The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
Insulin-Stimulated Phosphorylation of the Akt Substrate AS160 Is Impaired in Skeletal Muscle of Type 2 Diabetic Subjects
Abstract
AS160 is a newly described substrate for the protein kinase Akt that links insulin signaling and GLUT4 trafficking. In this study, we determined the expression of and in vivo insulin action on AS160 in human skeletal muscle. In addition, we compared the effect of physiological hyperinsulinemia on AS160 phosphorylation in 10 lean−to−moderately obese type 2 diabetic and 9 healthy subjects. Insulin infusion increased the phosphorylation of several proteins reacting with a phospho-Akt substrate antibody. We focused on AS160, as this Akt substrate has been linked to glucose transport. A 160-kDa phosphorylated protein was identified as AS160 by immunoblot analysis with an AS160-specific antibody. Physiological hyperinsulinemia increased AS160 phosphorylation 2.9-fold in skeletal muscle of control subjects (P < 0.001). Insulin-stimulated AS160 phosphorylation was reduced 39% (P < 0.05) in type 2 diabetic patients. AS160 protein expression was similar in type 2 diabetic and control subjects. Impaired AS160 phosphorylation was related to aberrant Akt signaling; insulin action on Akt Ser473 phosphorylation was not significantly reduced in type 2 diabetic compared with control subjects, whereas Thr308 phosphorylation was impaired 51% (P < 0.05). In conclusion, physiological hyperinsulinemia increases AS160 phosphorylation in human skeletal muscle. Moreover, defects in insulin action on AS160 may impair GLUT4 trafficking in type 2 diabetes.
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Insulin-stimulated Phosphorylation of a Rab GTPase-activating Protein Regulates GLUT4 Translocation
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Structure, regulation and function of PKB/AKT—a major therapeutic target
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A Method to Identify Serine Kinase Substrates
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Self-citationIdentification of a PKB/Akt Hydrophobic Motif Ser-473 Kinase as DNA-dependent Protein Kinase
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Self-citationUnravelling the activation mechanisms of protein kinase B/Akt
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Sleep duration and risk of type 2 diabetes: a meta-analysis of prospective studies
Shan, Z., Ma, H., Xie, M., Yan, P., Guo, Y., Bao, W., Rong, Y., Jackson, C. L., Hu, F. B., & Liu, L. (2015) · Diabetes Care · doi:10.2337/dc14-2073 · Cited by 902
Metabolic Syndrome and Insulin Resistance: Underlying Causes and Modification by Exercise Training
Roberts, C. K., Hevener, A. L., & Barnard, R. J. (2013) · Comprehensive Physiology · doi:10.1002/cphy.c110062 · Cited by 831
Plomgaard, P., Bouzakri, K., Krogh-Madsen, R., Mittendorfer, B., Zierath, J. R., & Pedersen, B. K. (2005) · Diabetes · doi:10.2337/diabetes.54.10.2939 · Cited by 627
Self-citationFunctional Properties and Genomics of Glucose Transporters
Zhao, F.-Q., & Keating, A. (2007) · Current Genomics · doi:10.2174/138920207780368187 · Cited by 549
Metadata
- Authors
- Karlsson, H. K. R., Zierath, J. R., Kane, S., Krook, A., Lienhard, G. E., & Wallberg-Henriksson, H.
- Venue
- Diabetes
- Publisher
- American Diabetes Association
- Published
- 2005-06-01
- Volume
- 54
- Issue
- 6
- Pages
- 1692-1697
- ISSN
- 0012-1797 (ISSN-L)
- 1939-327X
- OpenAlex
- W2170864435
- Cited by
- 300
- References
- 31
- FWCI
- 7.72
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Insulin-Stimulated Phosphorylation of the Akt Substrate AS160 Is Impaired in Skeletal Muscle of Type 2 Diabetic Subjects. https://app.cochat.ai/papers/10.2337/diabetes.54.6.1692
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- Karlsson, H. K. R., Zierath, J. R., Kane, S., Krook, A., Lienhard, G. E., & Wallberg-Henriksson, H. (2005). Insulin-Stimulated Phosphorylation of the Akt Substrate AS160 Is Impaired in Skeletal Muscle of Type 2 Diabetic Subjects. Diabetes. https://doi.org/10.2337/diabetes.54.6.1692
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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