This image shows Dieter H. Wolf

Dieter H. Wolf

Prof. Dr.

Professor of Biochemistry (retired)
Department of Biochemistry, Institute of Biochemistry and Technical Biochemistry



Allmandring 31
70569 Stuttgart
Room: 01.189


Biochemistry. Proteolysis and the Ubiquitin-Proteasome System in Cellular Control

Personal Information
Date and Place of Birth     18. September 1941, Frankfurt am Main
Citizenship                         German Citizen

1962-1963     Study of Engineering - Technische Universität Karlsruhe
1965              Study of Chemistry and Pre-Diploma in Chemistry - Technische Universität Karlsruhe
1968              Diploma in Chemistry - Technische Universität München
1968-1972     Thesis on the regulation of glutamine synthetase of E.coli by covalent modification at the
                      Institute of Biochemistry, Universität Freiburg, Prof. Dr. Helmut Holzer
1972              Ph.D. (Dr.) Biochemistry - Universität Freiburg
1973-1975     Post Doctoral Research Fellow, Yeast Genetics - Cornell University, Ithaca, N.Y., USA.
                      Prof. Dr. Gerald R. Fink
1978              Habilitation, Biochemistry - Universität Freiburg

Academic Appointments
1975-1980     Research Assistant and Leader of a Research Group at the
                      Institute of Biochemistry, Universität Freiburg
1980-1985     Assistant Professor, Biochemistry - Universität Freiburg
1985-1989     Associate Professor, Biochemistry - Universität Freiburg
1989-2011     Professor, Chair and Director of the Institute of Biochemistry - Universität Stuttgart
1994-1995     Dean of the Faculty of Chemistry - Universität Stuttgart

Other Appointments
Member of the Adivory Editorial Board of the EMBO Journal

Previous Other Appointments
Member of the Editorial or Advisory Editorial Board of Microbiology, Yeast, Biological Chemistry, EMBO Reports.
Editor of the Book „Proteasomes: The World of Regulatory Proteolysis“ Landes Bioscience (2000)
(together with W. Hilt)
Guest Editor of a Multi-Author Review on the Ubiquitin-Proteasome System in Cellular and Molecular Life Sciences (CMLS) 61 (2004) (together with W. Hilt)
Guest Editor of a Special Issue of Biochimica et Biophysica Acta Molecular Cell Research 1695 (2004) on the Ubiquitin-Proteasome System (together with T. Sommer and W. Hilt)
Guest Editor of a Special Issue of Biochimica et Biophysica Acta Molecular Cell Research 1843 (2014) on the Ubiquitin-Proteasome System (together with T. Sommer)

Honors and Awards
1971                 Goedecke Research Award
1973                 Post-Doctoral Fellowship of the Deutsche Forschungsgemeinschaft (DFG)
1991                 Alexander von Humboldt – J. C. Mutis Award
1995                 Medal of Honor of the City of Clermont-Ferrand, France
2000                 Elected Member of the European Molecular Biology Organization (EMBO)
2007                 Research Prize of the Land Baden-Württemberg for Basic Research
2009                 Corresponding Member of the Heidelberg Academy of Sciences

Major Achievements of the Wolf Laboratory in the Past (175 Publications)
1975                Isolation of the first proteinase mutant of yeast for starting a study on the
                        function of intracellular proteolysis, an at the time neglected field of research
                        (J. Bacteriol. (1975) 123, 1150-1156).
1977 - 1988     Discovery of many novel proteinases of yeast, among those hormone
                        (pheromone) processing enzymes (EMBO J. (1985) 4, 173-177) and
                        proteinase yscE, the yeast proteasome (J. Biol. Chem. (1984) 259, 13344-13348).
1989                Discovery of the vacuolar (lysosomal) proteinases of yeast as essential
                        catalysts for massive protein degradation under starvation as well as for cell
                        differentiation (sporulation) and cell survival (J. Biol. Chem. (1989) 264, 16037-16045).
1991                Discovery of the proteasome as the essential proteinase of the ubiquitin
                        triggered degradation pathway of proteins in the cell ( in vivo) (EMBO J. (1991) 10, 555-562).
                        Since then the term„ubiqitin-proteasome pathway“ (UPS) is used.
1992                Degradation of proteins in denatured state in the inner cavity of the cylinder
                        of the proteasome (instead of on the outer surface, as proposed) is predicted
                        (Mol. Microbiol. (1992) 6, 2437-2442).
1991 – 1994    The genes of most 20S core subunits of the proteasome are identified and
                        analyzed (Biochemistry (1994) 33, 12229-12237).
1993                A first indication that the proteasome might be invoved in cell cycle
                        regulation is provided (FEBS Lett. (1993) 336, 34-36).
1994                Autophagcytosis mutants of yeast are isolated (FEBS Lett. (1994) 349, 275-280).
1994                Degradation of the first regulatory enzyme (fructose-1,6-bisphosphatase) by
                        the proteasome in the cell is discovered (Nature (1994) 369, 283-284).
1996                Retrograde transport of a fully glycosylated misfolded protein across the
                        membrane of the endoplasmic reticulum into the cytoplasm and its
                        ubiquitination and degradation by the proteasome is discovered. This finding
                        makes the dogma fall that proteins, once imported into the ER will never
                        return back into the cytosol. The finding discloses the basic mechanism of
                        ER-associated protein degradation (Science (1996) 273, 1725-1728;
                        Highlighted in: „Landmark Papers in Yeast Biology“ (P. Lindner, D. Shore,
                        M. N. Hall, eds.) Cold Spring Harbor Laboratory Press 2006).
                        With Der1 the first specific component of the ER-associated protein
                        degradation pathway is discovered (EMBO J. (1996) 15, 753-763).
                        Furthermore, N-glycosylation as a crucial determinant for ER-associated
                        protein degradation is disclosed (Yeast (1996) 12, 1229-1238).
1997                The active sites and their autocatalytic activation in the proteasome is
                        uncovered (J. Biol. Chem. (1997) 272, 25200-25209).
2001                Membrane topology and function as a ubiquitin ligase of ER-localized
                        Der3/Hrd1 is uncovered (J. Biol. Chem. (2001) 276, 10663-10669).
2008                Discovery of the Gid complex as a novel RING ubiquitin ligase involved in
                        regulation of carbohydrate metabolism. The orthologous Muskelin/CTLH
                        complex is proposed to be the mammalian counterpart (Mol. Biol. Cell
                        (2008) 19, 3323-3333).
2008                Discovery of the N-end rule ubiquitin ligase Ubr1 as the E3 directing
                        misfolded proteins of the cytoplasm to polyubiquitination and proteasomal
                        degradation (FEBS Lett. (2008) 582, 4143-4146).
2012                The topology of the seven-membered Gid ubiquitin ligase complex is
                        unraveled (J. Biol. Chem. (2012) 287, 25602-25614).
2013                The cytoplasmic ubiquitin ligase Ubr1 is discovered as an additional
                        ligase ubiquitinating misfolded membrane proteins of the
                        endoplasmic reticulum under stress and in the absence of the canonical
                        ER ligases. The finding links ER-associated protein degradation with
                        cytoplasmic protein quality control. (Proc. Natl. Acad. Sci. USA
                        (2013) 110, 15271-15276).

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