The Role of AMPK in the Regulation of Skeletal Muscle Size, Hypertrophy, and Regeneration
Open accessAbstract
AMPK (5’-adenosine monophosphate-activated protein kinase) is heavily involved in skeletal muscle metabolic control through its regulation of many downstream targets. Because of their effects on anabolic and catabolic cellular processes, AMPK plays an important role in the control of skeletal muscle development and growth. In this review, the effects of AMPK signaling, and those of its upstream activator, liver kinase B1 (LKB1), on skeletal muscle growth and atrophy are reviewed. The effect of AMPK activity on satellite cell-mediated muscle growth and regeneration after injury is also reviewed. Together, the current data indicate that AMPK does play an important role in regulating muscle mass and regeneration, with AMPKα1 playing a prominent role in stimulating anabolism and in regulating satellite cell dynamics during regeneration, and AMPKα2 playing a potentially more important role in regulating muscle degradation during atrophy.
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AMPK can inhibit RNA polymerase I activity through multiple mechanisms, including suppression of TIF-1A function and modulation of chromatin accessibility at rDNA loci.
“AMPK can inhibit RNA polymerase I activity through multiple mechanisms, including suppression of TIF-1A function and modulation of chromatin accessibility at rDNA loci”
From Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators (2026) · cites this paper as [62]
Section 3.1 discusses AMPK inhibition of protein synthesis through mTORC1 and eEF2, not inhibition of RNA polymerase I. Searches for TIF-1A, rDNA chromatin accessibility, and ribosomal RNA transcription found no passage addressing the claimed mechanisms; page numbers were not available in our copy. (LLM, conf=0.75)
Experimental — accuracy not yet measuredA novel biomechanical stimulus might initiate Pol I, but concurrent metabolic stress might abort snoRNA-guided processing downstream, leading to aborted assembly despite massive precursor transcripts.
“A novel biomechanical stimulus might successfully initiate Pol I, but concurrent metabolic stress might abort snoRNA-guided processing downstream, leading to aborted assembly despite massive precursor transcripts [60,62].”
From Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators (2026) · cites this paper as [62]
Section 3.1 discusses AMPK-mediated inhibition of protein translation through mTORC1 and eEF2, not the proposed interruption of ribosome assembly. Searches for Pol I initiation, snoRNA-guided processing, and precursor transcripts found no passage addressing that sequence; the copy therefore cannot verify the claim. (LLM, conf=0.76)
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“Initial observations in dominant-negative AMPK (AMPK-DN) transgenic mice in which a dominant negative AMPKα2 subunit was overexpressed under the muscle creatine kinase promoter (expressed in heart and skeletal muscle) showed that EDL muscles tended to be larger than in wild-type (WT) mice, suggesting that AMPK might n…”
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Evidence for control of protein synthesis in HeLa cells via the elongation rate
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AMPK inhibits myoblast differentiation through a PGC-1α-dependent mechanism
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Promise and challenges for direct small molecule AMPK activators
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LKB1 and the regulation of malonyl-CoA and fatty acid oxidation in muscle
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TAK1 regulates skeletal muscle mass and mitochondrial function
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Ablation of LKB1 in the heart leads to energy deprivation and impaired cardiac function
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Chronic paraplegia-induced muscle atrophy downregulates the mTOR/S6K1 signaling pathway
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Self-citationMitochondrial and performance adaptations to exercise training in mice lacking skeletal muscle LKB1
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Self-citationThe Role of T Lymphocytes in Skeletal Muscle Repair From Traumatic and Contraction-Induced Injury
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Skeletal muscle dysfunction in muscle-specific LKB1 knockout mice.
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Self-citationResponses of Skeletal Muscle Hypertrophy in Wistar Rats to Different Resistance Exercise Models
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The AMPK-related kinase SNARK regulates muscle mass and myocyte survival
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LKB1 Destabilizes Microtubules in Myoblasts and Contributes to Myoblast Differentiation
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AMP-activated kinase α2 deficiency protects mice from denervation-induced skeletal muscle atrophy
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Myostatin inhibits eEF2K-eEF2 by regulating AMPK to suppress protein synthesis
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The effect of caffeine on skeletal muscle anabolic signaling and hypertrophy.
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“Known Unknowns”: Current Questions in Muscle Satellite Cell Biology
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Self-citationLkb1 deletion upregulates Pax7 expression through activating Notch signaling pathway in myoblasts
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Mechanisms of IGF-1-Mediated Regulation of Skeletal Muscle Hypertrophy and Atrophy
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“Importantly, IGF-1 level is reduced in both of these atrophying conditions and Akt is inhibited in skeletal muscle, although the role of AMPK (which is known to inhibit Akt/mTOR and activate FoxO [78,92]) in relation to IGF-1 signaling in atrophying conditions is not clear.”
