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Limited and Degradative Proteolysis in the Context of Posttranslational Regulatory Networks: Current Technical and Conceptional Advances

  • Stefan Tholen
  • Maria Magdalena Koczorowska
  • Zon Weng Lai
  • Joern Dengjel
  • Oliver SchillingEmail author
Chapter

Abstract

Proteolytic processing is a major posttranslational modification (PTM) and essential in a variety of pathological and physiological processes. Proteolysis is integrated in a complex network of multiple PTMs, such as phosphorylation, acetylation or ubiquitination, that form a strongly regulated network. Currently the investigation of the co-operative action of proteolysis with other PTMs is emerging. Recently developed proteomic and degradomic techniques enable the determination of the active site specificity of proteases, the identification of in vivo substrates as well as the elucidation of the impact of proteases to proteome composition. Activity-based probes allow for detection and localization of protease activity.

This chapter provides a comprehensive overview of proteomic and degradomic tools that characterize protease action and highlights important nodes of the proteolytic network. Moreover it illustrates how proteolysis is modulated by other PTMs, and depicts its role in protein turnover.

Keywords

Cleavage Site Primary Amine Ubiquitin Proteasome System Limited Proteolysis Tobacco Etch Virus 
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.

Notes

Acknowledgements

O.S. is supported by the Deutsche Forschungsgemeinschaft (DFG, SCHI 871/2 (Emmy-Noether) and SCHI 871/5), a starting grant of the European Research Council (Programme “Ideas”—Call identifier: ERC-2011-StG 282111-ProteaSys), and the Excellence Initiative of the German Federal and State Governments (EXC 294, BIOSS). J.D. is supported by the Excellence Initiative of the German Federal and State Governments through Freiburg Institute for Advanced Studies (FRIAS), School of Life Sciences—LifeNet and the Center for Biological Signalling Studies (BIOSS), by grants DE 1757/2-1 from the German Research Foundation, DFG, and through GerontoSys II—NephAge (031 5896 A) from the German Ministry for Education and Research, BMBF.

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Copyright information

© Springer-Verlag Wien 2013

Authors and Affiliations

  • Stefan Tholen
    • 1
    • 2
  • Maria Magdalena Koczorowska
    • 1
  • Zon Weng Lai
    • 1
  • Joern Dengjel
    • 3
    • 4
    • 5
  • Oliver Schilling
    • 6
    • 7
    Email author
  1. 1.Institute for Molecular Medicine and Cell ResearchUniversity of FreiburgFreiburgGermany
  2. 2.Faculty of BiologyUniversity of FreiburgFreiburgGermany
  3. 3.Freiburg Institute for Advanced Studies (FRIAS), School of Life Science-LifeNetUniversity of FreiburgFreiburgGermany
  4. 4.ZBSA Center for Biological Systems AnalysisUniversity of FreiburgFreiburgGermany
  5. 5.BIOSS Centre for Biological Signaling StudiesUniversity of FreiburgFreiburgGermany
  6. 6.Institute for Molecular Medicine and Cell ResearchUniversity of FreiburgFreiburgGermany
  7. 7.BIOSS Centre for Biological Signaling StudiesUniversity of FreiburgFreiburgGermany

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