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Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0177834
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dc.titleSite-specific phosphorylation of casein kinase 1δ(CK1δ) regulates its activity towards the circadian regulator PER2
dc.contributor.authorEng G.W.L.
dc.contributor.authorEdison
dc.contributor.authorVirshup D.M.
dc.date.accessioned2020-03-19T09:03:07Z
dc.date.available2020-03-19T09:03:07Z
dc.date.issued2017
dc.identifier.citationEng G.W.L., Edison, Virshup D.M. (2017). Site-specific phosphorylation of casein kinase 1δ(CK1δ) regulates its activity towards the circadian regulator PER2. PLoS ONE 12 (5) : e0177834. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0177834
dc.identifier.issn1932-6203
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/165794
dc.description.abstractCircadian rhythms are intrinsic ?24 hour cycles that regulate diverse aspects of physiology, and in turn are regulated by interactions with the external environment. Casein kinase 1 delta (CK1?, CSNK1D) is a key regulator of the clock, phosphorylating both stabilizing and destabilizing sites on the PER2 protein, in a mechanism known as the phosphoswitch. CK1? can itself be regulated by phosphorylation on its regulatory domain, but the specific sites involved, and the role this plays in control of circadian rhythms as well as other CK1-dependent processes is not well understood. Using a sensitized PER2
dc.publisherPublic Library of Science
dc.sourceUnpaywall 20200320
dc.subjectcasein kinase Idelta
dc.subjectcycline
dc.subjectdinaciclib
dc.subjectPER2 protein
dc.subjectproline
dc.subjectstaurosporine
dc.subjectcasein kinase Idelta
dc.subjectcircadian rhythm signaling protein
dc.subjectPER2 protein, human
dc.subjectserine
dc.subjectthreonine
dc.subjectanimal cell
dc.subjectArticle
dc.subjectcell cycle
dc.subjectcircadian rhythm
dc.subjectcontrolled study
dc.subjectembryo
dc.subjectenzyme activity
dc.subjectenzyme regulation
dc.subjectextracellular space
dc.subjectintracellular signaling
dc.subjectluciferase assay
dc.subjectmouse
dc.subjectnonhuman
dc.subjectprotein degradation
dc.subjectprotein domain
dc.subjectprotein phosphorylation
dc.subjectprotein stability
dc.subjectsignal transduction
dc.subjectbinding site
dc.subjectchemistry
dc.subjectgene expression regulation
dc.subjectgenetics
dc.subjectHEK293 cell line
dc.subjecthuman
dc.subjectmetabolism
dc.subjectmutation
dc.subjectphosphorylation
dc.subjectBinding Sites
dc.subjectCasein Kinase Idelta
dc.subjectCell Cycle
dc.subjectGene Expression Regulation
dc.subjectHEK293 Cells
dc.subjectHumans
dc.subjectMutation
dc.subjectPeriod Circadian Proteins
dc.subjectPhosphorylation
dc.subjectProtein Stability
dc.subjectSerine
dc.subjectSignal Transduction
dc.subjectThreonine
dc.typeArticle
dc.contributor.departmentDUKE-NUS MEDICAL SCHOOL
dc.description.doi10.1371/journal.pone.0177834
dc.description.sourcetitlePLoS ONE
dc.description.volume12
dc.description.issue5
dc.description.pagee0177834
dc.published.statePublished
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