Lysine modifications and autophagy.
Nutrient deprivation or cellular stress leads to the activation of a catabolic pathway that is conserved across species, known as autophagy. This process is considered to be adaptive and plays an important role in a number of cellular processes, including metabolism, immunity and development. Autophagy has also been linked to diseases, such as cancer and neurodegeneration, highlighting the importance of a better insight into its regulation. In the present chapter, we discuss how PTMs (post-translational modifications) of lysine residues by acetylation and ubiquitination alter the function of key proteins involved in the activation, maturation and substrate selectivity of autophagy. We also discuss the clinical potential of targeting these modifications to modulate autophagic activities.
Duke Scholars
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Related Subject Headings
- Ubiquitination
- Protein Processing, Post-Translational
- Lysine
- Humans
- Biochemistry & Molecular Biology
- Autophagy
- Animals
- 3101 Biochemistry and cell biology
- 0601 Biochemistry and Cell Biology
Citation
Published In
DOI
EISSN
Publication Date
Volume
Start / End Page
Location
Related Subject Headings
- Ubiquitination
- Protein Processing, Post-Translational
- Lysine
- Humans
- Biochemistry & Molecular Biology
- Autophagy
- Animals
- 3101 Biochemistry and cell biology
- 0601 Biochemistry and Cell Biology