Yoshitaka Matsuo

The paper identifies the roles of Ubp2 and Ubp3 in editing polyubiquitin chains on ribosomes to maintain RQC activity.

The paper identifies Otu2's role in deubiquitinating eS7 on recycled 40S ribosomal subunits to reset translation, revealing structural mechanisms for this process.

This study identifies Hel2 as a sensor for ribosome collision in secretory pathways, showing it binds to mistargeted ribosome-nascent chain complexes and contributes to mitochondrial function.

This study shows that eS7A ubiquitination during ER stress in yeast regulates mRNA translation and affects stress outcomes.

The paper shows the Ccr4-Not complex interacts with the ribosome's E-site when codon optimality is low, linking translation efficiency to mRNA stability.