Huaqun Zhang

TL;DR: This study shows how CHIP docks onto Hsp70/Hsc70 and defines a bipartite mode of interaction between TPR domains and their binding partners, and shows how posttranslational modifications of the Hsc70 lid and tail disrupt key contacts with the CHIP-TPR and may regulateCHIP-mediated ubiquitination.

TL;DR: The ubiquitin ligase CHIP plays an important role in cytosolic protein quality control by ubiquitinating proteins chaperoned by Hsp70/Hsc70 and Hsp90 and targeting them for degradation as discussed by the authors.

TL;DR: CHIP-mediated protein turnover is markedly post-translationally enhanced by direct protein kinase G phosphorylation at S20 (mouse, S19 human), which increases CHIP binding affinity to Hsc70, CHIP protein half-life, and consequent clearance of stress-induced ubiquitinated-insoluble proteins.

TL;DR: This study describes a well-characterized analog of MMP7 that is available for future inhibitor design efforts and suggests that improved inhibitory character may be due to interactions with the S1' substrate binding pocket.

TL;DR: This study sheds light on the roles of the Mn2+-dependent exonucleases in remodeling gene silencing and shows that ISG20-mediated guide trimming makes Argonaute3 (AGO3) a slicer.