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Assembly and Function of the Proteasome

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Ubiquitin Family Modifiers and the Proteasome

Part of the book series: Methods in Molecular Biology ((MIMB,volume 832))

Abstract

Proteasome is a highly organized protease complex comprising a catalytic 20S core particle (CP) and two 19S regulatory particles (RP), which together form the 26S structure. The 26S proteasome is responsible for the degradation of most ubiquitylated proteins through a multistep process involving recognition of the polyubiquitin chain, unfolding of the substrate, and translocation of the substrate into the active site in the cavity of the CP. Recent studies have shed light on various aspects of the complex functions of the 26S proteasome. In addition, the recent identification of various proteasome-dedicated chaperones indicates that the assembly pathways of the RP and CP are multistep processes. In this review, we summarize recent advances in the understanding of the proteasome structure, function, and assembly.

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Acknowledgments

We thank E. Sakata and W. Baumeister (Max Planck Institute of Biochemistry, Germany) for the cryo-EM image of the 26S proteasome. This work was supported by grants from the Ministry of Education, Culture, Sports, Science and Technology (MEXT) of Japan; the Targeted Proteins Research Program; and Health and Labor Science Research Grants.

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Authors and Affiliations

  1. Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan

    Yasushi Saeki & Keiji Tanaka

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  1. Yasushi Saeki
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  2. Keiji Tanaka
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Correspondence to Keiji Tanaka .

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  1. Institut für Genetik, Universität Köln, Zülpicher Str. 47, Köln, 50674, Germany

    R. Jürgen Dohmen

  2. Fak. Biologie, Universität Konstanz, Konstanz, 78457, Germany

    Martin Scheffner

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Saeki, Y., Tanaka, K. (2012). Assembly and Function of the Proteasome. In: Dohmen, R., Scheffner, M. (eds) Ubiquitin Family Modifiers and the Proteasome. Methods in Molecular Biology, vol 832. Humana Press. https://doi.org/10.1007/978-1-61779-474-2_22

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  • DOI: https://doi.org/10.1007/978-1-61779-474-2_22

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  • Print ISBN: 978-1-61779-473-5

  • Online ISBN: 978-1-61779-474-2

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