BackgroundSarcopenia and Muscle Aging: A Brief Overview
Dao, T., Green, A. E., Kim, Y.-A., Bae, S., Ha, K., Gariani, K., Lee, M.-R., Menzies, K. J., & Ryu, D. (2020) · Endocrinology and Metabolism · doi:10.3803/enm.2020.405 · Cited by 228 · see citing works
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“AMPK, a potential longevity target [66], plays an important role in the regulation of skeletal muscle mass and regeneration [67].”
BackgroundVarghese, S., Rao, S., Khattak, A., Zamir, F., & Chaari, A. (2024) · Nutrients · doi:10.3390/nu16213663 · Cited by 152 · see citing works
The flesh texture of teleost fish: Characteristics and interventional strategies
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“of AMPK, which can in turn inhibit the mTOR signaling pathway, and p70S6K is immediately downstream of mTOR complex 1 (mTORC1) [108].”
BackgroundRoles of mTOR Signaling in Tissue Regeneration
Wei, X., Luo, L., & Chen, J.-Z. (2019) · Cells · doi:10.3390/cells8091075 · Cited by 132 · see citing works
“Their progenies either maintain the satellite cells pool through self-renewal or differentiate into myoblasts expressing myogenic markers Myf5 (myogenic factor 5), MyoD (myogenic differentiation 1), myogenin and MRF4 (myogenic regulatory factor 4) [130,133] (Figure 3C).”
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Organ protection by SGLT2 inhibitors: role of metabolic energy and water conservation
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“Moreover, low energy levels in muscle fibers are also associated with increased AMP-kinase (AMPK) activity, which is associated with inhibition of mTORC directly or indirectly (reviewed in [49]).”
BackgroundGuo, A., Li, K., Tian, H., Fan, Z., Chen, Q., Yang, Y., Yu, J., Wu, Y., & Xiao, Q. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16448 · Cited by 112 · see citing works
Metformin induces muscle atrophy by transcriptional regulation of myostatin via HDAC6 and FoxO3a
Kang, M. J., Moon, J. W., Lee, J. O., Kim, J. H., Jung, E. J., Kim, S. J., Oh, J. Y., Wu, S. W., Lee, P. R., Park, S. H., et al. (2021) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12833 · Cited by 102 · see citing works
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Ubiquitin Ligases at the Heart of Skeletal Muscle Atrophy Control
Peris-Moreno, D., Cussonneau, L., Combaret, L., Polge, C., & Taillandier, D. (2021) · Molecules · doi:10.3390/molecules26020407 · Cited by 87 · see citing works
“Additionally, AMPK also promotes skeletal muscle autophagy [88].”
Sekar, P., Hsiao, G., Hsu, S.-H., Huang, D.-Y., Lin, W., & Chan, C.-M. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102786 · Cited by 84 · see citing works
The hallmarks of myotonic dystrophy type 1 muscle dysfunction
Ozimski, L. L., Sabater-Arcis, M., Bargiela, A., & Artero, R. D. (2020) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12674 · Cited by 81 · see citing works
“AMPK has been shown to play a vital role in maintaining and remodelling skeletal muscle (Thomson, 2018).”
BackgroundYan, Y., Li, M., Lin, J., Ji, Y., Wang, K., Yan, D., Shen, Y., Wang, W., Huang, Z., Jiang, H., et al. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.947387 · Cited by 81 · see citing works
“AMPK inhibits the protein synthesis by inhibiting the activities of mechanistic target of rapamycin, complex 1 (mTORC1) and eukaryotic elongation factor 2 (eEF2) (Thomson, 2018).”
BackgroundVignaud, J., Loiseau, C., Hérault, J., Mayer, C., Côme, M., Martin, I., & Ulmann, L. (2023) · Antioxidants · doi:10.3390/antiox12051050 · Cited by 72 · see citing works
“In contrast, during muscle disease associated with mitochondrial dysfunction, AMPK suppresses the MPS via an inhibition of mTORC1 [49].”
BackgroundRybalka, E., Timpani, C. A., Debruin, D. A., Bagaric, R. M., Campelj, D. G., & Hayes, A. (2020) · Cells · doi:10.3390/cells9122657 · Cited by 65 · see citing works
“In this regard, myostatin may act as an environmental sensor/signaler of nutritional status (particularly in a low amino acid environment) [10] in synergy with the cellular energy sensor, adenosine monophosphate-activated protein kinase (AMPK) [11], promoting a negative feedback loop that inhibits ribosomal biogenesis…”
BackgroundInfluentialMishra, S., Cosentino, C., Tamta, A. K., Khan, D., Srinivasan, S., Ravi, V., Abbotto, E., Arathi, B. P., Kumar, S. A., Jain, A., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-32905-w · Cited by 56 · see citing works
Livshits, G., & Kalinkovich, A. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101852 · Cited by 55 · see citing works
Post‐translational regulation of muscle growth, muscle aging and sarcopenia
Zhong, Q., Zheng, K., Li, W., An, K., Liu, Y., Xiao, X., Hai, S., Dong, B., Li, S., An, Z., et al. (2023) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.13241 · Cited by 54 · see citing works
“tion of mTOR in response to energy expenditure and reduced protein synthesis.(30) In damaged muscle, the activation of the AMPK signalling pathway enhances the transcriptional activ-”
BackgroundThe Role of Mitophagy in Skeletal Muscle Damage and Regeneration
Chatzinikita, E., Maridaki, M. D., Palikaras, K., Koutsilieris, M., & Philippou, Α. (2023) · Cells · doi:10.3390/cells12050716 · Cited by 53 · see citing works
SIRT1 signaling pathways in sarcopenia: Novel mechanisms and potential therapeutic targets
Yang, L., Liu, D., Jiang, S., Li, H., Chen, L., Wu, Y., Essien, A. E., Opoku, M., Naranmandakh, S., Liu, S., et al. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116917 · Cited by 54 · see citing works
Daidzein alleviates cisplatin‐induced muscle atrophy by regulating Glut4/ AMPK / FoxO pathway
Zhang, H., Chi, M., Chen, L., Sun, X., Wan, L., Yang, Q., & Guo, C. (2021) · Phytotherapy Research · doi:10.1002/ptr.7132 · Cited by 52 · see citing works
“skeletal muscle atrophy, and activation of AMPK can promote the expression of FoxO in the nucleus (Greer et al., 2007; Thomson, 2018).”
