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The Function of Modulators in Proteasome MHC Class I Antigen Processing Activity

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Symposium in Immunology VII

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Abstract

In eukaryotes the major non-lysosmal proteolytic system is characterized by a high-molecular-mass ATP-dependent 26S protease (for review see Coux et al. 1996). This complex is composed of the 20S proteasome, forming the proteolytic core, and the 19S regulator PA700, rendering ATP dependence and binding sites for ubiquitinated protein substrates (Rivett 1993; Hochstrasser 1995). The essential 26S enzyme complex is, in collaboration with the ubiquitin signalling pathway, responsible for the selective turnover of cytosolic and nuclear proteins.

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Authors
  1. P.-M. Kloetzel
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Editors and Affiliations

  1. Institut für Immunologie der Universität Wien, Borschkegasse 8 a, 1090, Wien, Austria

    Martha M. Eibl

  2. Abteilung Hämatologie, Johannes Gutenberg Universität, Langenbeckstr. 1, 55101, Mainz, Germany

    Christoph Huber

  3. Abteilung für Rheumatologie und Klinische Immunologie, Medizinische Universitätsklinik, Hugstetter Str. 55, 79106, Freiburg, Germany

    Hans H. Peter

  4. Pädiatrische Pneumologie und Immunologie, Universitäts-Klinikum Rudolf-Virchow Standort Charlottenburg, Heubnerweg 6, 14059, Berlin, Germany

    Ulrich Wahn

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© 1998 Springer-Verlag Berlin Heidelberg

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Kloetzel, PM. (1998). The Function of Modulators in Proteasome MHC Class I Antigen Processing Activity. In: Eibl, M.M., Huber, C., Peter, H.H., Wahn, U. (eds) Symposium in Immunology VII. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-80466-3_4

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  • DOI: https://doi.org/10.1007/978-3-642-80466-3_4

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-540-63360-0

  • Online ISBN: 978-3-642-80466-3

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