Dieses Bild zeigt Wolf

Herr Prof. Dr.

Dieter H. Wolf

Prof. (im Ruhestand)
Abteilung Biochemie, Institut für Biochemie und Technische Biochemie

Kontakt

0711 685 64371
0711 685 64392

Allmandring 31
70569 Stuttgart
Deutschland
Raum: 01.189

Fachgebiet

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

Education
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 „ubiquitin-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).