BackgroundToda, K., Yamauchi, Y., Tanaka, A., Kuhara, T., Odamaki, T., Yoshimoto, S., & Xiao, J. (2020) · Nutrients · doi:10.3390/nu12010219 · Cited by 53 · see citing works
“B-3HK significantly promoted the activation of AMPK (Figure 4A,B), which regulates energy balance at both the cellular and physiological levels as a master regulator of metabolism [22,23].”
BackgroundAshtary-Larky, D., Bagheri, R., Asbaghi, O., Tinsley, G. M., Kooti, W., Abbasnezhad, A., Afrisham, R., & Wong, A. (2022) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2021.1890689 · Cited by 50 · see citing works
“Importantly, differences in stored glycogen and the associated water content could influence BM results, along with other body composition outcomes, when comparing KD and non-KD regimens (Tinsley and Willoughby 2016).”
BackgroundResultInfluentialmiR-7 Restores Phenotypes in Myotonic Dystrophy Muscle Cells by Repressing Hyperactivated Autophagy
Sabater-Arcis, M., Bargiela, A., Furling, D., & Artero, R. D. (2019) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2019.11.012 · Cited by 48 · see citing works
“AMPK is involved in the regulation of several metabolic pathways that regulate muscle size, such as autophagy and UPS activation or inhibition of protein synthesis via mTOR blockade.(49) However, our data suggest that this pathway remains unaltered in DM1 and that, in consequence, the activation of autophagy and UPS s…”
BackgroundHuang, Y., Wang, C., Cui, H., Sun, G., Qi, X., & Yao, X. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1590524 · Cited by 45 · see citing works
“AMPK can be strongly activated in skeletal muscle by repeated muscle contractions and exercise (Thomson, 2018).”
Xie, Y., Gu, Y., Li, Z., He, B., & Zhang, L. (2024) · Nutrients · doi:10.3390/nu16173007 · Cited by 48 · see citing works
“However, there is a lack of literature directly comparing the four dietary interventions combined with exercise, which makes the results more susceptible to the influence of indirect comparisons.”
BackgroundTherapeutic Implications of miRNAs for Muscle-Wasting Conditions
Yedigaryan, L., & Sampaolesi, M. (2021) · Cells · doi:10.3390/cells10113035 · Cited by 43 · see citing works
“Additionally, AMPK suppresses anabolic processes such as protein synthesis [76].”
BackgroundEffects of Various Muscle Disuse States and Countermeasures on Muscle Molecular Signaling
Sharlo, K. A., Tyganov, S. A., Tomilovskaya, E., Popov, D. V., Saveko, A. A., & Shenkman, B. S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010468 · Cited by 45 · see citing works
“When activated, AMPK can suppress mTORC1 signaling through the phosphorylation and activation of TSC2 [116] or the phosphorylation of Raptor (regulatory-associated protein of mammalian target of rapamycin, a part of the mTORC1 complex), which leads to its subsequent sequestration by regulatory proteins of the 14-3-3 f…”
BackgroundHuang, C., Ge, F., Ma, X., Dai, R., Dingkao, R., Zhuoma, Z., Burenchao, G., Bao, P., Wu, X., Guo, X., et al. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.772557 · Cited by 39 · see citing works
“A total of 117 DEMs were identified that were related to the differentiation and proliferation of myoblasts, AMPK signaling pathway, MAPK signaling pathway, PI3K–Akt signaling pathway, etc. (Neri et al., 2002; Anderson, 2006; Gehart et al., 2010; Thomson, 2018).”
BackgroundNAD+ centric mechanisms and molecular determinants of skeletal muscle disease and aging
Wagner, S., Manickam, R., Brotto, M. A. P., & Tipparaju, S. M. (2022) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-022-04408-1 · Cited by 39 · see citing works
Regenerating Myofibers after an Acute Muscle Injury: What Do We Really Know about Them?
