Structures of the 26S proteasome in complex with the Hsp70 cochaperone Bag1 reveal a novel mechanism of ubiquitin-independent proteasomal degradation
Authors Maestro-Lopez M, Cheng TC, Muntaner J, Menendez M, Alonso M, Schweitzer A, Cuellar J, Valpuesta JM, Sakata E Journal BioRxiv Citation bioRxiv 2025.01.22.633148. Abstract The 26S proteasome primarily degrades proteins marked by polyubiquitin chains. Although ubiquitin-independent pathways for proteasomal degradation exist, the mechanisms involved remain poorly understood. Bag1 links