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Increased AS160 phosphorylation, but not TBC1D1 phosphorylation, with increased postexercise insulin sensitivity in rat skeletal muscle
Open accessAbstract
A single exercise bout can increase insulin-independent glucose transport immediately postexercise and insulin-dependent glucose transport (GT) for several hours postexercise. Akt substrate of 160 kDa (AS160) and TBC1D1 are paralog Rab GTPase-activating proteins that have been proposed to contribute to these exercise effects. Previous research demonstrated greater AS160 and Akt threonine phosphorylation in rat skeletal muscle at 3–4 h postexercise concomitant with enhanced insulin-stimulated GT. To further probe whether these signaling events or TBC1D1 phosphorylation were important for the enhanced postexercise insulin-stimulated GT, male Wistar rats were studied using four experimental protocols (2-h swim exercise, differing with regard to timing of muscle sampling and whether food was provided postexercise) that were known to vary in their influence of insulin-independent and insulin-dependent GT postexercise. The results indicated that, in isolated rat epitrochlearis muscle, 1) elevated phosphorylation of AS160 (measured using anti-phospho-Akt substrate, PAS-AS160, and phosphospecific anti-Thr 642-AS160, pThr 642-AS160) consistently tracked with elevated insulin-stimulated GT; 2) PAS-TBC1D1 was not different from sedentary values at 3 or 27 h postexercise, when insulin sensitivity was increased; 3) insulin-stimulated Akt activity was not increased postexercise in muscles with increased insulin sensitivity; 4) PAS-TBC1D1 was increased immediately postexercise, when insulin-independent GT was elevated, and reversed at 3 and 27 h postexercise, when insulin-independent GT was also reversed; and 5) there was no significant effect of exercise or insulin on total abundance of AS160, TBC1D1, Akt, or GLUT4 protein with any of the protocols. The results are consistent with increased AS160 phosphorylation (PAS-AS160 or pThr 642-AS160) but not increased PAS-TBC1D1 or Akt activity, which is important for increased postexercise insulin-stimulated GT in rat skeletal muscle. They also support the idea that increased TBC1D1 phosphorylation may play a role in the insulin-independent increase in GT postexercise.
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“Funai et al. [142] found that refeeding rather than fasting following exercise reduced the enhanced effects of insulin on glucose uptake as well as TBC1D4 T642 and PAS phosphorylation.”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [142]
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Metadata
- Authors
- Funai, K., Schweitzer, G. G., Sharma, N., Kanzaki, M., & Cartee, G. D.
- Affiliations
- University of Michigan (US)
- Venue
- American Journal of Physiology-Endocrinology and Metabolism
- Publisher
- American Physiological Society
- Published
- 2009-07
- Volume
- 297
- Issue
- 1
- Pages
- E242-E251
- ISSN
- 0193-1849 (ISSN-L)
- 1522-1555
- PMC
- PMC2711658
- OpenAlex
- W1985381832
- Cited by
- 119
- References
- 56
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 6 · 2023: 4 · 2022: 2 · 2021: 8 · 2020: 5 · 2019: 10 · 2018: 10 · 2017: 11 · 2016: 9 · 2015: 11 · 2014: 13 · 2013: 4 · 2012: 7
- FWCI
- 2.82
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- American Journal of Physiology-Endocrinology and Metabolism (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01ag011026-21)
- National Institute on Aging (AG-011026)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK071771, R01DK071771)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
- Health Sciences › Medicine › Physiology (medical) › Cardiovascular and exercise physiology
- Keywords
- AS160 phosphorylation, insulin sensitivity, insulin-independent glucose transport, insulin-stimulated glucose transport, Akt signaling, Rab GTPase-activating protein, skeletal muscle, epitrochlearis muscle, GLUT4, physical activity
- MeSH terms
- Animals, Biological Transport, Glucose, Glycogen, Insulin Resistance, Male, Phosphorylation, Physical Conditioning, Animal, Protein Kinases, Proteins, Threonine, Up-Regulation, Rats, Wistar, Muscle, Skeletal, GTPase-Activating Proteins, Oncogene Protein v-akt, Rats
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