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dc.contributor.authorAlfieri, C
dc.contributor.authorTischer, T
dc.contributor.authorBarford, D
dc.date.accessioned2020-07-08T09:36:27Z
dc.date.issued2020-06
dc.identifier.citationEMBO reports, 2020, 21 (6), pp. e49831 - ?
dc.identifier.issn1469-221X
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/3819
dc.identifier.eissn1469-3178en_US
dc.identifier.doi10.15252/embr.201949831en_US
dc.description.abstractThe anaphase-promoting complex (APC/C) is the key E3 ubiquitin ligase which directs mitotic progression and exit by catalysing the sequential ubiquitination of specific substrates. The activity of the APC/C in mitosis is restrained by the spindle assembly checkpoint (SAC), which coordinates chromosome segregation with the assembly of the mitotic spindle. The SAC effector is the mitotic checkpoint complex (MCC), which binds and inhibits the APC/C. It is incompletely understood how the APC/C switches substrate specificity in a cell cycle-specific manner. For instance, it is unclear how in prometaphase, when APC/C activity towards cyclin B and securin is repressed by the MCC, the kinase Nek2A is ubiquitinated. Here, we combine biochemical and structural analysis with functional studies in cells to show that Nek2A is a conformational-specific binder of the APC/C-MCC complex (APC/CMCC ) and that, in contrast to cyclin A, Nek2A can be ubiquitinated efficiently by the APC/C in conjunction with both the E2 enzymes UbcH10 and UbcH5. We propose that these special features of Nek2A allow its prometaphase-specific ubiquitination.
dc.formatPrint-Electronic
dc.format.extente49831 - ?
dc.languageeng
dc.language.isoeng
dc.rights.urihttp://www.rioxx.net/licenses/under-embargo-all-rights-reserved
dc.titleA unique binding mode of Nek2A to the APC/C allows its ubiquitination during prometaphase.
dc.typeJournal Article
dcterms.dateAccepted2020-03-17
rioxxterms.versionofrecord10.15252/embr.201949831
rioxxterms.licenseref.urihttps://creativecommons.org/licenses/by/4.0
rioxxterms.licenseref.startdate2020-06en_US
rioxxterms.typeJournal Article/Review
dc.relation.isPartOfEMBO reports
pubs.issue6
pubs.notesNo embargo
pubs.organisational-group/ICR
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Structural Biology
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Structural Biology/Molecular mechanisms of cell cycle regulation
pubs.organisational-group/ICR
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Structural Biology
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Structural Biology/Molecular mechanisms of cell cycle regulation
pubs.publication-statusPublished
pubs.volume21en_US
pubs.embargo.termsNo embargo
icr.researchteamMolecular mechanisms of cell cycle regulationen_US
dc.contributor.icrauthorAlfieri, Claudioen


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