Tom A. Rapoport

Oct 17, 2024 | biorxiv.org | Dan Zhao |Xudong Wu |Tom A. Rapoport |Westlake Laboratory

AbstractMisfolded glycoproteins in the endoplasmic reticulum (ER) lumen are translocated into the cytosol and degraded by the proteasome, a conserved process called ER-associated protein degradation (ERAD). In S. cerevisiae, the glycan of these proteins is trimmed by the luminal mannosidase Mnl1 (Htm1) to generate a signal that triggers degradation. Curiously, Mnl1 is permanently associated with protein disulfide isomerase (Pdi1).

Feb 23, 2024 | cell.com | Steven Gygi |Tom A. Rapoport

Highlights•Cdc48 ATPase-dependent proteasomal protein degradation reconstituted in vitro•Substrate shuttling between the proteasome and Cdc48 is mediated by Rad23 and Ubx5•Shp1 stimulates protein unfolding by Cdc48, rather than substrate recruitment•Bidirectional substrate shuttling between the molecular machines occurs in yeastSummaryMost eukaryotic proteins are degraded by the 26S proteasome after modification with a polyubiquitin chain.