The role of skeletal muscle Akt in the regulation of muscle mass and glucose homeostasis
Open accessAbstract
OBJECTIVE: Skeletal muscle insulin signaling is a major determinant of muscle growth and glucose homeostasis. Protein kinase B/Akt plays a prominent role in mediating many of the metabolic effects of insulin. Mice and humans harboring systemic loss-of-function mutations in Akt2, the most abundant Akt isoform in metabolic tissues, are glucose intolerant and insulin resistant. Since the skeletal muscle accounts for a significant amount of postprandial glucose disposal, a popular hypothesis in the diabetes field suggests that a reduction in Akt, specifically in skeletal muscle, leads to systemic glucose intolerance and insulin resistance. Despite this common belief, the specific role of skeletal muscle Akt in muscle growth and insulin sensitivity remains undefined. METHODS: We generated multiple mouse models of skeletal muscle Akt deficiency to evaluate the role of muscle Akt signaling in vivo. The effects of these genetic perturbations on muscle mass, glucose homeostasis and insulin sensitivity were assessed using both in vivo and ex vivo assays. RESULTS: Surprisingly, mice lacking Akt2 alone in skeletal muscle displayed normal skeletal muscle insulin signaling, glucose tolerance, and insulin sensitivity despite a dramatic reduction in phosphorylated Akt. In contrast, deletion of both Akt isoforms (M-AktDKO) prevented downstream signaling and resulted in muscle atrophy. Despite the absence of Akt signaling, in vivo and ex vivo insulin-stimulated glucose uptake were normal in M-AktDKO mice. Similar effects on insulin sensitivity were observed in mice with prolonged deletion (4 weeks) of both skeletal muscle Akt isoforms selectively in adulthood. Conversely, short term deletion (2 weeks) of skeletal muscle specific Akt in adult muscles impaired insulin tolerance paralleling the effect observed by acute pharmacological inhibition of Akt in vitro. Mechanistically, chronic ablation of Akt induced mitochondrial dysfunction and activation of AMPK, which was required for insulin-stimulated glucose uptake in the absence of Akt. CONCLUSIONS: Together, these data indicate that chronic reduction in Akt activity alone in skeletal muscle is not sufficient to induce insulin resistance or prevent glucose uptake in all conditions. Therefore, since insulin-stimulated glucose disposal in skeletal muscle is markedly impaired in insulin-resistant states, we hypothesize that alterations in signaling molecules in addition to skeletal muscle Akt are necessary to perturb glucose tolerance and insulin sensitivity in vivo.
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Deletion of both Akt1 and Akt2 in skeletal muscle reduces both muscle size and muscle protein synthesis, indicating that only minimal amounts of Akt in muscle are needed to transmit downstream signaling and preserve muscle mass in vivo.
“recent studies utilizing skeletal muscle-specific knockouts of both Akt1 and Akt2 demonstrated that deletion of both isoforms reduces both muscle size and muscle protein synthesis, indicating that only minimal amounts of Akt in muscle are needed to transmit downstream signaling and preserve muscle mass in vivo [19,20].”
From Antibody blockade of activin type II receptors preserves skeletal muscle mass and enhances fat loss during GLP-1 receptor agonism (2024) · cites this paper as [19]
Skeletal muscle Akt signaling is both required and sufficient for muscle hypertrophy, as genetic loss of Akt isoforms in the muscle leads to decreased muscle size in adult mice.
“Skeletal muscle Akt signaling is both required and sufficient for muscle hypertrophy, as genetic loss of Akt isoforms in the muscle leads to decreased muscle size in adult mice [19,20,22].”
From Antibody blockade of activin type II receptors preserves skeletal muscle mass and enhances fat loss during GLP-1 receptor agonism (2024) · cites this paper as [19]
M-AktDKO mice display significant deficits in muscle growth and protein synthesis, consistent with a major anabolic role for Akt in muscle.
“As described in prior studies, these mice display significant deficits in muscle growth and protein synthesis, consistent with a major anabolic role for Akt in muscle [19,20].”
From Antibody blockade of activin type II receptors preserves skeletal muscle mass and enhances fat loss during GLP-1 receptor agonism (2024) · cites this paper as [19]
Residual Akt1 expression in whole muscle tissue is due to the expression of Akt1 in non-muscle cells.
“Residual Akt1 expression in whole muscle tissue is due to the expression of Akt1 in non-muscle cells [19].”
From Antibody blockade of activin type II receptors preserves skeletal muscle mass and enhances fat loss during GLP-1 receptor agonism (2024) · cites this paper as [19]
AKT1 rs1130214 polymorphism affects the AKT pathway, influencing MPS rates.
“Furthermore, the AKT1 rs1130214 polymorphism affects the AKT pathway, a critical component of the mTOR signaling cascade, influencing MPS rates [59].”
