Resumen
Ubiquitination is a prevalent post-translation modification system that is involved in almost all aspects of eukaryotic biology. It involves the attachment of ubiquitin, a small, highly conserved protein to selected substrates. The most notable function of ubiquitin is the targeting of modified proteins to the multi-proteolytic 26S proteasome complex for degradation. The ubiquitin proteasome system (UPS) regulates the abundance of numerous enzymes, structural and regulatory proteins ensuring proper cellular function. Plants utilize the UPS to facilitate cellular changes required to respond to and tolerate adverse growth conditions. In this review, the regulatory role of the UPS in responses to abiotic stress is discussed, particularly the function of ubiquitin-dependent degradation in the suppression, activation and attenuation or termination of stress signaling.
Idioma original | English |
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Título de la publicación alojada | International Review of Cell and Molecular Biology |
Editores | Lorenzo Galluzzi |
Editorial | Elsevier Inc. |
Páginas | 65-110 |
Número de páginas | 46 |
ISBN (versión impresa) | 9780128167038 |
DOI | |
Estado | Published - 2019 |
Serie de la publicación
Nombre | International Review of Cell and Molecular Biology |
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Volumen | 343 |
ISSN (versión impresa) | 1937-6448 |
Nota bibliográfica
Publisher Copyright:© 2019 Elsevier Inc.
ASJC Scopus Subject Areas
- Biochemistry
- Molecular Biology
- Cell Biology
PubMed: MeSH publication types
- Journal Article
- Review