Post-translational modifications of the energy guardian AMP-activated protein kinase
Journal article
Ovens, Ashley J., Scott, John W., Langendorf, Christopher G., Kemp, Bruce E., Oakhill, Jonathan S. and Smiles, William J.. (2021). Post-translational modifications of the energy guardian AMP-activated protein kinase. International Journal of Molecular Sciences. 22(3), p. Article 1229. https://doi.org/10.3390/ijms22031229
Authors | Ovens, Ashley J., Scott, John W., Langendorf, Christopher G., Kemp, Bruce E., Oakhill, Jonathan S. and Smiles, William J. |
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Abstract | 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. |
Keywords | AMPK; energy metabolism; phosphorylation; ubiquitination; oxidation |
Year | 2021 |
Journal | International Journal of Molecular Sciences |
Journal citation | 22 (3), p. Article 1229 |
Publisher | Multidisciplinary Digital Publishing Institute (MDPI AG) |
ISSN | 1422-0067 |
Digital Object Identifier (DOI) | https://doi.org/10.3390/ijms22031229 |
PubMed ID | 33513781 |
Scopus EID | 2-s2.0-85099909865 |
PubMed Central ID | PMC7866021 |
Open access | Published as ‘gold’ (paid) open access |
Research or scholarly | Research |
Page range | 1-28 |
Funder | National Health and Medical Research Council (NHMRC) |
Australian Research Council (ARC) | |
Publisher's version | License File Access Level Open |
Output status | Published |
Publication dates | |
Online | 27 Jan 2021 |
Publication process dates | |
Accepted | 22 Jan 2021 |
Deposited | 25 Mar 2022 |
ARC Funded Research | This output has been funded, wholly or partially, under the Australian Research Council Act 2001 |
Grant ID | NHMRC/1145265 |
NHMRC/1085460 | |
ARC/DP170101196 | |
NHMRC/1143080 |
https://acuresearchbank.acu.edu.au/item/8x9vv/post-translational-modifications-of-the-energy-guardian-amp-activated-protein-kinase
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Publisher's version
OA_Ovens_2021_Post_Translational_Modifications_of_the_Energy.pdf | |
License: CC BY 4.0 | |
File access level: Open |
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