Chair of Biochemistry


    Original Publications

    Takiuchi T, Nakagawa T, Tamiya H, Fujita H, Sasaki Y, Saeki Y, Takeda H, Sawasaki T, Buchberger A, Kimura T and Iwai K (2014). Suppression of LUBAC-mediated linear ubiquitination by a specific interaction between LUBAC and the deubiquitinases CYLD and OTULIN. Genes Cells 19:254-272.

    Böhm S  and Buchberger A (2013). The budding yeast Cdc48-Shp1 complex promotes cell cycle progression by positive regulation of Protein Phosphatase 1 (Glc7). PLoS One 8:e56486.

    Stapf C, Cartwright E, Bycroft M, Hofmann K and Buchberger A (2011). The general definition of the p97/valosin-containing protein (VCP)-interacting motif (VIM) delineates a new family of p97 cofactors. J Biol Chem 286:38670-38678.

    Hänzelmann P, Buchberger A and Schindelin H (2011). Hierarchical binding of cofactors to the AAA ATPase p97. Structure 19:833-843.

    Böhm S, Lamberti G, Fernández-Sáiz V, Stapf C and Buchberger A (2011). Cellular functions of Ufd2 and Ufd3 in proteasomal protein degradation depend on Cdc48 binding. Mol Cell Biol 31:1528-1539.

    Fernández-Sáiz V and Buchberger A (2010). Imbalances in p97 co-factor interactions in human proteinopathy. EMBO Rep 11:479-485.

    Knauth K, Cartwright E, Freund S, Bycroft M and Buchberger A (2009). VHL mutations linked to type 2C von Hippel-Lindau disease cause extensive structural perturbations in pVHL. J Biol Chem 284:10514-10522.

    Kern M, Fernandez-Saiz V, Schäfer Z and Buchberger A (2009). UBXD1 binds p97 through two independent binding sites. Biochem Biophys Res Comm 380:303-307.

    Bex C, Knauth K, Dambacher S and Buchberger A (2007). A yeast two-hybrid system reconstituting substrate recognition of the von Hippel-Lindau tumor suppressor protein. Nucleic Acids Res 35:e142.

    Allen M, Buchberger A* and Bycroft M (2006). The PUB domain functions as a p97 binding module in human peptide N-glycanase. J Biol Chem 281:25502-25508. *co-corresponding author

    Knauth K, Bex C, Jemth P and Buchberger A (2006). Renal cell carcinoma risk in type 2 von Hippel-Lindau disease correlates with defects in pVHL stability and HIF-1alpha interactions. Oncogene 25:370-377.

    Schuberth C and Buchberger A (2005). Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated degradation. Nat Cell Biol 7:999-1006.
    [Read Dispatch in Current Biology, Research Focus in Trends Cell Biol.Research Highlight in Nature Rev. Mol. Cell Biol.]

    Schuberth C, Richly H, Rumpf S and Buchberger A (2004). Shp1 and Ubx2 are adaptors of Cdc48 involved in ubiquitin-dependent protein degradation. EMBO Rep 5:818-824.

    Buchberger A, Howard MJ, Proctor M and Bycroft M (2001). The UBX domain: a widespread ubiquitin-like module. J Mol Biol 307:17-24.

    Buchberger A, Howard MJ, Freund SMV, Proctor M, Butler PJG, Fersht AR and Bycroft M (2000). Biophysical characterization of Elongin C from Saccharomyces cerevisiae. Biochemistry 39:11137-11146.

    Woodward ER, Buchberger A, Clifford SC, Hurst LD, Affara NA and Maher ER (2000). Comparative sequence analysis of the VHL tumor suppressor gene. Genomics 65:253-265.

    Buchberger A, Gässler C, Büttner M, McMacken R and Bukau B (1999). Functional defects of the DnaK756 mutant chaperone of Escherichia coli indicate distinct roles for amino- and carboxyl-terminal residues in substrate and co-chaperone interaction and interdomain communication. J Biol Chem 274:38017-38026.

    Gässler CS, Buchberger A, Laufen T, Mayer MP, Schröder H, Valencia A and Bukau B (1998). Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone. Proc Natl Acad Sci USA 95:15229-15234.

