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Ubiquitin-Dependent Protein Degradation

  • S. Jentsch
  • W. Seufert
  • T. Sommer
  • H.-A. Reins
  • J. Jungmann
  • H.-P. Hauser
Conference paper
Part of the Colloquium der Gesellschaft für Biologische Chemie book series (MOSBACH, volume 43)

Abstract

Intracellular protein levels are controlled by protein synthesis and degradation. One major proteolytic pathway of eukaryotes requires the covalent attachment of ubiquitin, a small (8.5 kDa) and highly conserved protein, to proteolytic substrates prior to degradation (for reviews see Hershko 1991; Finley and Chau 1991; Jentsch et al. 1991, Jentsch 1992a; Jentsch 1992b). This pathway is highly selective and mediates the elimination of abnormal proteins and controls the half-lives of some regulatory proteins. Known targets include transcriptional regulators (Hochstrasser et al. 1991) p53 (Scheffner et al. 1990) and cyclins (Glotzer et al. 1991). In a number of eukaryotes, cyclin degradation is required to exit from mitosis.

Keywords

Spindle Pole Body Proteolytic Substrate Intracellular Protein Level Cyclin Degradation Enzyme UBC4 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Berlin Heidelberg 1993

Authors and Affiliations

  • S. Jentsch
    • 1
  • W. Seufert
    • 1
  • T. Sommer
    • 1
  • H.-A. Reins
    • 1
  • J. Jungmann
    • 1
  • H.-P. Hauser
    • 1
  1. 1.Friedrich-Miescher-Laboratorium der Max-Planck-GesellschaftTübingenGermany

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