Post-Translational Modifications of the Energy Guardian AMP-Activated Protein Kinase

Physical exercise elicits physiological metabolic perturbations such as energetic and oxidative stress; however, a diverse range of cellular processes are stimulated in response to combat these challenges and maintain cellular energy homeostasis. AMP-activated protein kinase (AMPK) is a highly conse...

Full description

Saved in:
Bibliographic Details
Published inInternational journal of molecular sciences Vol. 22; no. 3; p. 1229
Main Authors Ovens, Ashley J., Scott, John W., Langendorf, Christopher G., Kemp, Bruce E., Oakhill, Jonathan S., Smiles, William J.
Format Journal Article
LanguageEnglish
Published Switzerland MDPI 27.01.2021
Subjects
Acetylation
AMP-Activated Protein Kinases - chemistry
AMP-Activated Protein Kinases - genetics
AMP-Activated Protein Kinases - metabolism
Animals
Energy Metabolism
Homeostasis
Humans
Methylation
Oxidation-Reduction
Oxidative Stress
Phosphorylation
Protein Domains
Protein Processing, Post-Translational
Review
Signal Transduction - genetics
Ubiquitination
oxidation
AMPK
ubiquitination
phosphorylation
energy metabolism
Online AccessGet full text
ISSN1422-0067
1422-0067
DOI10.3390/ijms22031229

Cover

More Information
Summary:Physical exercise elicits physiological metabolic perturbations such as energetic and oxidative stress; however, a diverse range of cellular processes are stimulated in response to combat these challenges and maintain cellular energy homeostasis. AMP-activated protein kinase (AMPK) is a highly conserved enzyme that acts as a metabolic fuel sensor and is central to this adaptive response to exercise. The complexity of AMPK’s role in modulating a range of cellular signalling cascades is well documented, yet aside from its well-characterised regulation by activation loop phosphorylation, AMPK is further subject to a multitude of additional regulatory stimuli. Therefore, in this review we comprehensively outline current knowledge around the post-translational modifications of AMPK, including novel phosphorylation sites, as well as underappreciated roles for ubiquitination, sumoylation, acetylation, methylation and oxidation. We provide insight into the physiological ramifications of these AMPK modifications, which not only affect its activity, but also subcellular localisation, nutrient interactions and protein stability. Lastly, we highlight the current knowledge gaps in this area of AMPK research and provide perspectives on how the field can apply greater rigour to the characterisation of novel AMPK regulatory modifications.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
ObjectType-Review-3
content type line 23
ISSN:1422-0067
1422-0067
DOI:10.3390/ijms22031229