RPL26/uL24 UFMylation is essential for ribosome-associated quality control at the endoplasmic reticulum.
Proc Natl Acad Sci U S A
; 120(16): e2220340120, 2023 04 18.
Article
en En
| MEDLINE
| ID: mdl-37036982
ABSTRACT
Ribosomes that stall while translating cytosolic proteins are incapacitated by incomplete nascent chains, termed "arrest peptides" (APs) that are destroyed by the ubiquitin proteasome system (UPS) via a process known as the ribosome-associated quality control (RQC) pathway. By contrast, APs on ribosomes that stall while translocating secretory proteins into the endoplasmic reticulum (ER-APs) are shielded from cytosol by the ER membrane and the tightly sealed ribosome-translocon junction (RTJ). How this junction is breached to enable access of cytosolic UPS machinery and 26S proteasomes to translocon- and ribosome-obstructing ER-APs is not known. Here, we show that UPS and RQC-dependent degradation of ER-APs strictly requires conjugation of the ubiquitin-like (Ubl) protein UFM1 to 60S ribosomal subunits at the RTJ. Therefore, UFMylation of translocon-bound 60S subunits modulates the RTJ to promote access of proteasomes and RQC machinery to ER-APs.
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Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Ribosomas
/
Retículo Endoplásmico
Tipo de estudio:
Risk_factors_studies
Idioma:
En
Revista:
Proc Natl Acad Sci U S A
Año:
2023
Tipo del documento:
Article