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.
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.
Studies of Lowe syndrome patient cells, which lack the inositol 5-phosphatase OCRL, suggest that a defect in endocytosis plays a role in the pathological manifestations of the disease.
The mitochondrial protein unfoldase ClpX activates the first enzyme in heme biosynthesis, ALAS, by targeted unfolding that gates access of cofactor to the ALAS active site.
Cryo-EM structures of the AAA+ ClpXP protease bound to an ssrA degron reveal the mechanism of substrate recognition and show how the machine transitions from recognition to translocation and unfolding.
Systematic analyses of DNA replication machinery components in human cells reveal a requirement of MCM-dependent de novo loading or mobilization of cohesin at replication forks in establishing sister-chromatid cohesion.
The cohesin loading factor Scc2/Nipbl interacts frequently with cohesin after the loading reaction in a manner consistent with a role in stimulating loop extrusion.
