HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: M500198-MCP200v1 5/2/234    most recent Submit a response Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Glossary Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Grelle, G. Articles by Wanker, E. E. Search for Related Content PubMed PubMed Citation Articles by Grelle, G. Articles by Wanker, E. E. Social Bookmarking                      What's this?

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, 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^,||

From the 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.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				U. K. Jinwal, J. Koren III, S. I. Borysov, A. B. Schmid, J. F. Abisambra, L. J. Blair, A. G. Johnson, J. R. Jones, C. L. Shults, J. C. O'Leary III, et al. The Hsp90 Cochaperone, FKBP51, Increases Tau Stability and Polymerizes Microtubules J. Neurosci., January 13, 2010; 30(2): 591 - 599. [Abstract] [Full Text] [PDF]

				T. Aoyama, S. Hata, T. Nakao, Y. Tanigawa, C. Oka, and M. Kawaichi Cayman ataxia protein caytaxin is transported by kinesin along neurites through binding to kinesin light chains J. Cell Sci., November 15, 2009; 122(22): 4177 - 4185. [Abstract] [Full Text] [PDF]

				A. C. Rutledge, W. Qiu, R. Zhang, R. Kohen-Avramoglu, N. Nemat-Gorgani, and K. Adeli Mechanisms Targeting Apolipoprotein B100 to Proteasomal Degradation: Evidence That Degradation Is Initiated by BiP Binding at the N Terminus and the Formation of a p97 Complex at the C Terminus Arterioscler Thromb Vasc Biol, April 1, 2009; 29(4): 579 - 585. [Abstract] [Full Text] [PDF]

				H. Adachi, M. Waza, K. Tokui, M. Katsuno, M. Minamiyama, F. Tanaka, M. Doyu, and G. Sobue CHIP Overexpression Reduces Mutant Androgen Receptor Protein and Ameliorates Phenotypes of the Spinal and Bulbar Muscular Atrophy Transgenic Mouse Model J. Neurosci., May 9, 2007; 27(19): 5115 - 5126. [Abstract] [Full Text] [PDF]

				C. Scheich, D. Kummel, D. Soumailakakis, U. Heinemann, and K. Bussow Vectors for co-expression of an unrestricted number of proteins Nucleic Acids Res., March 19, 2007; 35(6): e43 - e43. [Abstract] [Full Text] [PDF]

				C. A. Dickey, M. Yue, W.-L. Lin, D. W. Dickson, J. H. Dunmore, W. C. Lee, C. Zehr, G. West, S. Cao, A. M. K. Clark, et al. Deletion of the ubiquitin ligase CHIP leads to the accumulation, but not the aggregation, of both endogenous phospho- and caspase-3-cleaved tau species. J. Neurosci., June 28, 2006; 26(26): 6985 - 6996. [Abstract] [Full Text] [PDF]

				G. Li, G. Zhao, X. Zhou, H. Schindelin, and W. J. Lennarz The AAA ATPase p97 links peptide N-glycanase to the endoplasmic reticulum-associated E3 ligase autocrine motility factor receptor PNAS, May 30, 2006; 103(22): 8348 - 8353. [Abstract] [Full Text] [PDF]