Thr649Ala-AS160 knock-in mutation does not impair contraction/AICAR-induced glucose transport in mouse muscle
Open accessAbstract
AS160 and its closely related protein TBC1D1 have emerged as key mediators for both insulin- and contraction-stimulated muscle glucose uptake through regulating GLUT4 trafficking. Insulin increases AS160 phosphorylation at multiple Akt/PKB consensus sites, including Thr 649, and promotes its binding to 14-3-3 proteins through phospho-Thr 649. We recently provided genetic evidence that AS160-Thr 649 phosphorylation/14-3-3 binding plays a key role in mediating insulin-stimulated glucose uptake in muscle. Contraction has also been proposed to increase phosphorylation of AS160 and TBC1D1 via AMPK, which could be detected by a generic phospho-Akt substrate (PAS) antibody. Here, analysis of AS160 immunoprecipitates from muscle extracts with site-specific phospho-antibodies revealed that contraction and AICAR caused no increase but rather a slight decrease in phosphorylation of the major PAS recognition site AS160-Thr 649. In line with this, contraction failed to enhance 14-3-3 binding to AS160. Consistent with previous reports, we also observed that in situ contraction stimulated the signal intensity of PAS antibody immunoreactive protein of ∼150–160 kDa in muscle extracts. Using a TBC1D1 deletion mutant mouse, we showed that TBC1D1 protein accounted for the majority of the PAS antibody immunoreactive signals of ∼150–160 kDa in extracts of contracted muscles. Consistent with the proposed role of AS160-Thr 649 phosphorylation/14-3-3 binding in mediating glucose uptake, AS160-Thr 649 Ala knock-in mice displayed normal glucose uptake upon contraction and AICAR in isolated muscles. We conclude that the previously reported PAS antibody immunoreactive band ∼150–160 kDa, which were increased upon contraction, does not represent AS160 but TBC1D1, and that AS160-Thr 649 Ala substitution impairs insulin- but neither contraction- nor AICAR-stimulated glucose uptake in mouse skeletal muscle.
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TBC1D4 T649A KI mice do not have impaired AICAR and contraction mediated glucose uptake.
“Consistent with this, TBC1D4 T649A KI mice do not have impaired AICAR and contraction mediated glucose uptake, suggesting that the other three sites (S325, S595, and S758) may also be important for regulating TBC1D4 activity and glucose uptake during exercise [78].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [78]
S595 phosphorylation was increased upon in situ contraction in muscle extracts from both wild-type and TBC1D4 T649A KI mice.
“Worth mentioning is that the S595 site has also been shown to be a potential AMPK site [80], and indeed, its phosphorylation was increased upon in situ contraction in muscle extracts from both wild-type and TBC1D4 T649A KI mice [78].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [78]
14-3-3 binding is not considered important for regulating glucose uptake during exercise for TBC1D4.
“This is in contrast to TBC1D4 whereby 14-3-3 binding is not considered important for regulating glucose uptake during exercise [78].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [78]
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- Authors
- Ducommun, S., Wang, H. Y., Sakamoto, K., MacKintosh, C., & Chen, S.
- Affiliations
- University of Dundee (GB)
- Model Animal Research Center (CN)
- Corresponding author
- Chen, Shuai
- Venue
- American Journal of Physiology-Endocrinology and Metabolism
- Publisher
- American Physiological Society
- Published
- 2012-05-01
- Volume
- 302
- Issue
- 9
- Pages
- E1036-E1043
- ISSN
- 0193-1849 (ISSN-L)
- 1522-1555
- PMC
- PMC3361978
- OpenAlex
- W2119581987
- Cited by
- 35
- References
- 35
- Citations by year
- 2025: 2 · 2024: 1 · 2023: 1 · 2021: 3 · 2020: 2 · 2019: 1 · 2017: 1 · 2016: 5 · 2015: 5 · 2014: 4 · 2013: 7 · 2012: 3
- FWCI
- 2.44
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- American Journal of Physiology-Endocrinology and Metabolism (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Discovery Research Portal (University of Dundee) (submittedVersion)
- Funders
- University of Dundee
- Diabetes UK
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Keywords
- AS160, TBC1D1, 14-3-3 binding, muscle glucose uptake, AICAR, AMPK, GLUT4 trafficking, insulin signaling, skeletal muscle, knock-in mice
- MeSH terms
- Aminoimidazole Carboxamide, Analysis of Variance, Animals, Blood Glucose, Insulin, Mice, Transgenic, Muscle Contraction, Mutation, Nuclear Proteins, Phosphorylation, Ribonucleotides, Signal Transduction, Muscle, Skeletal, Amino Acid Substitution, GTPase-Activating Proteins, 14-3-3 Proteins, Glucose Transporter Type 4, Mice, AMP-Activated Protein Kinases, Gene Knock-In Techniques
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