Chapter title |
Proteostasis
|
---|---|
Chapter number | 5 |
Book title |
Proteostasis
|
Published in |
Methods in molecular biology, January 2016
|
DOI | 10.1007/978-1-4939-3756-1_5 |
Pubmed ID | |
Book ISBNs |
978-1-4939-3754-7, 978-1-4939-3756-1
|
Authors |
Hovsepian, Junie, Becuwe, Michel, Kleifeld, Oded, Glickman, Michael H, Léon, Sébastien, Junie Hovsepian, Michel Becuwe, Oded Kleifeld, Michael H. Glickman, Sébastien Léon |
Editors |
Rune Matthiesen |
Abstract |
Ubiquitylation is a reversible posttranslational modification that is critical for most, if not all, cellular processes and essential for viability. Ubiquitin conjugates to substrate proteins either as a single moiety (monoubiquitylation) or as polymers composed of ubiquitin molecules linked to each other with various topologies and structures (polyubiquitylation). This contributes to an elaborate ubiquitin code that is decrypted by specific ubiquitin-binding proteins. Indeed, these different types of ubiquitylation have different functional outcomes, notably affecting the stability of the substrate, its interactions, its activity, or its subcellular localization. In this chapter, we describe protocols to determine whether a protein is ubiquitylated, to identify the site that is ubiquitylated, and provide direction to study the topology of the ubiquitin modification, in the yeast Saccharomyces cerevisiae. |
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