The coordinated action of UFMylation and the RQC pathways clears arrested polypeptides at the ER
Milica Mihailović·Gülsün Elif Karagöz·Bu Erte·Ioanna Styliara·Yasin Dagdas·Ni Zhan·Aleksandra S. Anisimova
Clearance of arrested nascent polypeptides resulting from ribosomal stalling is essential for proteostasis. Stalled endoplasmic reticulum (ER)-bound ribosomes are marked by ubiquitin-fold modifier 1 (UFM1) on the large ribosomal subunit protein RPL26, but the precise role of this modification in ribosome-associated quality control (RQC) remains poorly understood. Here, we define the interplay between the UFMylation machinery and the RQC in clearing arrested polypeptides upon ribosome stalling at