Mitotic phosphorylation of the lamin B receptor by a serine/arginine kinase and p34(cdc2)

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dc.contributor.authorNikolakaki, E.en
dc.contributor.authorMeier, J.en
dc.contributor.authorSimos, G.en
dc.contributor.authorGeorgatos, S. D.en
dc.contributor.authorGiannakouros, T.en
dc.date.accessioned2015-11-24T19:04:16Z
dc.date.available2015-11-24T19:04:16Z
dc.identifier.issn0021-9258-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/20008
dc.rightsDefault Licence-
dc.subjectAmino Acid Sequenceen
dc.subjectAnimalsen
dc.subjectArginine Kinase/*metabolismen
dc.subjectCDC2 Protein Kinase/*metabolismen
dc.subjectCells, Cultureden
dc.subjectChickensen
dc.subjectMitosisen
dc.subjectMolecular Sequence Dataen
dc.subjectNuclear Envelope/*metabolismen
dc.subjectPeptide Mappingen
dc.subjectPeptides/chemistry/metabolismen
dc.subjectPhosphopeptides/metabolismen
dc.subjectPhosphorylationen
dc.subjectProtein-Serine-Threonine Kinases/*metabolismen
dc.subjectReceptors, Cytoplasmic and Nuclear/*metabolismen
dc.subjectTurkeysen
dc.titleMitotic phosphorylation of the lamin B receptor by a serine/arginine kinase and p34(cdc2)en
heal.abstractThe lamin B receptor (LBR) is an integral protein of the inner nuclear membrane that is modified at interphase by a nuclear envelope-bound protein kinase. This enzyme (RS kinase) specifically phosphorylates arginine-serine dipeptide motifs located at the NH2-terminal domain of LBR and regulates its interactions with other nuclear envelope proteins. To compare the phosphorylation state of LBR during interphase and mitosis, we performed phosphopeptide mapping of in vitro and in vivo 32P-labeled LBR and analyzed a series of recombinant proteins and synthetic peptides. Our results show that LBR undergoes two types of mitotic phosphorylation mediated by the RS and the p34(cdc2) protein kinases, respectively. The RS kinase modifies similar sites at interphase and mitosis (i.e. Ser76, Ser78, Ser80, Ser82, Ser84), whereas p34(cdc2) mainly phosphorylates Ser71. These findings clarify the phosphorylation state of LBR during the cell cycle and provide new information for understanding the mechanisms responsible for nuclear envelope assembly and disassembly.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/9045635-
heal.identifier.secondaryhttp://www.jbc.org/content/272/10/6208.full.pdf-
heal.journalNameJ Biol Chemen
heal.journalTypepeer-reviewed-
heal.languageen-
heal.publicationDate1997-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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