sodium ions control the rates of both substrate binding and dissociation of an archaeal homologue of glutamate transporters in a manner that minimizes binding intermediates and maximizes transport efficiency.
A post-lysosomal cholesterol transport inhibitor reveals how the endoplasmic reticulum membrane regulates total cellular cholesterol by constantly monitoring a critical pool of cholesterol in the plasma membrane.
A single-nucleotide I232T polymorphic change in FcγRIIB's transmembrane domain bends FcγRIIB's ectodomains toward cell membrane to allosterically hinder FcγRIIB's ligand association, providing novel molecular mechanism for functional loss of FcγRIIB-I232T.