Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/19679
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dc.contributor.authorAkoumianaki, T.en
dc.contributor.authorKardassis, D.en
dc.contributor.authorPolioudaki, H.en
dc.contributor.authorGeorgatos, S. D.en
dc.contributor.authorTheodoropoulos, P. A.en
dc.date.accessioned2015-11-24T19:01:21Z-
dc.date.available2015-11-24T19:01:21Z-
dc.identifier.issn0021-9533-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/19679-
dc.rightsDefault Licence-
dc.subjectAcetylationen
dc.subjectActive Transport, Cell Nucleusen
dc.subjectCell Cycleen
dc.subjectCell Nucleus/drug effects/*metabolismen
dc.subjectCell Proliferationen
dc.subjectChromosomal Proteins, Non-Histone/metabolismen
dc.subjectCold Temperatureen
dc.subjectCytoplasm/*metabolismen
dc.subjectDiffusionen
dc.subjectFluorescence Recovery After Photobleachingen
dc.subjectHeLa Cellsen
dc.subjectHistones/metabolismen
dc.subjectHumansen
dc.subjectKineticsen
dc.subjectNocodazole/pharmacologyen
dc.subjectNuclear Export Signalsen
dc.subjectPhosphorylationen
dc.subjectProtein Conformationen
dc.subjectReceptors, Cytoplasmic and Nuclear/metabolismen
dc.subjectRecombinant Fusion Proteins/metabolismen
dc.subjectTransfectionen
dc.subjectTubulin/chemistry/genetics/*metabolismen
dc.subjectTubulin Modulators/pharmacologyen
dc.titleNucleocytoplasmic shuttling of soluble tubulin in mammalian cellsen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primary10.1242/jcs.043034-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/19299461-
heal.identifier.secondaryhttp://jcs.biologists.org/content/122/8/1111.full.pdf-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate2009-
heal.abstractWe have investigated the subcellular distribution and dynamics of soluble tubulin in unperturbed and transfected HeLa cells. Under normal culture conditions, endogenous alpha/beta tubulin is confined to the cytoplasm. However, when the soluble pool of subunits is elevated by combined cold-nocodazole treatment and when constitutive nuclear export is inhibited by leptomycin B, tubulin accumulates in the cell nucleus. Transfection assays and FRAP experiments reveal that GFP-tagged beta-tubulin shuttles between the cytoplasm and the cell nucleus. Nuclear import seems to occur by passive diffusion, whereas exit from the nucleus appears to rely on nuclear export signals (NESs). Several such motifs can be identified by sequence criteria along the beta-tubulin molecule and mutations in one of these (NES-1) cause a significant accumulation in the nuclear compartment. Under these conditions, the cells are arrested in the G0-G1 phase and eventually die, suggesting that soluble tubulin interferes with important nuclear functions. Consistent with this interpretation, soluble tubulin exhibits stoichiometric binding to recombinant, normally modified and hyper-phosphorylated/acetylated histone H3. Tubulin-bound H3 no longer interacts with heterochromatin protein 1 and lamin B receptor, which are known to form a ternary complex under in vitro conditions. Based on these observations, we suggest that nuclear accumulation of soluble tubulin is part of an intrinsic defense mechanism, which tends to limit cell proliferation under pathological conditions. This readily explains why nuclear tubulin has been detected so far only in cancer or in transformed cells, and why accumulation of this protein in the nucleus increases after treatment with chemotherapeutic agents.en
heal.journalNameJ Cell Scien
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ

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