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dc.contributor.authorClancy, A
dc.contributor.authorHeride, C
dc.contributor.authorPinto-Fernández, A
dc.contributor.authorElcocks, H
dc.contributor.authorKallinos, A
dc.contributor.authorKayser-Bricker, KJ
dc.contributor.authorWang, W
dc.contributor.authorSmith, V
dc.contributor.authorDavis, S
dc.contributor.authorFessler, S
dc.contributor.authorMcKinnon, C
dc.contributor.authorKatz, M
dc.contributor.authorHammonds, T
dc.contributor.authorJones, NP
dc.contributor.authorO'Connell, J
dc.contributor.authorFollows, B
dc.contributor.authorMischke, S
dc.contributor.authorCaravella, JA
dc.contributor.authorIoannidis, S
dc.contributor.authorDinsmore, C
dc.contributor.authorKim, S
dc.contributor.authorBehrens, A
dc.contributor.authorKomander, D
dc.contributor.authorKessler, BM
dc.contributor.authorUrbé, S
dc.contributor.authorClague, MJ
dc.date.accessioned2021-03-31T13:18:31Z
dc.date.available2021-03-31T13:18:31Z
dc.identifier.citationThe Journal of cell biology, 2021, 220 (3)
dc.identifier.issn0021-9525
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/4479
dc.identifier.eissn1540-8140
dc.identifier.doi10.1083/jcb.202004211
dc.description.abstractWhen a ribosome stalls during translation, it runs the risk of collision with a trailing ribosome. Such an encounter leads to the formation of a stable di-ribosome complex, which needs to be resolved by a dedicated machinery. The initial stalling and the subsequent resolution of di-ribosomal complexes requires activity of Makorin and ZNF598 ubiquitin E3 ligases, respectively, through ubiquitylation of the eS10 and uS10 subunits of the ribosome. We have developed a specific small-molecule inhibitor of the deubiquitylase USP9X. Proteomics analysis, following inhibitor treatment of HCT116 cells, confirms previous reports linking USP9X with centrosome-associated protein stability but also reveals a loss of Makorin 2 and ZNF598. We show that USP9X interacts with both these ubiquitin E3 ligases, regulating their abundance through the control of protein stability. In the absence of USP9X or following chemical inhibition of its catalytic activity, levels of Makorins and ZNF598 are diminished, and the ribosomal quality control pathway is impaired.
dc.formatPrint
dc.languageeng
dc.language.isoeng
dc.rights.urihttps://creativecommons.org/licenses/by/4.0
dc.titleThe deubiquitylase USP9X controls ribosomal stalling.
dc.typeJournal Article
dcterms.dateAccepted2020-12-11
rioxxterms.versionVoR
rioxxterms.versionofrecord10.1083/jcb.202004211
rioxxterms.licenseref.urihttps://creativecommons.org/licenses/by/4.0
rioxxterms.typeJournal Article/Review
dc.relation.isPartOfThe Journal of cell biology
pubs.issue3
pubs.notesNot known
pubs.organisational-group/ICR
pubs.organisational-group/ICR
pubs.publication-statusPublished
pubs.volume220
pubs.embargo.termsNot known
dc.contributor.icrauthorBehrens, Axelen


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