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To eat, or NOt to eat: S ‐nitrosylation signaling in autophagy
Abstract
Autophagy is the main catabolic cellular process through which cells adapt their needs (e.g., growth and proliferation) to environmental availability of nutrients (e.g., amino acid and glucose) and growth factors. The rapid activation of the autophagy response essentially depends on protein post‐translational modifications (PTMs), which act as molecular switches triggering signaling cascades. Deregulation of autophagy contributes to pathological conditions, such as cancer and neurodegeneration. Therefore, understanding how PTMs affect the occurrence of autophagy is of the highest importance for clinical applications. Besides phosphorylation and ubiquitylation, which represent the best known examples of PTMs, redox‐based modifications are also emerging as contributing to the regulation of intracellular signaling. Of note, S ‐nitrosylation of cysteine residues is a redox PTM and is the principal mechanism of nitric oxide‐based signaling. Results emerging in recent years suggest that NO has a role in modulating autophagy. However, the function of S ‐nitrosylation in autophagy regulation remains still unveiled. By this review, we describe the upstream events regulating autophagy activation focusing on recently published evidence implying a S ‐nitrosylation‐dependent regulation.
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“Other important autophagy-related proteins such as ATG3, ATG5, ATG7 and ATG18A in plants are also targets for persulfidation, but the role of this modification needs further clarification [1009].”
From Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1 (2021) · cites this paper as [1009]
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Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1
Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., et al. (2021) · Autophagy · doi:10.1080/15548627.2020.1797280 · Cited by 2,897
Self-citation
Metadata
- Authors
- Montagna, C., Rizza, S., Maiani, E., Piredda, L., Filomeni, G., & Cecconi, F.
- Affiliations
- Danish Cancer Society Research Center Copenhagen Denmark
- Department of Biology University of Rome Tor Vergata Italy
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2016-05-05
- Volume
- 283
- Issue
- 21
- Pages
- 3857-3869
- ISSN
- 1742-464X
- 1742-4658
- Cited by
- 42
- References
- 11
- Language
- en
- Funders
- Kræftens Bekæmpelse (KBVU R72‐A4408, KBVU R72‐A4647)
- Lundbeckfonden (R167‐2013‐16100, R52‐A4895)
- Novo Nordisk (7559)
- Associazione Italiana per la Ricerca sul Cancro (11452, IG2012)
- Fondazione Italiana Sclerosi Multipla
- Fondazione Telethon (GGP14202)
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