Purified Pannexin 1 channels activated by caspase cleavage in proteoliposomes reconstitute a permeation pathway for intercellular signaling molecules important in inflammation and cell clearance.
The tethering complex HOPS employs affinity for each of the 4 SNAREs to catalyze assembly of 3-SNARE intermediates, supporting an immediate burst of membrane fusion triggered by the 4th SNARE.
The high-resolution x-ray structure of an asymmetrical SeCitS dimer, present in the inward- and outward-facing state, provides a complete mechanism of substrate and ion translocation in a sodium-dependent symporter.
Rigorous assays of membrane fusion show that a distinct tethering step is required for lumenal compartment mixing in a manner that extends beyond simply increasing the amount of total trans-SNARE complex.
A method for determining how many ions are required to drive transport in an electrogenic secondary active transporter will help understand the mechanisms of bacterial transporters whose structures have been solved.
Sec17 is shown to have divergent effects on pre-fusion SNARE complex activity, depending on the state of SNARE zippering and HOPS, an SM-tether complex, controls the outcome of Sec17-SNARE engagement.
Discovery of the structural basis for recognition and uptake of a human precursor for body odour production reveals an important role for bacterial peptide transport and novel routes to prevent its production in humans.
A simple, yet elegant method for robust self-assembly of diverse membrane proteins into soluble peptide nanoparticles for their structural and functional analysis in detergent-free solutions.
Solid state NMR is unable to detect any association of substrate to the second binding site, S2, in the extracellular vestibule of the Neurotransmitter:Sodium Symporter LeuT.
