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A more recent version of this article appeared on February 1, 2006.
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Submitted on July 5, 2005
Revised on November 4, 2005
Accepted on November 6, 2005

Identification of VCP/p97, CHIP and amphiphysin II interaction partners using membrane-based human proteome arrays

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

Neuroproteomics, Max-Delbrück-Centrum für Molekulare Medizin, Berlin D-13125

Corresponding Author: ewanker{at}mdc-berlin.de

Proteins mediate their biological function through interactions with other proteins. Therefore, the systematic identification and characterization of protein-protein interactions has become a powerful proteomics strategy to understand protein function and comprehensive cellular regulatory networks. For the screening of VCP, 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 VCP/AMFR, 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 FBP, which are crucial for the association with the SH3 domain of amphiphysin II. Together, these studies indicate that our human proteome array technology permits the identification of protein-protein interactions, which are functionally involved in neurodegenerative disease processes, the degradation of protein substrates and the transport of membrane vesicles.


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