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Título

Integration of multiple ubiquitin signals in proteasome regulation

Autor Isasa, Marta; Zuin, Alice; Crosas, Bernat
Palabras clave Rpn10
Proteasome
Ubiquitin
Fecha de publicación 2012
EditorSpringer
Citación Bioinformatics and Drug Discovery(Cap. 15): 337-370 (2012)
Methods in Molecular Biology 910
ResumenThe 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. © 2012 Springer Science+Business Media New York.
URI http://hdl.handle.net/10261/87913
DOI10.1007/978-1-61779-965-5_15
Identificadoresdoi: 10.1007/978-1-61779-965-5_15
isbn: 978-1-61779-964-8
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