Eri Sakata

TL;DR: The quality of the map allowed us to assign α-helices, the predominant secondary structure element of the regulatory particle subunits, throughout the entire map and determine the architecture of the Rpn8/Rpn11 heterodimer, which had hitherto remained elusive.

TL;DR: The findings suggest that the Arg 42 mutation induces a conformational change in the Rpn10‐binding site of Ubl, resulting in impaired proteasomal binding of parkin, which could be the cause of AR‐JP.

TL;DR: The structure of the human 26S proteasome described here reveals previously unidentified features of the AAA-ATPase heterohexamer, and is likely to be important for coordinating the proteasomal subunits during substrate processing.

TL;DR: Cryo-electron microscopy reconstructions of the yeast 26S proteasome in the presence of different nucleotides and nucleotide analogs are reported, allowing for the construction of atomic models of the AAA+ ATPase module as it progresses through the functional cycle.

TL;DR: An integrated model is presented which sheds light on the early steps of protein degradation by the 26S complex and a belt of high “activity” surrounding the AAA-ATPase module is tentatively assigned to the reversible association of proteasome interacting proteins and the conformational heterogeneity among the particles.