Show simple item record

dc.contributor.authorSmith, RJ
dc.contributor.authorCordeiro, MH
dc.contributor.authorDavey, NE
dc.contributor.authorVallardi, G
dc.contributor.authorCiliberto, A
dc.contributor.authorGross, F
dc.contributor.authorSaurin, AT
dc.date.accessioned2020-06-03T10:20:10Z
dc.date.issued2019-08-20
dc.identifier.citationCell reports, 2019, 28 (8), pp. 2206 - 2219.e8
dc.identifier.issn2211-1247
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/3680
dc.identifier.eissn2211-1247
dc.identifier.doi10.1016/j.celrep.2019.07.067
dc.description.abstractPP1 and PP2A-B56 are major serine/threonine phosphatase families that achieve specificity by colocalizing with substrates. At the kinetochore, however, both phosphatases localize to an almost identical molecular space and yet they still manage to regulate unique pathways and processes. By switching or modulating the positions of PP1/PP2A-B56 at kinetochores, we show that their unique downstream effects are not due to either the identity of the phosphatase or its precise location. Instead, these phosphatases signal differently because their kinetochore recruitment can be either inhibited (PP1) or enhanced (PP2A) by phosphorylation inputs. Mathematical modeling explains how these inverse phospho-dependencies elicit unique forms of cross-regulation and feedback, which allows otherwise indistinguishable phosphatases to produce distinct network behaviors and control different mitotic processes. Furthermore, our genome-wide analysis suggests that these major phosphatase families may have evolved to respond to phosphorylation inputs in opposite ways because many other PP1 and PP2A-B56-binding motifs are also phospho-regulated.
dc.formatPrint
dc.format.extent2206 - 2219.e8
dc.languageeng
dc.language.isoeng
dc.publisherCELL PRESS
dc.rights.urihttps://creativecommons.org/licenses/by/4.0
dc.subjectHela Cells
dc.subjectKinetochores
dc.subjectHumans
dc.subjectMicrotubule-Associated Proteins
dc.subjectReceptors, Neuropeptide Y
dc.subjectSignal Transduction
dc.subjectAmino Acid Sequence
dc.subjectAmino Acid Motifs
dc.subjectPhosphorylation
dc.subjectPhenotype
dc.subjectModels, Biological
dc.subjectProtein Phosphatase 2
dc.titlePP1 and PP2A Use Opposite Phospho-dependencies to Control Distinct Processes at the Kinetochore.
dc.typeJournal Article
dcterms.dateAccepted2019-07-18
rioxxterms.versionofrecord10.1016/j.celrep.2019.07.067
rioxxterms.licenseref.urihttps://creativecommons.org/licenses/by/4.0
rioxxterms.licenseref.startdate2019-08
rioxxterms.typeJournal Article/Review
dc.relation.isPartOfCell reports
pubs.issue8
pubs.notesNot known
pubs.organisational-group/ICR
pubs.publication-statusPublished
pubs.volume28
pubs.embargo.termsNot known
dc.contributor.icrauthorDavey, Norman


Files in this item

Thumbnail

This item appears in the following collection(s)

Show simple item record

https://creativecommons.org/licenses/by/4.0
Except where otherwise noted, this item's license is described as https://creativecommons.org/licenses/by/4.0