Pizza, F. X., & Buckley, K. H. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241612545 · Cited by 37 · see citing works
Skeletal muscle atrophy after sciatic nerve damage: Mechanistic insights
Yadav, A., & Dabur, R. (2024) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2024.176506 · Cited by 38 · see citing works
A transition to degeneration triggered by oxidative stress in degenerative disorders
Stern, M., & McNew, J. A. (2020) · Molecular Psychiatry · doi:10.1038/s41380-020-00943-9 · Cited by 33 · see citing works
Pathophysiological changes of muscle after ischemic stroke: a secondary consequence of stroke injury
Hu, Q., Tian, D., Luan, F., Yang, R., & Zeng, N. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.382221 · Cited by 33 · see citing works
“…proliferators-activated receptor γ coactivator 1 alpha (PGC-1α) plays a role in promoting slow muscle fiber expression and pro-mitotic mitochondrial biosynthesis to improve motility (Boström et al., 2012), and changes in AMPK levels are positively correlated with PGC-1α expression (Thomson, 2018).”
Fukada, S., & Ito, N. (2021) · Experimental Cell Research · doi:10.1016/j.yexcr.2021.112907 · Cited by 31 · see citing works
Fovet, T., Guilhot, C., Delobel, P., Chopard, A., Py, G., & Brioche, T. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.834597 · Cited by 29 · see citing works
“This is consistent with the lower metabolic stress observed in ET muscles, because such stress normally delays protein synthesis activation after physical activity (MacDougall et al., 1995; Bolster et al., 2002; Dreyer et al., 2006; Thomson, 2018).”
ResultVerpoorten, S., Sfyri, P., Scully, D., Mitchell, R., Tzimou, A., Mougios, V., Patel, K., & Matsakas, A. (2019) · Acta Physiologica · doi:10.1111/apha.13395 · Cited by 30 · see citing works
Slc20a1/Pit1 and Slc20a2/Pit2 are essential for normal skeletal myofiber function and survival
Chande, S., Caballero, D., Ho, B., Fetene, J. A., Serna, J., Pesta, D. H., Nasiri, A. R., Jurczak, M. J., Chavkin, N. W., Hernando, N., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-59430-4 · Cited by 30 · see citing works
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Sun, C., Yang, D. K., Chen, Z., Xiao, J., Xiao, Q., Li, C., Zhou, Z., Peng, X., Tang, C., & Zheng, L. (2022) · FEBS Journal · doi:10.1111/febs.16637 · Cited by 29 · see citing works
Sataranatarajan, K., Pharaoh, G. A., Brown, J. L., Ranjit, R., Piekarz, K. M., Street, K., Wren, J. D., Georgescu, C., Kinter, C. S., Kinter, M. T., et al. (2020) · GeroScience · doi:10.1007/s11357-020-00189-x · Cited by 29 · see citing works
LncEDCH1 improves mitochondrial function to reduce muscle atrophy by interacting with SERCA2
Cai, B., Ma, M., Zhang, J., Wang, Z., Kong, S., Zhou, Z., Lian, L., Zhang, J., Li, J., Wang, Y., et al. (2021) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2021.12.004 · Cited by 29 · see citing works
Salucci, S., Bartoletti‐Stella, A., Bavelloni, A., Aramini, B., Blalock, W. L., Fabbri, F., Vannini, I., Sambri, V., Stella, F., & Faenza, I. (2022) · Nutrients · doi:10.3390/nu14173567 · Cited by 30 · see citing works
“Moreover, mTORC1 inhibition blocks muscle hypertrophy in post-natal development and muscle regeneration [51].”
BackgroundGinseng and ginsenosides: Therapeutic potential for sarcopenia
Zha, W., Sun, Y., Gong, W., Li, L., Kim, W., & Li, H. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113876 · Cited by 29 · see citing works
Molecular mechanisms of post‐burn muscle wasting and the therapeutic potential of physical exercise
Dombrecht, D., Daele, U. V., Asbroeck, B. V., Schieffelers, D. R., Guns, P., Gebruers, N., Meirte, J., & van Breda, E. (2023) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.13188 · Cited by 28 · see citing works
“tein kinase (AMPK), a key regulator of energy homoeostasis with a critical role as energy sensor during exercise and metabolic disorders.(32) AMPK is involved in both anabolic and catabolic pathways, maintaining energy stores and ensuring a balance between energy supply and demand, whereas in skeletal muscle AMPK inhi…”
BackgroundLiu, X., Zhao, L., Gao, Y., Chen, Y., Tian, Q., Son, J. S., Chae, S. A., de Avila, J. M., Zhu, M. J., & Du, . (2022) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.13150 · Cited by 28 · see citing works
“Notably, AMPK also regulates skeletal muscle development and regeneration.(18) During muscle regeneration, inflammatory response is meticulously modulated.”
