Hypophosphorylation of the architectural chromatin protein DEK in death-receptor-induced apoptosis revealed by the isotope coded protein label proteomic platform

Lade...
Vorschaubild
Dateien
tabbert_182425.pdf
tabbert_182425.pdfGröße: 7.36 MBDownloads: 486
Datum
2006
Autor:innen
Tabbert, Anja
Kappes, Ferdinand
Kellermann, Josef
Herausgeber:innen
Kontakt
ISSN der Zeitschrift
Electronic ISSN
ISBN
Bibliografische Daten
Verlag
Schriftenreihe
Auflagebezeichnung
ArXiv-ID
Internationale Patentnummer
Angaben zur Forschungsförderung
Projekt
Open Access-Veröffentlichung
Open Access Green
Core Facility der Universität Konstanz
Gesperrt bis
Titel in einer weiteren Sprache
Forschungsvorhaben
Organisationseinheiten
Zeitschriftenheft
Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published
Erschienen in
PROTEOMICS. 2006, 6(21), pp. 5758-5772. ISSN 1615-9853. eISSN 1615-9861. Available under: doi: 10.1002/pmic.200600197
Zusammenfassung

During apoptosis nuclear morphology changes dramatically due to alterations of chromatin architecture and cleavage of structural nuclear proteins. To characterize early events in apoptotic nuclear dismantling we have performed a proteomic study of apoptotic nuclei. To this end we have combined a cell-free apoptosis system with a proteomic platform based on the differential isotopic labeling of primary amines with N-nicotinoyloxy-succinimide. We exploited the ability of this system to produce nuclei arrested at different stages of apoptosis to analyze proteome alterations which occur prior to or at a low level of caspase activation. We show that the majority of proteins affected at the onset of apoptosis are involved in chromatin architecture and RNA metabolism. Among them is DEK, an architectural chromatin protein which is linked to autoimmune disorders. The proteomic analysis points to the occurrence of multiple PTMs in early apoptotic nuclei. This is confirmed by showing that the level of phosphorylation of DEK is decreased following apoptosis induction. These results suggest the unexpected existence of an early crosstalk between cytoplasm and nucleus during apoptosis. They further establish a previously unrecognized link between DEK and cell death, which will prove useful in the elucidation of the physiological function of this protein.

Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
570 Biowissenschaften, Biologie
Schlagwörter
Caspase, hnRNP, Isotope coded protein label, Oncoprotein, Post-translational modification
Konferenz
Rezension
undefined / . - undefined, undefined
Zitieren
ISO 690TABBERT, Anja, Ferdinand KAPPES, Rolf KNIPPERS, Josef KELLERMANN, Friedrich LOTTSPEICH, Elisa FERRANDO-MAY, 2006. Hypophosphorylation of the architectural chromatin protein DEK in death-receptor-induced apoptosis revealed by the isotope coded protein label proteomic platform. In: PROTEOMICS. 2006, 6(21), pp. 5758-5772. ISSN 1615-9853. eISSN 1615-9861. Available under: doi: 10.1002/pmic.200600197
BibTex
@article{Tabbert2006-11Hypop-18242,
  year={2006},
  doi={10.1002/pmic.200600197},
  title={Hypophosphorylation of the architectural chromatin protein DEK in death-receptor-induced apoptosis revealed by the isotope coded protein label proteomic platform},
  number={21},
  volume={6},
  issn={1615-9853},
  journal={PROTEOMICS},
  pages={5758--5772},
  author={Tabbert, Anja and Kappes, Ferdinand and Knippers, Rolf and Kellermann, Josef and Lottspeich, Friedrich and Ferrando-May, Elisa}
}
RDF
<rdf:RDF
    xmlns:dcterms="http://purl.org/dc/terms/"
    xmlns:dc="http://purl.org/dc/elements/1.1/"
    xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#"
    xmlns:bibo="http://purl.org/ontology/bibo/"
    xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#"
    xmlns:foaf="http://xmlns.com/foaf/0.1/"
    xmlns:void="http://rdfs.org/ns/void#"
    xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > 
  <rdf:Description rdf:about="https://kops.uni-konstanz.de/server/rdf/resource/123456789/18242">
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-03-22T09:20:50Z</dc:date>
    <dc:language>eng</dc:language>
    <dc:creator>Tabbert, Anja</dc:creator>
    <dc:contributor>Tabbert, Anja</dc:contributor>
    <dc:rights>terms-of-use</dc:rights>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dcterms:issued>2006-11</dcterms:issued>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/18242/2/tabbert_182425.pdf"/>
    <dc:creator>Ferrando-May, Elisa</dc:creator>
    <dcterms:title>Hypophosphorylation of the architectural chromatin protein DEK in death-receptor-induced apoptosis revealed by the isotope coded protein label proteomic platform</dcterms:title>
    <dc:contributor>Kappes, Ferdinand</dc:contributor>
    <dc:contributor>Lottspeich, Friedrich</dc:contributor>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/52"/>
    <dc:creator>Lottspeich, Friedrich</dc:creator>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/52"/>
    <dcterms:abstract xml:lang="eng">During apoptosis nuclear morphology changes dramatically due to alterations of chromatin architecture and cleavage of structural nuclear proteins. To characterize early events in apoptotic nuclear dismantling we have performed a proteomic study of apoptotic nuclei. To this end we have combined a cell-free apoptosis system with a proteomic platform based on the differential isotopic labeling of primary amines with N-nicotinoyloxy-succinimide. We exploited the ability of this system to produce nuclei arrested at different stages of apoptosis to analyze proteome alterations which occur prior to or at a low level of caspase activation. We show that the majority of proteins affected at the onset of apoptosis are involved in chromatin architecture and RNA metabolism. Among them is DEK, an architectural chromatin protein which is linked to autoimmune disorders. The proteomic analysis points to the occurrence of multiple PTMs in early apoptotic nuclei. This is confirmed by showing that the level of phosphorylation of DEK is decreased following apoptosis induction. These results suggest the unexpected existence of an early crosstalk between cytoplasm and nucleus during apoptosis. They further establish a previously unrecognized link between DEK and cell death, which will prove useful in the elucidation of the physiological function of this protein.</dcterms:abstract>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:creator>Kellermann, Josef</dc:creator>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-03-22T09:20:50Z</dcterms:available>
    <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/18242"/>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/18242/2/tabbert_182425.pdf"/>
    <dc:contributor>Knippers, Rolf</dc:contributor>
    <dc:contributor>Kellermann, Josef</dc:contributor>
    <dc:contributor>Ferrando-May, Elisa</dc:contributor>
    <dc:creator>Knippers, Rolf</dc:creator>
    <dc:creator>Kappes, Ferdinand</dc:creator>
    <dcterms:bibliographicCitation>Proteomics ; 6 (2006), 21. -  S. 5758-5772</dcterms:bibliographicCitation>
  </rdf:Description>
</rdf:RDF>
Interner Vermerk
xmlui.Submission.submit.DescribeStep.inputForms.label.kops_note_fromSubmitter
Kontakt
URL der Originalveröffentl.
Prüfdatum der URL
Prüfungsdatum der Dissertation
Finanzierungsart
Kommentar zur Publikation
Allianzlizenz
Corresponding Authors der Uni Konstanz vorhanden
Internationale Co-Autor:innen
Universitätsbibliographie
Ja
Begutachtet
Diese Publikation teilen