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Protein-protein-interaction network organization of the hypusine modification system.

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Protein-protein-interaction network organization of the hypusine modification system. / Sievert, Henning; Venz, Simone; Platas-Barradas, Oscar; Dhople, Vishnu M; Schaletzky, Martin; Nagel, Claus-Henning; Balabanov, Melanie; Preukschas, Michael; Pällmann, Nora; Bokemeyer, Carsten; Brümmendorf, Tim; Pörtner, Ralf; Walther, Reinhard; Duncan, Kent E.; Hauber, Joachim; Balabanov, Stefan.

In: MOL CELL PROTEOMICS, Vol. 11, No. 11, 11, 2012, p. 1289-1305.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Sievert, H, Venz, S, Platas-Barradas, O, Dhople, VM, Schaletzky, M, Nagel, C-H, Balabanov, M, Preukschas, M, Pällmann, N, Bokemeyer, C, Brümmendorf, T, Pörtner, R, Walther, R, Duncan, KE, Hauber, J & Balabanov, S 2012, 'Protein-protein-interaction network organization of the hypusine modification system.', MOL CELL PROTEOMICS, vol. 11, no. 11, 11, pp. 1289-1305. <http://www.ncbi.nlm.nih.gov/pubmed/22888148?dopt=Citation>

APA

Sievert, H., Venz, S., Platas-Barradas, O., Dhople, V. M., Schaletzky, M., Nagel, C-H., Balabanov, M., Preukschas, M., Pällmann, N., Bokemeyer, C., Brümmendorf, T., Pörtner, R., Walther, R., Duncan, K. E., Hauber, J., & Balabanov, S. (2012). Protein-protein-interaction network organization of the hypusine modification system. MOL CELL PROTEOMICS, 11(11), 1289-1305. [11]. http://www.ncbi.nlm.nih.gov/pubmed/22888148?dopt=Citation

Vancouver

Sievert H, Venz S, Platas-Barradas O, Dhople VM, Schaletzky M, Nagel C-H et al. Protein-protein-interaction network organization of the hypusine modification system. MOL CELL PROTEOMICS. 2012;11(11):1289-1305. 11.

Bibtex

@article{85fd6e6f78504456b473b82a50a2ca2e,
title = "Protein-protein-interaction network organization of the hypusine modification system.",
abstract = "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.",
keywords = "Animals, Humans, Reproducibility of Results, Mice, Protein Transport, Computational Biology, Mass Spectrometry, NIH 3T3 Cells, *Protein Processing, Post-Translational, Recombinant Fusion Proteins/metabolism, DNA-Binding Proteins/metabolism, Nuclear Proteins/metabolism, Peptide Fragments/metabolism, Subcellular Fractions/metabolism, Lysine/*analogs & derivatives/metabolism, Mixed Function Oxygenases/metabolism, Multivesicular Bodies/metabolism, Oxidoreductases Acting on CH-NH Group Donors/metabolism, Peptide Initiation Factors/metabolism, *Protein Interaction Maps, RNA-Binding Proteins/metabolism, Ribosomal Proteins/metabolism, Animals, Humans, Reproducibility of Results, Mice, Protein Transport, Computational Biology, Mass Spectrometry, NIH 3T3 Cells, *Protein Processing, Post-Translational, Recombinant Fusion Proteins/metabolism, DNA-Binding Proteins/metabolism, Nuclear Proteins/metabolism, Peptide Fragments/metabolism, Subcellular Fractions/metabolism, Lysine/*analogs & derivatives/metabolism, Mixed Function Oxygenases/metabolism, Multivesicular Bodies/metabolism, Oxidoreductases Acting on CH-NH Group Donors/metabolism, Peptide Initiation Factors/metabolism, *Protein Interaction Maps, RNA-Binding Proteins/metabolism, Ribosomal Proteins/metabolism",
author = "Henning Sievert and Simone Venz and Oscar Platas-Barradas and Dhople, {Vishnu M} and Martin Schaletzky and Claus-Henning Nagel and Melanie Balabanov and Michael Preukschas and Nora P{\"a}llmann and Carsten Bokemeyer and Tim Br{\"u}mmendorf and Ralf P{\"o}rtner and Reinhard Walther and Duncan, {Kent E.} and Joachim Hauber and Stefan Balabanov",
year = "2012",
language = "English",
volume = "11",
pages = "1289--1305",
journal = "MOL CELL PROTEOMICS",
issn = "1535-9476",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "11",

}

RIS

TY - JOUR

T1 - Protein-protein-interaction network organization of the hypusine modification system.

AU - Sievert, Henning

AU - Venz, Simone

AU - Platas-Barradas, Oscar

AU - Dhople, Vishnu M

AU - Schaletzky, Martin

AU - Nagel, Claus-Henning

AU - Balabanov, Melanie

AU - Preukschas, Michael

AU - Pällmann, Nora

AU - Bokemeyer, Carsten

AU - Brümmendorf, Tim

AU - Pörtner, Ralf

AU - Walther, Reinhard

AU - Duncan, Kent E.

AU - Hauber, Joachim

AU - Balabanov, Stefan

PY - 2012

Y1 - 2012

N2 - 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.

AB - 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.

KW - Animals

KW - Humans

KW - Reproducibility of Results

KW - Mice

KW - Protein Transport

KW - Computational Biology

KW - Mass Spectrometry

KW - NIH 3T3 Cells

KW - Protein Processing, Post-Translational

KW - Recombinant Fusion Proteins/metabolism

KW - DNA-Binding Proteins/metabolism

KW - Nuclear Proteins/metabolism

KW - Peptide Fragments/metabolism

KW - Subcellular Fractions/metabolism

KW - Lysine/analogs & derivatives/metabolism

KW - Mixed Function Oxygenases/metabolism

KW - Multivesicular Bodies/metabolism

KW - Oxidoreductases Acting on CH-NH Group Donors/metabolism

KW - Peptide Initiation Factors/metabolism

KW - Protein Interaction Maps

KW - RNA-Binding Proteins/metabolism

KW - Ribosomal Proteins/metabolism

KW - Animals

KW - Humans

KW - Reproducibility of Results

KW - Mice

KW - Protein Transport

KW - Computational Biology

KW - Mass Spectrometry

KW - NIH 3T3 Cells

KW - Protein Processing, Post-Translational

KW - Recombinant Fusion Proteins/metabolism

KW - DNA-Binding Proteins/metabolism

KW - Nuclear Proteins/metabolism

KW - Peptide Fragments/metabolism

KW - Subcellular Fractions/metabolism

KW - Lysine/analogs & derivatives/metabolism

KW - Mixed Function Oxygenases/metabolism

KW - Multivesicular Bodies/metabolism

KW - Oxidoreductases Acting on CH-NH Group Donors/metabolism

KW - Peptide Initiation Factors/metabolism

KW - Protein Interaction Maps

KW - RNA-Binding Proteins/metabolism

KW - Ribosomal Proteins/metabolism

M3 - SCORING: Journal article

VL - 11

SP - 1289

EP - 1305

JO - MOL CELL PROTEOMICS

JF - MOL CELL PROTEOMICS

SN - 1535-9476

IS - 11

M1 - 11

ER -