BackgroundJun, L., Tao, Y.-X., Geetha, T., & Babu, J. R. (2024) · Current Nutrition Reports · doi:10.1007/s13668-024-00555-7 · Cited by 27 · see citing works
“Specifically, phosphorylation of AMPKα1 subunit at Thr183 plays a prominent role in stimulating anabolism during regeneration process, while phosphorylation of AMPKα2 subunit at Thr172 plays a role in regulating muscle degradation during atrophy [37].”
BackgroundHan, J.-Y., Park, M., & Lee, H. (2023) · BMC Complementary Medicine and Therapies · doi:10.1186/s12906-023-04033-5 · Cited by 27 · see citing works
“AMP-activated protein kinase-α (AMPKα), a central regulator of mitochondrial biogenesis, controls intracellular energy balance and is an essential factor in skeletal muscle atrophy [17, 18].”
BackgroundShimizu, J., & Kawano, F. (2022) · The Journal of Physiology · doi:10.1113/jp282917 · Cited by 26 · see citing works
“AMPK is activated via phosphorylation by metabolic stress and functions to switch cellular fuel utilization from glucose to fatty acids, stimulating mitochondrial biogenesis (Thomson, 2018).”
BackgroundAlcohol, Resistance Exercise, and mTOR Pathway Signaling: An Evidence-Based Narrative Review
Levitt, D., Luk, H.-Y., & Vingren, J. (2022) · Biomolecules · doi:10.3390/biom13010002 · Cited by 24 · see citing works
Effects of Fucoxanthin on the Inhibition of Dexamethasone-Induced Skeletal Muscle Loss in Mice
Yoshikawa, M., Hosokawa, M., Miyashita, K., Nishino, H., & Hashimoto, T. (2021) · Nutrients · doi:10.3390/nu13041079 · Cited by 25 · see citing works
“Mitochondrial dysfunction increases AMP and ROS and activates AMPK, which suppresses protein synthesis via inhibition of mTOR signaling [35] and hence results in muscle atrophy [36].”
BackgroundMechanisms of the NAD+ salvage pathway in enhancing skeletal muscle function
Su, M., Qiu, F., Li, Y., Che, T., Li, N., & Zhang, S. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1464815 · Cited by 24 · see citing works
“Studies have shown that the absence of AMPK α 1 leads to a reduction in satellite cell numbers and decreased expression of myogenic factors such as Myf5 and Myogenin (Fu et al., 2015; Thomson, 2018).”
BackgroundDuan, Z., Tu, C., Liu, Q. H., Li, S., Li, Y., Xie, P., & Li, Z. (2020) · Journal of Cellular Biochemistry · doi:10.1002/jcb.29605 · Cited by 23 · see citing works
“Accumulating evidence suggests that the AMPK‐mTOR pathway might act as the primary signal axis for autophagy.(37,38) Our results show that AdipoRon promoted the phosphorylation of the AMPK protein and then inhibited the phosphorylation of mTOR protein in chondrocytes.”
BackgroundLi, Y., Feng, Y., Chen, X., He, J., Luo, Y., Yu, B., Chen, D., & Huang, Z. (2024) · Meat Science · doi:10.1016/j.meatsci.2024.109436 · Cited by 23 · see citing works
Tsukita, K., Yano, T., Tamura, A., & Tsukita, S. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20236012 · Cited by 23 · see citing works
The Roles of AMPK in Revascularization
Chen, M.-H., & Fu, Q.-M. (2020) · Cardiology Research and Practice · doi:10.1155/2020/4028635 · Cited by 23 · see citing works
“Zhenkun Lou et al. have found that AMPKα1 or AMPKα2 ubiquitination blocks its phosphorylation by LKB1, which could be rescued by the deubiquitinase ubiquitin specific peptidase 10 (USP10) [54].”
BackgroundInfluentialMiRNA Profiling in Pectoral Muscle Throughout Pre- to Post-Natal Stages of Chicken Development
Chen, M., Zhang, S., Xu, Z., Gao, J., Mishra, S. K., Zhu, Q., Zhao, X., Wang, Y., Yin, H., Fan, X., et al. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2020.00570 · Cited by 22 · see citing works
“These pathways had been reported to be involved in muscle growth and development (Schiaffino et al., 2013; Thomson, 2018; Du et al., 2019).”
BackgroundHigh-Frequency Stimulation on Skeletal Muscle Maintenance in Female Cachectic Mice
Sato, S., Gao, S., Puppa, M. J., Kostek, M., Wilson, L., & Carson, J. (2019) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0000000000001991 · Cited by 15 · see citing works
Elevated CO2 Levels Delay Skeletal Muscle Repair by Increasing Fatty Acid Oxidation
Ceco, E., Celli, D. A., Weinberg, S. E., Shigemura, M., Welch, L. C., Volpe, L., Chandel, N. S., Bharat, A., Lecuona, E., & Sznajder, J. I. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2020.630910 · Cited by 21 · see citing works
“With regards to muscle regeneration, AMPKα1 plays a prominent role in regulating satellite cell dynamics, with AMPKα2 playing a potentially more important role in regulating muscle degradation during atrophy (Thomson, 2018).”
