Substrate-interacting pore loops of two ATPase subunits determine the . . . Commitment to degradation occurs when conserved pore loops in the proteasomal heterohexameric ATPase motor engage the flexible initiation region of a polyubiquitinated protein substrate for subsequent mechanical unfolding and translocation into a proteolytic chamber
Substrate-interacting pore loops of two ATPase subunits determine the . . . We find that the pore-1 loops of the Rpt6 and Rpt4 ATPase subunits play particularly important, yet distinct roles in substrate capture and unfolding, and in holding the ATPase motor in a static state prior to substrate engagement
Substrate-interacting pore loops of two ATPase subunits dete We find that the pore-1 loops of the Rpt6 and Rpt4 ATPase subunits play particularly important, yet distinct roles in substrate capture and unfolding, and in holding the ATPase motor in a static state prior to substrate engagement
López-Alfonzo E, et al. (2026) | SGD Commitment to degradation occurs when conserved pore loops in the heterohexameric ATPase motor of the proteasome engage the flexible initiation region of a polyubiquitinated protein substrate for subsequent mechanical unfolding and translocation into a proteolytic chamber
publications - Molecular and Cell Biology The Cdc48 unfoldase prepares well-folded protein substrates for degradation by the 26S proteasome (2019) Communications Biology 2:29 doi: 10 1038 s42003-019-0283-z