Regulation of autophagy by protein post-translational modification

• Published in: Laboratory investigation Vol. 95; no. 1; pp. 14 - 25
• Main Authors: Wani, Willayat Yousuf, Boyer-Guittaut, Michaël, Dodson, Matthew, Chatham, John, Darley-Usmar, Victor, Zhang, Jianhua
• Format: Journal Article
• Language: English
• Published: New York Elsevier Inc 01.01.2015; Nature Publishing Group US; Nature Publishing Group
• Subjects: 101/58; 14; 14/1; 14/19; 14/34; 14/35; 631/80/39/2346; 82/29; 82/80; 96/95; Animals; Autophagy - physiology; Humans; Laboratory Medicine; Medicine; Medicine & Public Health; mini-review; Mitophagy; Pathology; Phosphorylation; Protein Processing, Post-Translational; Proteins - metabolism; Proteins - physiology; Sulfhydryl Compounds - metabolism; Ubiquitination
• ISSN: 0023-6837; 1530-0307; 1530-0307
• DOI: 10.1038/labinvest.2014.131

Autophagy is a lysosome-mediated intracellular protein degradation process that involves about 38 autophagy-related genes as well as key signaling pathways that sense cellular metabolic and redox status, and has an important role in quality control of macromolecules and organelles. As with other major cellular pathways, autophagy proteins are subjected to regulatory post-translational modification. Phosphorylation is so far the most intensively studied post-translational modification in the autophagy process, followed by ubiquitination and acetylation. An interesting and new area is also now emerging, which appears to complement these more traditional mechanisms, and includes O-GlcNAcylation and redox regulation at thiol residues. Identification of the full spectrum of post-translational modifications of autophagy proteins, and determination of their impact on autophagy will be crucial for a better understanding of autophagy regulation, its deficits in diseases, and how to exploit this process for disease therapies.