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Ubiquitin-Proteasom-gesteuerte Regulation und Qualitätskontrolle der Zelle


Protein degradation by the ubiquitin-proteasome system (UPS) is essential for life. Degradation of enzymes and other regulatory proteins like activators or inhibitors is crucial for a multitude of cellular processes. Prominent examples are cell cycle progression or regulation of metabolic pathways. Furthermore, elimination of misfolded proteins is essential to prevent disturbance of cell functions.

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  1. Ciechanover A (2009) Tracing the history of the ubiquitin proteolytic system: the pioneering article. Biochem Biophys Res Commun 387:1–10

    CAS  Article  PubMed  Google Scholar 

  2. Bassermann F, Eichner R, Pagano M (2014) The ubiquitin proteasome system–implications for cell cycle control and the targeted treatment of cancer. Biochim Biophys Acta 1843:150–162

    CAS  Article  PubMed  Google Scholar 

  3. Amm I, Sommer T, Wolf DH (2014) Protein quality control and elimination of protein waste: the role of the ubiquitin-proteasome system. Biochim Biophys Acta 1843:182–196

    CAS  Article  PubMed  Google Scholar 

  4. Teichert U, Mechler B, Müller H et al. (1989) Lysosomal (vacuolar) proteinases of yeast are essential catalysts for protein degradation, differentiation, and cell survival. J Biol Chem 264:16037–16045

    CAS  PubMed  Google Scholar 

  5. Heinemeyer W, Kleinschmidt JA, Saidowsky J et al. (1991) Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase: mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival. EMBO J 10:555–562

    PubMed Central  CAS  PubMed  Google Scholar 

  6. Finley D, Ulrich HD, Sommer T et al. (2012) The ubiquitinproteasom system of Saccharomyces cerevisiae. Genetics 192:319–360

    PubMed Central  CAS  Article  PubMed  Google Scholar 

  7. Kachroo AH, Laurent JM, Yellmann CM et al. (2015) Systematic humanization of yeast genes reveals conserved functions and genetic modularity. Science 348:921–925

    CAS  Article  PubMed  Google Scholar 

  8. Schork SM, Bee G, Thumm M et al. (1994) Catabolite inactivation of fructose-1,6-bisphosphatase in yeast is mediated by the proteasome. FEBS Lett 349:270–274

    CAS  Article  PubMed  Google Scholar 

  9. Sannt O, Pfirrmann T, Braun B et al. (2008) The yeast GID complex, a novel ubiquitin ligase (E3) involved in the regulation of carbohydrate metabolism. Mol Biol Cell 19:3323–3333

    Article  Google Scholar 

  10. Menssen R, Schweiggert J, Schreiner J et al. (2012) Exploring the topology of the Gid complex, the E3 ubiquitin ligase involved in catabolite-induced degradation of gluconeogenic enzymes. J Biol Chem 287:25602–25614

    PubMed Central  CAS  Article  PubMed  Google Scholar 

  11. Pfirrmann T, Villavicencio-Lorini P, Subudhi AK et al. (2015) RMND5 from Xenopus laevis is an E3 ubiquitin-ligase and functions in early embryonic forebrain development. PLoS One 10:e0120342

    PubMed Central  Article  PubMed  Google Scholar 

  12. Scazzari M, Amm I, Wolf DH (2015) Quality control of a cytoplasmic protein complex: chaperone motors and the ubiquitin- proteasome system govern the fate of orphan fatty acid synthase subunit Fas2 of yeast. J Biol Chem 290:4677–4687

    CAS  Article  PubMed  Google Scholar 

  13. Hiller MM, Finger A, Schweiger M et al. (1996) ER degradation of a misfolded luminal protein by the cytosolic ubiquitin- proteasome pathway. Science 273:1725–1728

    CAS  Article  PubMed  Google Scholar 

  14. Stolz A, Besser S, Hottmann H et al. (2013) Previously unknown role for the ubiquitin ligase Ubr1 in endoplasmic reticulum-associated protein degradation. Proc Natl Acad Sci USA 110:15271–15276

    PubMed Central  CAS  Article  PubMed  Google Scholar 

  15. Krönke J, Fink EC, Hollenbach PW et al. (2015) Lenalidomide induces ubiquitination and degradation of CK1alpha in del(5q) MDS. Nature 523:183–188

    Article  PubMed  Google Scholar 

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Correspondence to Dieter H. Wolf.

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Ruth Menssen 19881993 Biochemiestudium an der FU Berlin; dort 19931997 Promotion. 19982002 Postdoktorandin am Institut für Industrielle Genetik der Uni versität Stuttgart. 20032007 Elternzeit. 20082010 Stipendiatin des Schlieben- Lange-Programms des Landes Baden-Württemberg. Seit 2011 Projektleiterin am Institut für Biochemie der Universität Stuttgart.

Dieter H. Wolf 19631968 Chemiestudium an der TU Karlsruhe und TU München. 19681972 Promotion am Institut für Biochemie an der Universität Freiburg. 19731975 Postdoktorand in der Abteilung für Genetik an der Cornell University, Ithaca, NY, USA. 19751980 Gruppenleiter am Institut für Biochemie der Universität Freiburg und Habilitation; ebenda 19801989 Professor. 19892011 Lehrstuhlinhaber und Direktor des Instituts für Biochemie der Universität Stuttgart. Seit 2011 Professor i. R. und Leiter einer Arbeitsgruppe zum Ubiquitin-Proteasom-System.

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Menssen, R., Wolf, D.H. Ubiquitin-Proteasom-gesteuerte Regulation und Qualitätskontrolle der Zelle. Biospektrum 21, 608–611 (2015).

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