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Integration of Multiple Ubiquitin Signals in Proteasome Regulation

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Bioinformatics and Drug Discovery

Part of the book series: Methods in Molecular Biology ((MIMB,volume 910))

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Abstract

The ubiquitin–proteasome system has emerged in the last decades as a new paradigm in cell physiology. Ubiquitin is found in fundamental levels of cell regulation, as a target for degradation to the proteasome or as a signal that controls protein function in a complex manner. Even though many aspects of the ubiquitin system remain unexplored, the contributions on the field uncover that ubiquitin represents one of the most sophisticated codes in cellular biology.

The proteasome is an ATP-dependent protease that degrades a large number of protein substrates in the cell. The proteasome recruits substrates by a number of receptors that interact with polyubiquitin. Recently, it has been shown that one of these receptors, Rpn10, is regulated by monoubiquitination. In this chapter, we show an overview of the central aspects of the pathway and describe the methodology to characterize in vitro the monoubiquitination of proteasome subunits.

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Authors and Affiliations

  1. Proteasome Regulation Lab, Cell Biology Department, Institute of Molecular Biology of Barcelona (CSIC), Barcelona, Spain

    Marta Isasa, Alice Zuin & Bernat Crosas

Authors
  1. Marta Isasa
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  2. Alice Zuin
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  3. Bernat Crosas
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Correspondence to Bernat Crosas .

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Editors and Affiliations

  1. , Department of Pathology, The University of New Mexico, Camino de Salud 915, Albuquerque, 87131, New Mexico, USA

    Richard S. Larson

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Isasa, M., Zuin, A., Crosas, B. (2012). Integration of Multiple Ubiquitin Signals in Proteasome Regulation. In: Larson, R. (eds) Bioinformatics and Drug Discovery. Methods in Molecular Biology, vol 910. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-61779-965-5_15

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  • DOI: https://doi.org/10.1007/978-1-61779-965-5_15

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  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-1-61779-964-8

  • Online ISBN: 978-1-61779-965-5

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