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dc.contributor.authorKouklis, P. D.en
dc.contributor.authorHutton, E.en
dc.contributor.authorFuchs, E.en
dc.date.accessioned2015-11-24T19:05:44Z-
dc.date.available2015-11-24T19:05:44Z-
dc.identifier.issn0021-9525-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/20231-
dc.rightsDefault Licence-
dc.subjectAmino Acid Sequenceen
dc.subjectCell Lineen
dc.subjectConserved Sequenceen
dc.subjectCytoskeletal Proteins/biosynthesis/isolation & purification/*metabolismen
dc.subjectDesmoplakinsen
dc.subjectDesmosomes/*metabolism/ultrastructureen
dc.subjectElectrophoresis, Polyacrylamide Gelen
dc.subjectGenomic Libraryen
dc.subjectHumansen
dc.subjectIntermediate Filaments/*metabolism/ultrastructureen
dc.subjectKeratinocytes/metabolism/ultrastructureen
dc.subjectKeratins/isolation & purification/*metabolismen
dc.subjectMolecular Sequence Dataen
dc.subjectProtein Bindingen
dc.subjectRecombinant Proteins/biosynthesis/isolation & purification/metabolismen
dc.subjectSequence Homology, Amino Aciden
dc.subjectSkinen
dc.subjectTransfectionen
dc.titleMaking a connection: direct binding between keratin intermediate filaments and desmosomal proteinsen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/7525601-
heal.identifier.secondaryhttp://jcb.rupress.org/content/127/4/1049.full.pdf-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate1994-
heal.abstractIn epidermal cells, keratin intermediate filaments connect with desmosomes to form extensive cadherin-mediated cytoskeletal architectures. Desmoplakin (DPI), a desmosomal component lacking a transmembrane domain, has been implicated in this interaction, although most studies have been conducted with cells that contain few or no desmosomes, and efforts to demonstrate direct interactions between desmoplakin and intermediate filaments have not been successful. In this report, we explore the biochemical nature of the connections between keratin filaments and desmosomes in epidermal keratinocytes. We show that the carboxy terminal "tail" of DPI associates directly with the amino terminal "head" of type II epidermal keratins, including K1, K2, K5, and K6. We have engineered and purified recombinant K5 head and DPI tail, and we demonstrate direct interaction in vitro by solution-binding assays and by ligand blot assays. This marked association is not seen with simple epithelial type II keratins, vimentin, or with type I keratins, providing a possible explanation for the greater stability of the epidermal keratin filament architecture over that of other cell types. We have identified an 18-amino acid residue stretch in the K5 head that is conserved only among type II epidermal keratins and that appears to play some role in DPI tail binding. This finding might have important implications for understanding a recent point mutation found within this binding site in a family with a blistering skin disorder.en
heal.journalNameJ Cell Biolen
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ

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