Protein-protein-interaction Network Organization of the Hypusine Modification System
| Autor: | Reinhard Walther, Kent E. Duncan, Joachim Hauber, Martin Schaletzky, Ralf Pörtner, Oscar Platas-Barradas, Stefan Balabanov, Melanie Braig, Claus-Henning Nagel, Carsten Bokemeyer, Vishnu M. Dhople, Simone Venz, Nora Pällmann, Henning Sievert, Tim H. Brümmendorf, Michael Preukschas |
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| Přispěvatelé: | University of Zurich, Balabanov, S |
| Rok vydání: | 2012 |
| Předmět: |
1303 Biochemistry
RNA-binding protein Biochemistry Mass Spectrometry Mixed Function Oxygenases Analytical Chemistry Mice chemistry.chemical_compound Peptide Initiation Factors Eukaryotic initiation factor Protein Interaction Maps 1602 Analytical Chemistry Oxidoreductases Acting on CH-NH Group Donors Biowissenschaften Biologie [570] Multivesicular Bodies Nuclear Proteins RNA-Binding Proteins Translation (biology) 570: Biowissenschaften Biologie DNA-Binding Proteins Protein Transport Medizin [610] Nucleophosmin Subcellular Fractions Ribosomal Proteins Recombinant Fusion Proteins 610 Medicine & health Computational biology Biology DNA-binding protein Ribosomal protein ddc:570 1312 Molecular Biology Animals Humans ddc:610 Molecular Biology Hypusine Tandem affinity purification Research Lysine DNA replication Computational Biology Reproducibility of Results Peptide Fragments chemistry 10032 Clinic for Oncology and Hematology NIH 3T3 Cells 610: Medizin Protein Processing Post-Translational |
| Zdroj: | Molecular & cellular proteomics : MCP 11 (11): 1289-1305 (2012) Molecular & Cellular Proteomics : MCP |
| ISSN: | 1535-9476 |
| DOI: | 10.1074/mcp.m112.019059 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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