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Lab Invest. 2015 Jan;95(1):14-25. doi: 10.1038/labinvest.2014.131. Epub 2014 Nov 3.

Regulation of autophagy by protein post-translational modification.

Author information

1
1] Center for Free Radical Biology, University of Alabama at Birmingham, Birmingham, AL, USA [2] Department of Pathology, University of Alabama at Birmingham, Birmingham, AL, USA.
2
Laboratoire de Biochimie, EA3922, SFR IBCT FED4234, Sciences et Techniques, Université de Franche-Comté, Besançon Cedex, France.
3
1] Center for Free Radical Biology, University of Alabama at Birmingham, Birmingham, AL, USA [2] Department of Pathology, University of Alabama at Birmingham, Birmingham, AL, USA [3] Department of Veterans Affairs, Birmingham VA Medical Center, Birmingham, AL, USA.

Abstract

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.

PMID:
25365205
PMCID:
PMC4454381
DOI:
10.1038/labinvest.2014.131
[Indexed for MEDLINE]
Free PMC Article

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