Tom A. Rapoport

The paper reports the structure of a peroxisomal import channel and shows how it adapts to transport proteins of different sizes.

The paper identifies activation and inactivation pathways of Mga2, a p53-like transcription factor in yeast, showing its role in lipid homeostasis through regulation of Ole1 expression.

The paper shows that Otu1 removes ubiquitin chains from substrates to enable their transfer from Cdc48 ATPase to proteasome for degradation.

The paper shows that hydrophilic residues in trans-membrane segments cause ER membrane proteins to partition into a thinned region near the ubiquitin ligase Hrd1, leading to their degradation.

The paper shows the Mnl1-Pdi1 complex initiates ERAD by de-mannosylating misfolded proteins and reducing their disulfides, enabling translocation for proteasomal degradation.

This study identifies REEP1 proteins as forming a novel ER-derived vesicular compartment and shows that mutations affecting their curvature-inducing activity lead to relocalization to the bulk ER.

The paper demonstrates bidirectional substrate shuttling between the 26S proteasome and Cdc48 ATPase in yeast, showing how this process facilitates protein degradation.