Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/24242
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dc.contributor.authorMaison, C.en
dc.contributor.authorPyrpasopoulou, A.en
dc.contributor.authorTheodoropoulos, P. A.en
dc.contributor.authorGeorgatos, S. D.en
dc.date.accessioned2015-11-24T19:39:23Z-
dc.date.available2015-11-24T19:39:23Z-
dc.identifier.issn0261-4189-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/24242-
dc.rightsDefault Licence-
dc.subjectAmino Acid Sequenceen
dc.subjectAnimalsen
dc.subjectAntibodies, Monoclonal/immunologyen
dc.subjectCell Lineen
dc.subject*DNA-Binding Proteinsen
dc.subjectElectrophoresis, Polyacrylamide Gelen
dc.subjectImmunohistochemistryen
dc.subject*Interphaseen
dc.subjectLamin Type Ben
dc.subjectLaminsen
dc.subjectMembrane Proteins/immunology/*metabolismen
dc.subject*Mitosisen
dc.subjectMitotic Spindle Apparatus/chemistry/*metabolismen
dc.subjectMolecular Sequence Dataen
dc.subjectNuclear Envelope/*chemistryen
dc.subjectNuclear Proteins/immunology/*metabolismen
dc.subjectPeptide Fragments/chemistryen
dc.subjectPhosphopeptides/metabolismen
dc.subjectProtein Kinases/chemistryen
dc.subjectRatsen
dc.subjectSequence Analysisen
dc.titleThe inner nuclear membrane protein LAP1 forms a native complex with B-type lamins and partitions with spindle-associated mitotic vesiclesen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primary10.1093/emboj/16.16.4839-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/9305626-
heal.identifier.secondaryhttp://www.nature.com/emboj/journal/v16/n16/pdf/7590462a.pdf-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate1997-
heal.abstractWe have examined the in situ organization and nearest neighbours of the 'lamina-associated polypeptide-1' (LAP1), a type II membrane protein and a major constituent of the mammalian nuclear envelope. We show here that, during interphase, LAP1 forms multimeric assemblies which are suspended in the inner nuclear membrane and are specifically associated with B-type lamins. The LAP1-lamin B complex is distinct from analogous complexes formed by the 'lamina-associated polypeptide-2' (LAP2), another inner nuclear membrane protein, and includes a protein kinase. Upon nuclear envelope breakdown, LAP1 partitions with mitotic vesicles which carry nuclear lamin B. The LAP1 vesicles can be distinguished from fragments of the nuclear envelope containing LAP2 and exhibit a striking co-alignment with spindle microtubules. These observations suggest that the inner nuclear membrane comprises discrete territories which accommodate specific integral membrane proteins and are differentially disassembled during mitosis.en
heal.journalNameEMBO Jen
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ

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