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Verlagslink DOI: 10.1074/mcp.M112.019059
Titel: Protein-protein-interaction network organization of the hypusine modification system
Sprache: English
Autor/Autorin: Sievert, Henning 
Venz, Simone 
Platas Barradas, Oscar 
Dhople, Vishnu Mukund 
Schaletzky, Martin 
Nagel, Claus-Henning 
Braig, Melanie 
Preukschas, Michael 
Pällmann, Nora 
Bokemeyer, Carsten 
Brümmendorf, Tim H. 
Pörtner, Ralf 
Walther, Reinhard 
Duncan, Kent E. 
Hauber, Joachim 
Balabanov, Stefan 
Schlagwörter: Animals;Computational Biology;DNA-Binding Proteins;Humans;Lysine;Mass Spectrometry;Mice;Mixed Function Oxygenases;Multivesicular Bodies;NIH 3T3 Cells;Nuclear Proteins;Oxidoreductases Acting on CH-NH Group Donors;Peptide Fragments;Peptide Initiation Factors;Protein Transport;RNA-Binding Proteins;Recombinant Fusion Proteins;Reproducibility of Results;Ribosomal Proteins;Subcellular Fractions;Protein Interaction Maps;Protein Processing, Post-Translational
Erscheinungsdatum: 10-Aug-2012
Verlag: American Society for Biochemistry and Molecular Biology, HighWire Press
Quellenangabe: Molecular & cellular proteomics : MCP 11 (11): 1289-1305 (2012)
Zeitschrift oder Schriftenreihe: Molecular & cellular proteomics 
Zusammenfassung (englisch): Hypusine modification of eukaryotic initiation factor 5A (eIF-5A) represents a unique and highly specific post-translational modification with regulatory functions in cancer, diabetes, and infectious diseases. However, the specific cellular pathways that are influenced by the hypusine modification remain largely unknown. To globally characterize eIF-5A and hypusine-dependent pathways, we used an approach that combines large-scale bioreactor cell culture with tandem affinity purification and mass spectrometry: "bioreactor-TAP-MS/MS." By applying this approach systematically to all four components of the hypusine modification system (eIF-5A1, eIF-5A2, DHS, and DOHH), we identified 248 interacting proteins as components of the cellular hypusine network, with diverse functions including regulation of translation, mRNA processing, DNA replication, and cell cycle regulation. Network analysis of this data set enabled us to provide a comprehensive overview of the protein-protein interaction landscape of the hypusine modification system. In addition, we validated the interaction of eIF-5A with some of the newly identified associated proteins in more detail. Our analysis has revealed numerous novel interactions, and thus provides a valuable resource for understanding how this crucial homeostatic signaling pathway affects different cellular functions.
URI: https://tubdok.tub.tuhh.de/handle/11420/1940
DOI: 10.15480/882.1937
ISSN: 1535-9484
Institut: Bioprozess- und Biosystemtechnik V-1 
Dokumenttyp: (wissenschaftlicher) Artikel
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