BackgroundWheel running improves fasting‐induced AMPK signaling in skeletal muscle from tumor‐bearing mice
Fix, D. K., Counts, B. R., Smuder, A. J., Sarzynski, M. A., Koh, H., & Carson, J. A. (2021) · Physiological Reports · doi:10.14814/phy2.14924 · Cited by 19 · see citing works
“Nevertheless, many different catabolic conditions have investigated skeletal muscle atrophy regulation by metabolic disruptions that induce AMPK signaling (Bujak et al., 2015; Di Magno et al., 2016; Nakashima & Yakabe, 2007; Sanchez, Candau, et al., 2012; Sanchez, Csibi, et al., 2012; Thomson, 2018).”
BackgroundMinari, A. L. A., & Thomatieli-Santos, R. (2021) · American Journal of Physiology. Regulatory Integrative and Comparative Physiology · doi:10.1152/ajpregu.00038.2021 · Cited by 16 · see citing works
Malila, Y., Thanatsang, K. V., Sanpinit, P., Arayamethakorn, S., Soglia, F., Zappaterra, M., Bordini, M., Sirri, F., Rungrassamee, W., Davoli, R., et al. (2022) · PLoS ONE · doi:10.1371/journal.pone.0275160 · Cited by 20 · see citing works
“In addition, AMPK plays a key role in regulating skeletal muscle growth, development, and repair [21].”
BackgroundRavel‐Chapuis, A., Duchesne, É., & Jasmin, B. J. (2022) · The Journal of Physiology · doi:10.1113/jp282725 · Cited by 19 · see citing works
“This last element further obscures the investigation of AMPK in the context of exercise because the molecular responses to different exercise modalities are less clear in humans than in animals (Thomson, 2018).”
BackgroundGamberi, T., Magherini, F., & Fiaschi, T. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20071544 · Cited by 18 · see citing works
“Full AMPK activation occurs through both phosphorylation by liver kinase B1 (LKB1) and AMP binding [8].”
BackgroundTransient changes to metabolic homeostasis initiate mitochondrial adaptation to endurance exercise
Dent, J. R., Stocks, B., Campelj, D. G., & Philp, A. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.03.022 · Cited by 18 · see citing works
Aoki, Y., Ozawa, T., Numata, O., & Takemasa, T. (2019) · Nutrients · doi:10.3390/nu11092131 · Cited by 18 · see citing works
“Additionally, dominant-negative Ampk transgenic mice in which a dominant-negative Ampkα2 subunit was overexpressed under the muscle creatine kinase promoter (expressed in heart and skeletal muscle) showed that EDL muscles tended to be larger than in wild-type mice, suggesting that Ampk might negatively regulate basal…”
BackgroundDou, Y., Wei, Y., Zhang, Z., Li, C., Song, C., Liu, Y., Qi, K., Li, X., Li, X., Qiao, R., et al. (2023) · BMC Genomics · doi:10.1186/s12864-023-09346-w · Cited by 17 · see citing works
“Among them, the AMPK signaling pathway is an important signaling pathway of energy metabolism that is heavily involved in skeletal muscle metabolic processes; controls skeletal muscle growth and development by regulating many downstream targets; is related to myocyte energy metabolism, protein synthesis, and catabolis…”
BackgroundAMPK/mTOR balance during exercise: implications for insulin resistance in aging muscle
Mingzheng, X., & You, W. (2025) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-025-05362-4 · Cited by 17 · see citing works
“As a result of the energetic challenge, intracellular AMP/ATP and ADP/ATP ratios increase, serving as crucial triggers for AMPK activation [39].”
Effect of Age and Lipoperoxidation in Rat and Human Adipose Tissue-Derived Stem Cells
Muñoz, M., Argüelles, S., Marotta, F., Barbagallo, M., Cano, M., & Ayala, A. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/6473279 · Cited by 16 · see citing works
“Recent studies have shown that AMPK activation, in response to various stimuli, such as exercise and muscle contraction, gradually declines during aging [77].”
LKB1 signaling is altered in skeletal muscle of a Duchenne muscular dystrophy mouse model
Boccanegra, B., Mantuano, P., Conte, E., Cerchiara, A. G., Tulimiero, L., Quarta, R., Caputo, E., Sanarica, F., Forino, M., Spadotto, V., et al. (2023) · Disease Models & Mechanisms · doi:10.1242/dmm.049930 · Cited by 16 · see citing works
“Nonetheless, chronic activation in basal conditions may have deleterious effects on muscle homeostasis, inhibiting muscle growth and stimulating pro-atrophic pathways (Thomson, 2018).”
Beta-hydroxybutyric acid attenuates neuronal damage in epileptic mice
Guo, Q.-H., Liu, S., Wang, S., Wu, M., Li, Z., & Wang, Y. (2019) · Acta Histochemica · doi:10.1016/j.acthis.2019.03.009 · Cited by 16 · see citing works
Gombos, Z., Koltai, E., Torma, F., Bakonyi, P., Kolonics, A., Aczél, D., Ditrói, T., Nagy, P., Kawamura, T., & Radak, Z. O. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147588 · Cited by 17 · see citing works
“Hence, as a result of intensive investigation a lot is known about the molecular pathways that are involved in increased protein synthesis and attenuated catabolic processes, which happen to occur during the hypertrophy of skeletal muscle [6,7].”
