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.
ER-stress sensing mechanism of the unfolded protein response sensor/transducer IRE1 is conserved from yeast to mammals, where in mammals, unfolded protein binding to IRE1's ER lumenal domain is coupled to its oligomerization and activation through an allosteric conformational change.
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.
Insights into the basic metabolic architecture and adaptations of malaria parasites for growth within human erythrocytes exemplify how incisive knowledge of biochemical pathways and mechanisms may be leveraged to develop new therapies.
Whole endosome recording shows that chloride interacts with vesicular glutamate transporters as both allosteric activator and permeant ion, and although the mode of permeation differs, chloride and glutamate use a related conduction pathway.
Biochemical and biological studies reveal that caspases feed back onto the Unfolded Protein Response by cleaving the ER-stress sensor IRE1 to produce a cytoprotective N-terminal fragment that inhibits BAX-dependent apoptosis.