Cleaning up stalled ribosome-translocon complexes with ufmylation

Abstract

Ufmylation, a metazoan-specific ubiquitin-like post-translational modification, is implicated in numerous cellular processes and mammalian phenotypes. Here, Wang et al. uncover an important function of ribosome ufmylation in protein quality control at ribosomes that have stalled during co-translational translocation of endoplasmic reticulum (ER)-targeted proteins. Post-translational modifications (PTMs) diversify the proteome and modulate protein function on faster time scales compared to transcriptional or translational regulation. While ubiquitination is one of the most common PTMs, several ubiquitin-like proteins have also been described. One intriguing example first described in 2004 is ufmylation, 1 in which the ubiquitin-like small protein Ubiquitin-Fold Modifier 1 (UFM1) is reversibly conjugated to lysine residues on substrates via a cascade of UFM1-specific ligases and proteases. Interestingly, this modification is found only in metazoans and can occur in plants, but not yeast, suggesting

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