BackgroundLiu, J., Zhao, H., Yang, L., Wang, X., Yang, L., Xing, Y., Lv, X., Ma, H., & Song, G. (2022) · BMC Endocrine Disorders · doi:10.1186/s12902-021-00921-4 · Cited by 16 · see citing works
“The fatty acid synthesis can be increased by reducing the inhibitory effect of malonyl-CoA on CPT-1α oxidative metabolism [31].”
BackgroundTranscriptome Analysis of Differentially Expressed mRNA Related to Pigeon Muscle Development
Ding, H., Lin, Y., Zhang, T., Chen, L., Zhang, G., Wang, J., Xie, K., & Dai, G. (2021) · Animals · doi:10.3390/ani11082311 · Cited by 15 · see citing works
“AMPK plays an important role in controlling skeletal muscle development and growth due to its effects on anabolism and catalytic cellular processes [27].”
BackgroundLi, K., Wang, M., Wang, R., Wang, X., Jiao, H., Zhao, J., Zhou, Y., Li, H., & Lin, H. (2023) · Journal of Nutrition · doi:10.1016/j.tjnut.2023.08.024 · Cited by 15 · see citing works
Epigenetics of Skeletal Muscle Atrophy
Du, J., Wu, Q., & Bae, E. J. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25158362 · Cited by 15 · see citing works
“The AMPK pathway is essential in skeletal muscle atrophy, as it can inhibit protein synthesis by modulating the phosphorylation of mTOR and eukaryotic initiation factor 2 [43].”
BackgroundGrönholdtKlein, M., Altun, M., Becklén, M., Kahm, E. D., Fahlström, A., Rullman, E., & Ulfhake, B. (2019) · Acta Physiologica · doi:10.1111/apha.13335 · Cited by 15 · see citing works
Transcriptional Changes Involved in Atrophying Muscles during Prolonged Fasting in Rats
Ibrahim, M., Wasselin, T., Challet, É., DORSSELAER, A. V., Maho, Y. L., Raclot, T., & Bertile, F. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21175984 · Cited by 15 · see citing works
“AMPK generally activates catabolic factors while inactivating anabolic ones, thereby controlling energy metabolism and muscle growth or atrophy [83].”
BackgroundChernyavskij, D. A., Pletjushkina, O. Y., Kashtanova, A. V., Galkin, I. I., Karpukhina, A. A., Chernyak, B. V., Vassetzky, Y. S., & Popova, E. N. (2023) · Antioxidants · doi:10.3390/antiox12030602 · Cited by 15 · see citing works
Mechanisms of endurance and resistance exercise in type 2 diabetes mellitus: A Narrative review
Zhao, X., Huang, F., Sun, Y., & Li, L. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.151731 · Cited by 14 · see citing works
Regulatory Role of N6-Methyladenosine in Longissimus Dorsi Development in Yak
Ma, X., La, Y., Bao, P., Chu, M., Guo, X., Wu, X., Pei, J., Ding, X., Liang, C., & Yan, P. (2022) · Frontiers in Veterinary Science · doi:10.3389/fvets.2022.757115 · Cited by 14 · see citing works
“In addition, AMPK not only plays a key regulatory role in muscle energy metabolism but also participates in the transformation of muscle fiber types (44).”
BackgroundJaitovich, A. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00292.2022 · Cited by 14 · see citing works
Pudjihartono, N., Ho, D., Golovina, E., Fadason, T., Kempa-Liehr, A. W., & O'Sullivan, J. M. (2023) · Journal of Autoimmunity · doi:10.1016/j.jaut.2023.103046 · Cited by 14 · see citing works
Chan, C.-M., Sekar, P., Huang, D.-Y., Hsu, S.-H., & Lin, W. (2020) · Antioxidants · doi:10.3390/antiox9111057 · Cited by 15 · see citing works
Ho, J., Baskaran, R., Wang, M.-F., Mohammedsaleh, Z. M., Yang, H., Balasubramanian, B., & Lin, W. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23158167 · Cited by 13 · see citing works
“In addition, swimming exercise protects mice against myocardial and liver apoptosis [18,19].”
BackgroundSu, L.-Y., Huang, W.-C., Kan, N., Tung, T.-H., Huynh, L. B. P., & Huang, S. (2023) · Nutrients · doi:10.3390/nu15010249 · Cited by 13 · see citing works
“Studies have also supported that resveratrol is involved in the activation of AMP-activated protein kinase (AMPK) during muscle contraction over a longer exercise period [11].”
BackgroundThe Role of Natural Products in the Improvement of Cancer-Associated Cachexia
Han, Y., Kim, H. I., & Park, J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24108772 · Cited by 13 · see citing works
“In cancer-induced cachexia, it has been reported that AMPK could play a key role in regulating energy production and consumption, and it has been suggested to contribute to the development of muscle wasting and weight loss seen in cachexia [21,83,84].”
