Research Topics
Genomes and Genes
| Alexander BuchbergerSummaryCountry: Germany Publications
| Collaborators
|
Detail Information
Publications
From UBA to UBX: new words in the ubiquitin vocabularyAlexander Buchberger
Dept of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18a, D 82152 Martinsried, Germany
Trends Cell Biol 12:216-21. 2002..Here, I give an overview of important ubiquitin-related protein motifs, including the UBA, UIM, UBD and UBX domains, and propose a model for the role of subclasses of UBA-domain-containing proteins in ubiquitin-mediated proteolysis...- Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated protein degradationChristian Schuberth
Max Planck Institute of Biochemistry, Department of Molecular Cell Biology, Am Klopferspitz 18, 82152 Martinsried, Germany
Nat Cell Biol 7:999-1006. 2005..Lack of Ubx2 causes defects in ERAD that are exacerbated under stress conditions. These findings are consistent with a model in which Ubx2 coordinates the assembly of a highly efficient ERAD machinery at the ER membrane... 
UBXD1 binds p97 through two independent binding sitesMaximilian Kern
Max Planck Institute of Biochemistry, Department of Molecular Cell Biology, Am Klopferspitz 18, 82152 Martinsried, Germany
Biochem Biophys Res Commun 380:303-7. 2009..This novel, bipartite binding mode suggests that UBXD1 could be an efficient regulator of p97 cofactor interactions...- Imbalances in p97 co-factor interactions in human proteinopathyVanesa Fernández-Sáiz
Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
EMBO Rep 11:479-85. 2010..Our results suggest that imbalanced co-factor binding to p97 is a key pathological feature of IBMPFD and potentially of other proteinopathies involving p97... 
Shp1 and Ubx2 are adaptors of Cdc48 involved in ubiquitin-dependent protein degradationChristian Schuberth
Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
EMBO Rep 5:818-24. 2004..Our data suggest that Shp1 and Ubx2 are adaptors for Cdc48-dependent protein degradation through the ubiquitin/proteasome pathway...- A yeast two-hybrid system reconstituting substrate recognition of the von Hippel-Lindau tumor suppressor proteinClaudia Bex
Max Planck Institute of Biochemistry, Department of Molecular Cell Biology, Am Klopferspitz 18, 82152 Martinsried, Germany
Nucleic Acids Res 35:e142. 2007..Additional future applications may include structure/function analyses of pVHL-HIF1/2alpha binding and screens for therapeutically relevant compounds that either stabilize or disrupt this interaction... - VHL mutations linked to type 2C von Hippel-Lindau disease cause extensive structural perturbations in pVHLKatja Knauth
Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
J Biol Chem 284:10514-22. 2009..Together, our data reveal unexpectedly strong structural defects of type 2C-associated pVHL mutant proteins that are likely to affect both HIF-1/2alpha-related and -unrelated pVHL functions in the pathogenesis of pheochromocytomas... - The PUB domain functions as a p97 binding module in human peptide N-glycanaseMark D Allen
Centre for Protein Engineering, Medical Research Council, Hills Road, Cambridge CB2 2QH, United Kingdom
J Biol Chem 281:25502-8. 2006..Furthermore, we show that the PUB and UBX domains do not bind to p97 in a mutually exclusive manner. Our results suggest that PUB domain-containing proteins constitute a widespread family of diverse p97 cofactors...