Building on previous work (Mysling et al., 2016), it is shown that angiopoietin-like protein 4 (ANGPTL4) inhibits lipoprotein lipase activity by catalyzing the unfolding of its hydrolase domain.
Adapting a cytosolic enzyme that breaks down glutathione to function in the lumen of the endoplasmic reticulum challenges the long-held view that reduced glutathione fuels disulfide rearrangements during protein folding.
The AAA+ protein unfolding motor ClpX grips substrates with the uppermost part of its substrate-binding pore, and requires interactions with hydrophobic amino acid side chains to operate with optimal efficiency.
Pulsed-labeling hydrogen exchange on the ribonuclease H family show that the major folding intermediate is conserved over three billion years of evolution, but the path leading to this intermediate varies.
Neuronal ELAV-like (nELAVL) proteins are associated with non-coding Y RNAs in stressed neurons and in the brains of Alzheimer's disease patients, suggesting a new means of regulatory protein sequestration and mRNA target regulation.
The physical interaction network encoded in the multi-domain protein native structure handles the trade-off between the fast, stable folding and the efficient, reliable function.
C-mannosylation supports native folding of thrombospondin type 1 repeats in the endoplasmic reticulum and stabilizes the folded proteins by modulating the dynamics of the tryptophan-arginine ladder.