BackgroundWei, X., Wang, J., Sun, Y., Zhao, T., Luo, X., Lu, J., Hou, W., Yu, X., Xue, L., Yan, Y. L., et al. (2023) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30453 · Cited by 13 · see citing works
Yu, H., He, Y., Qin, M., Wang, L., Rong, K., & Zhang, X. (2024) · Aquaculture · doi:10.1016/j.aquaculture.2024.740591 · Cited by 13 · see citing works
Fine-tuning AMPK in physiology and disease using point-mutant mouse models
Ashraf, N., & Nostrand, J. L. V. (2024) · Disease Models & Mechanisms · doi:10.1242/dmm.050798 · Cited by 12 · see citing works
“…muscle, AMPK facilitates glucose uptake, stimulates fatty acid β -oxidation (FAO, see Glossary, Box 2) and promotes mitochondrial biogenesis, thereby enhancing insulin sensitivity and maintaining a healthy body weight (Jørgensen et al., 2021; Lee et al., 2006; Rhein et al., 2021; Thomson, 2018).”
BackgroundZhang, Y., Li, T., Liu, Y., Wang, C., Wang, D., Xu, L., Zhao, H., Bai, X., Li, Z., & Wang, Y.-C. (2024) · Shock · doi:10.1097/shk.0000000000002430 · Cited by 13 · see citing works
“Muscle ring finger protein 1 (MuRF1) and F-box protein Atrogin-1 are two indicators that are commonly employed to assess skeletal muscle atrophy due to their high expression and sensitivity (3,7).”
InfluentialEffects of Maca on Muscle Hypertrophy in C2C12 Skeletal Muscle Cells
Yi, D., Yoshikawa, M., Sugimoto, T., Tomoo, K., Okada, Y., & Hashimoto, T. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23126825 · Cited by 13 · see citing works
“AMPK greatly affects skeletal muscle development and growth [32].”
BackgroundYakabe, M., Hosoi, T., Sasakawa, H., Akishita, M., & Ogawa, S. (2022) · BMC Complementary Medicine and Therapies · doi:10.1186/s12906-022-03812-w · Cited by 12 · see citing works
“In addition, 5’ adenosine monophosphate-activated protein kinase (AMPK) has two kinds of effects on metabolism: the inhibition of anabolism to minimize ATP consumption and the stimulation of catabolism to stimulate ATP production [6], and it is involved in skeletal muscle metabolic control [7].”
BackgroundAnalysis of the mechanism of skeletal muscle atrophy from the pathway of decreased protein synthesis
Chen, P., Jia, F., Wang, M., & Yang, S. (2025) · Frontiers in Physiology · doi:10.3389/fphys.2025.1533394 · Cited by 13 · see citing works
“This inhibits the binding of elongation factors to ribosomes, resulting in decreased translation efficiency and reduced protein synthesis (Thomson, 2018) (Figure 1).”
Valini, G. A. D. C., Duarte, M. D. S., Rodrigues, G. D. A., Veroneze, R., Saraiva, A., Hausman, G. J., & Rocha, G. C. (2020) · Ciência Rural · doi:10.1590/0103-8478cr20190948 · Cited by 12 · see citing works
Direct or indirect regulation of muscle protein synthesis by energy status?
Moinard, C., & Fontaine, E. M. (2020) · Clinical Nutrition · doi:10.1016/j.clnu.2020.07.015 · Cited by 12 · see citing works
- Authors
- Thomson, D. M.
- Affiliations
- Brigham Young University (US)
- Corresponding author
- Thomson, David M.
- ORCID
- Thomson, David M.
- Venue
- International Journal of Molecular Sciences
- Publisher
- MDPI AG
- Published
- 2018-10-11
- Volume
- 19
- Issue
- 10
- Pages
- 3125
- ISSN
- 1422-0067 (ISSN-L)
- PMC
- PMC6212977
- OpenAlex
- W2896374260
- Cited by
- 267
- References
- 142
- Citations by year
- 2026: 29 · 2025: 36 · 2024: 41 · 2023: 52 · 2022: 40 · 2021: 31 · 2020: 24 · 2019: 13 · 2018: 1
- FWCI
- 1.68
- Type
- journal article
- Language
- en
- Open access
- gold
- dx.doi.org
- Licence
- Locations
- International Journal of Molecular Sciences (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, other-oa)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
- Keywords
- AMPK, skeletal muscle growth, muscle hypertrophy, muscle atrophy, muscle regeneration, satellite cells, LKB1, AMPKα1, AMPKα2, muscle metabolism, myogenesis
- MeSH terms
- Animals, Energy Metabolism, Enzyme Activation, Humans, Hypertrophy, Organ Size, Regeneration, Wound Healing, Signal Transduction, Biomarkers, Muscle, Skeletal, Muscle Fibers, Skeletal, Muscle Development, AMP-Activated Protein Kinases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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