Format

Send to

Choose Destination
Am J Physiol Cell Physiol. 2016 Sep 1;311(3):C351-62. doi: 10.1152/ajpcell.00129.2016. Epub 2016 Jun 22.

Fine-tuning autophagy: from transcriptional to posttranslational regulation.

Author information

1
Institut Necker-Enfants Malades, Institut National de la Santé et de la Recherche Médicale U1151-Centre National de la Recherche Scientifique UMR 8253, Paris, France; Université Paris Diderot-Sorbonne Paris Cité, Paris, France; and.
2
Institut Necker-Enfants Malades, Institut National de la Santé et de la Recherche Médicale U1151-Centre National de la Recherche Scientifique UMR 8253, Paris, France; Université Paris Descartes-Sorbonne Paris Cité, Paris, France.
3
Institut Necker-Enfants Malades, Institut National de la Santé et de la Recherche Médicale U1151-Centre National de la Recherche Scientifique UMR 8253, Paris, France; Université Paris Descartes-Sorbonne Paris Cité, Paris, France patrice.codogno@inserm.fr.

Abstract

Macroautophagy (hereafter called autophagy) is a vacuolar lysosomal pathway for degradation of intracellular material in eukaryotic cells. Autophagy plays crucial roles in tissue homeostasis, in adaptation to stress situations, and in immune and inflammatory responses. Alteration of autophagy is associated with cancer, diabetes and obesity, cardiovascular disease, neurodegenerative disease, autoimmune disease, infection, and chronic inflammatory disease. Autophagy is controlled by autophagy-related (ATG) proteins that act in a coordinated manner to build up the initial autophagic vacuole named the autophagosome. It is now known that the activities of ATG proteins are modulated by posttranslational modifications such as phosphorylation, ubiquitination, and acetylation. Moreover, transcriptional and epigenetic controls are involved in the regulation of autophagy in stress situations. Here we summarize and discuss how posttranslational modifications and transcriptional and epigenetic controls regulate the involvement of autophagy in the proteostasis network.

KEYWORDS:

acetylation; macroautophagy; phosphorylation; posttranslational modifications; transcription; ubiquitination

PMID:
27335173
DOI:
10.1152/ajpcell.00129.2016
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Atypon
Loading ...
Support Center