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Originally published In Press as doi:10.1074/mcp.M500198-MCP200 on November 7, 2005.
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Molecular & Cellular Proteomics 5:234-244, 2006.
© 2006 by The American Society for Biochemistry and Molecular Biology, Inc.

Research

Identification of VCP/p97, Carboxyl Terminus of Hsp70-interacting Protein (CHIP), and Amphiphysin II Interaction Partners Using Membrane-based Human Proteome Arrays*,S

Gerlinde Grelle{ddagger}, Susanne Kostka{ddagger}, Albrecht Otto{ddagger}, Birgit Kersten{ddagger}, Klaus F. Genser{ddagger}, Eva-Christina Müller{ddagger}, Stephanie Wälter{ddagger}, Annett Böddrich{ddagger}, Ulrich Stelzl{ddagger}, Christian Hänig{ddagger}, Rudolf Volkmer-Engert§, Christiane Landgraf§, Simon Alberti, Jörg Höhfeld, Martin Strödicke{ddagger} and Erich E. Wanker{ddagger},||

From the {ddagger} Max-Delbrück-Centrum für Molekulare Medizin, Robert-Rössle-Strasse 10, D-13125 Berlin-Buch, Germany, § Institut für Medizinische Immunologie, Charité-Universitätsmedizin Berlin, Hessische Str. 3-4, D-10115 Berlin, Germany, and Institut für Zellbiologie und Bonner Forum Biomedizin, Rheinische Friedrich-Wilhelms-Universität Bonn, D-53121 Bonn, Germany

Proteins mediate their biological function through interactions with other proteins. Therefore, the systematic identification and characterization of protein-protein interactions have become a powerful proteomic strategy to understand protein function and comprehensive cellular regulatory networks. For the screening of valosin-containing protein, carboxyl terminus of Hsp70-interacting protein (CHIP), and amphiphysin II interaction partners, we utilized a membrane-based array technology that allows the identification of human protein-protein interactions with crude bacterial cell extracts. Many novel interaction pairs such as valosin-containing protein/autocrine motility factor receptor, CHIP/caytaxin, or amphiphysin II/DLP4 were identified and subsequently confirmed by pull-down, two-hybrid and co-immunoprecipitation experiments. In addition, assays were performed to validate the interactions functionally. CHIP e.g. was found to efficiently polyubiquitinate caytaxin in vitro, suggesting that it might influence caytaxin degradation in vivo. Using peptide arrays, we also identified the binding motifs in the proteins DLP4, XRCC4, and fructose-1,6-bisphosphatase, which are crucial for the association with the Src homology 3 domain of amphiphysin II. Together these studies indicate that our human proteome array technology permits the identification of protein-protein interactions that are functionally involved in neurodegenerative disease processes, the degradation of protein substrates, and the transport of membrane vesicles.

|| To whom correspondence should be addressed: Dept. of Neuroproteomics, Max-Delbrück-Centrum für Molekulare Medizin, Robert-Rössle-Strasse 10, D-13125 Berlin-Buch, Germany. Tel.: 49-30-9406-2157; Fax: 49-30-9406-2552; E-mail: ewanker{at}mdc-berlin.de


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