    Packschies L, Theyssen H, Buchberger A, Bukau B, Goody RS and Reinstein J (1997). GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism. Biochemistry 36:3417-3422.

    Buchberger A, Schröder H, Hesterkamp T, Schönfeld HJ and Bukau B (1996). Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding. J Mol Biol 261:328-333.

    Buchberger A, Theyssen H, Schröder H, McCarty JS, Virgallita G, Milkereit P, Reinstein J and Bukau B (1995). Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication. J Biol Chem 270:16903-16910.

    McCarty JS, Buchberger A, Reinstein J and Bukau B (1995). The role of ATP in the functional cycle of the DnaK chaperone system. J Mol Biol 249:126-137.

    Buchberger A, Schröder H, Büttner M, Valencia A and Bukau B (1994). A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE. Nat Struct Biol 1:95-101.

    Buchberger A, Valencia A, McMacken R, Sander C and Bukau B (1994). The chaperone function of DnaK requires the coupling of ATPase activity with substrate binding through residue E171. EMBO J 13:1687-1695.

    Reviews and Book Chapters

    Buchberger A, Schindelin H and Hänzelmann P (2015). Control of p97 function by cofactor binding. FEBS Lett 589:2578-2589.

    Buchberger A (2014). ERQC Autophagy: Yet Another Way to Die. Mol Cell 54:3-4.

    Buchberger A (2013). Roles of Cdc48 in regulated protein degradation in yeast. Subcell Biochem 66:195-222.

    Stolz A, Hilt W, Buchberger A and Wolf DH (2011). Cdc48: a power machine in protein degradation. Trends Biochem Sci 36:515-523.

    Buchberger A, Bukau B and Sommer T (2010). Protein Quality Control in the Cytosol and the Endoplasmic Reticulum: Brothers in Arms. Mol Cell 40:238-251.

    Buchberger A (2010). Control of ubiquitin conjugation by Cdc48 and its cofactors. Subcell Biochem 54:17-30.

    Schuberth C and Buchberger A (2008). UBX domain proteins: major regulators of the AAA ATPase Cdc48/p97. Cell Mol Life Sci 65:2360-2371.

    Buchberger A (2006). Cdc48 (p97) and its cofactors. In: Protein Degradation, Vol. 3: Cell Biology of the Ubiquitin-Proteasome System. RJ Mayer, AJ Ciechanover, M Rechsteiner (eds.), Wiley-VCH, Weinheim, pp. 194-211.

    Buchberger A (2002). From UBA to UBX: new words in the ubiquitin vocabulary. Trends Cell Biol 12:216-221.

    Wiederkehr T, Bukau B and Buchberger A (2002). Protein turnover: a CHIP programmed for proteolysis. Curr Biol 12:R26-R28.

    Buchberger A, Reinstein J and Bukau B (1999). The DnaK chaperone system: Mechanism and comparison with other Hsp70 systems. In: Molecular Chaperones and Folding Catalysts: Regulation, Cellular Function and Mechanisms. B Bukau (ed.), Harwood Academic Publishers, Amsterdam, pp. 609-635.

    Laufen T, Zuber U, Buchberger A and Bukau B (1998). DnaJ proteins. In: Molecular Chaperones in the Life Cycle of Proteins. AL Fink, Y Goto (eds.), Marcel Dekker, New York, pp. 241-274.

    Buchberger A and Bukau B (1997). Escherichia coli DnaK. In: Guidebook to Molecular Chaperones and Protein-Folding Catalysts. M-J Gething (ed.), Sambrook and Tooze, Oxford University Press, Oxford, pp. 22-25.

    Buchberger A and Bukau B (1997). Escherichia coli GrpE. In: Guidebook to Molecular Chaperones and Protein-Folding Catalysts. M-J Gething (ed.), Sambrook and Tooze, Oxford University Press, Oxford, pp. 137-139.

    Rüdiger S, Buchberger A and Bukau B (1997). Interaction of Hsp70 chaperones with substrates. Nat Struct Biol 4:342-349.



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