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