From Beyond Calories: Individual Metabolic and Hormonal Adaptations Driving Variability in Weight Management—A State-of-the-Art Narrative Review (2024) · cites this paper as [59]
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Insulin: The master regulator of glucose metabolism
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Insulin signalling and GLUT4 trafficking in insulin resistance
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Mechanisms of Estrogen Influence on Skeletal Muscle: Mass, Regeneration, and Mitochondrial Function
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Targeting PI3K-AKT/mTOR signaling in the prevention of autism
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Self-citationExcess Accumulation of Lipid Impairs Insulin Sensitivity in Skeletal Muscle
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Ultra-processed diet, systemic oxidative stress, and breach of immunologic tolerance
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AKT ISOFORMS-AS160-GLUT4: The defining axis of insulin resistance
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Is Arsenic Exposure a Risk Factor for Metabolic Syndrome? A Review of the Potential Mechanisms
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The Therapeutic Effects of Magnesium in Insulin Secretion and Insulin Resistance
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Rho Family GTPases and Rho GEFs in Glucose Homeostasis
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Insulin-Stimulated Muscle Glucose Uptake and Insulin Signaling in Lean and Obese Humans
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The PPARβ/δ-AMPK Connection in the Treatment of Insulin Resistance
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Corylifol A from Psoralea corylifolia L. Enhances Myogenesis and Alleviates Muscle Atrophy
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Vav2 catalysis-dependent pathways contribute to skeletal muscle growth and metabolic homeostasis
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The insulin signalling network
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Insulin action and resistance are dependent on a GSK3β-FBXW7-ERRα transcriptional axis
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Deconstructing the Role of PKC Epsilon in Glucose Homeostasis
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Gene-Environmental Interactions as Metabolic Drivers of Nonalcoholic Steatohepatitis
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AKT2 regulates development and metabolic homeostasis via AMPK-depedent pathway in skeletal muscle
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Exercise—A Panacea of Metabolic Dysregulation in Cancer: Physiological and Molecular Insights
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Chronic Elevation of Skeletal Muscle [Ca2+]i Impairs Glucose Uptake. An in Vivo and in Vitro Study
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AMPK/mTOR balance during exercise: implications for insulin resistance in aging muscle
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CORP: Using transgenic mice to study skeletal muscle physiology
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Diabetes mellitus: Complications, emerging therapeutic targets, and evolving treatment approaches
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UBXN9 governs GLUT4-mediated spatial confinement of RIG-I-like receptors and signaling
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Illumination of the Endogenous Insulin-Regulated TBC1D4 Interactome in Human Skeletal Muscle
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Effects of Whey Peptide Supplementation on Sarcopenic Obesity in High-Fat Diet-Fed Mice
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Hepatic sialic acid synthesis modulates glucose homeostasis in both liver and skeletal muscle
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Role of ARHGEF3 as a GEF and mTORC2 Regulator
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Omega-3 polyunsaturated fatty acids promote SNAREs mediated GLUT4 vesicle docking and fusion
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IGF-1 knockdown inhibits phosphorylation of Akt and ERK in chicken embryonic myotubes
Saneyasu, T., Nakamura, T., Honda, K., & Kamisoyama, H. (2022) · Growth Hormone & IGF Research · doi:10.1016/j.ghir.2022.101478 · Cited by 7 · see citing works
Identification of XAF1 as an endogenous AKT inhibitor
Chen, M., Wang, K., Han, Y., Yan, S., Yuan, H., Liu, Q., Li, L., Li, N., Zhu, H., Lu, D., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112690 · Cited by 7 · see citing works
- Authors
- Jaiswal, N., Gavin, M. G., Quinn, W. J., Luongo, T. S., Gelfer, R. G., Baur, J. A., & Titchenell, P. M.
- Affiliations
- University of Pennsylvania (US)
- Corresponding author
- Titchenell, P.M.
- Venue
- Molecular Metabolism
- Publisher
- Elsevier BV
- Published
- 2019-10
- Volume
- 28
- Pages
- 1-13
- ISSN
- 2212-8778 (ISSN-L)
- PMC
- PMC6822261
- OpenAlex
- W2964701486
- Cited by
- 167
- References
- 81
- Citations by year
- 2026: 10 · 2025: 28 · 2024: 27 · 2023: 20 · 2022: 40 · 2021: 23 · 2020: 18 · 2019: 1
- FWCI
- 6.78
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Molecular Metabolism (publishedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- University of Pennsylvania
- National Institutes of Health (P30 19525, K01 111715)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
- Keywords
- AKT2, Akt isoforms, muscle mass, muscle atrophy, glucose homeostasis, insulin resistance, insulin sensitivity, insulin-stimulated glucose uptake, mitochondrial dysfunction, AMPK, skeletal muscle insulin signaling
- MeSH terms
- Animals, Glucose, Homeostasis, Humans, Male, Weight Gain, Muscle, Skeletal, Proto-Oncogene Proteins c-akt, Mice
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