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TitleUFMylation orchestrates spatiotemporal coordination of RQC at the ER.
Journal, issue, pagesSci Adv, Vol. 11, Issue 18, Page eadv0435, Year 2025
Publish dateMay 2, 2025
AuthorsIvan Penchev / Samantha Gumbin / Francesco Scavone / Otto Berninghausen / Thomas Becker / Ron Kopito / Roland Beckmann /
PubMed AbstractDegradation of arrest peptides from endoplasmic reticulum (ER) translocon-bound 60 ribosomal subunits via the ribosome-associated quality control (ER-RQC) pathway requires covalent modification of ...Degradation of arrest peptides from endoplasmic reticulum (ER) translocon-bound 60 ribosomal subunits via the ribosome-associated quality control (ER-RQC) pathway requires covalent modification of RPL26/uL24 on 60 ribosomal subunits with UFM1. However, the underlying mechanism that coordinates the UFMylation and RQC pathways remains elusive. Structural analysis of ER-RQC intermediates revealed concomitant binding and direct interaction of the UFMylation and RQC machineries on the 60. In the presence of an arrested peptidyl-transfer RNA, the RQC factor NEMF and the UFM1 E3 ligase (E3) form a direct interaction via the UFL1 subunit of E3, and UFL1 adopts a conformation distinct from that previously observed for posttermination 60. While this concomitant binding occurs on translocon-bound 60, LTN1 recruitment and arrest peptide degradation require UFMylation-dependent 60 dissociation from the translocon. These data reveal a mechanism by which the UFMylation cycle orchestrates ER-RQC.
External linksSci Adv / PubMed:40315331 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 4.0 Å
Structure data

51681

9gy4

EMDB-51681, PDB-9gy4:
60S ribosomal subunit in complex with E3-UFM1 ligase and RQC machinery components NEMF and LTN1 (Composite map)
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-51682: 60S ribosomal subunit in complex with E3-UFM1 ligase and RQC machinery components NEMF and LTN1 (60S body)
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-51683: 60S ribosomal subunit in complex with E3-UFM1 ligase and RQC machinery components NEMF and LTN1 (UFM1 E3 ligase and NEMF)
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-51684: 60S ribosomal subunit in complex with E3-UFM1 ligase and RQC machinery components NEMF and LTN1 (LTN1)
Method: EM (single particle) / Resolution: 4.0 Å

EMDB-51685: 60S ribosomal subunit in complex with E3-UFM1 ligase and RQC machinery components NEMF and LTN1 (Consensus refinement map)
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-51686: 60S ribosomal subunit in complex with RQC components NEMF and LTN1
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-51687: 60S ribosomal subunit in complex with E3-UFM1 ligase, NEMF, and Sec61
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-51688: 60S ribosomal subunit in complex with NEMF and Sec61
Method: EM (single particle) / Resolution: 2.8 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsRIBOSOME / 60S / UFMylation / ER / RQC

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