the Functional Phase Separation of HOP and its Regulation
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Related Articles from SNS
TPR Domains Drive the Functional Phase Separation of HOP and its Regulation by Hsp90 and Hsp70
HOP is a cochaperone that facilitates client transfer between two major chaperones, Hsp90 and Hsp70. Emerging evidence, however, suggests that HOP plays additional roles in coordinating complex proteostasis networks. We demonstrate here that stress-dependent HOP foci are biomolecular condensates formed by liquid-liquid phase separation.
Structural basis for chaperone-guided assembly of RNA-induced silencing complex
Abstract The RNA-induced silencing complex (RISC), comprising an Argonaute (AGO) protein and a small RNA, is the central effector in RNA silencing. Small RNAs are loaded onto AGO as bulky duplexes in an HSP70- and HSP90-dependent process1,2,3, but the molecular mechanism remains poorly understood. Here we identify the human AGO–HSP90–p23 complex, which captures AGO in an RNA-free state, termed the AGO maturation complex (AMC).