The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
The Rab GTPase-Activating Protein AS160 Integrates Akt, Protein Kinase C, and AMP-Activated Protein Kinase Signals Regulating GLUT4 Traffic
Abstract
Insulin-dependent phosphorylation of Akt target AS160 is required for GLUT4 translocation. Insulin and platelet-derived growth factor (PDGF) (Akt activators) or activation of conventional/novel (c/n) protein kinase C (PKC) and 5′ AMP-activated protein kinase (AMPK) all promote a rise in membrane GLUT4 in skeletal muscle and cultured cells. However, the downstream effectors linking these pathways to GLUT4 traffic are unknown. Here we explore the hypothesis that AS160 is a molecular link among diverse signaling cascades converging on GLUT4 translocation. PDGF and insulin increased AS160 phosphorylation in CHO-IR cells. Stimuli that activate c/n PKC or AMPK also elevated AS160 phosphorylation. We therefore examined if these signaling pathways engage AS160 to regulate GLUT4 traffic in muscle cells. Nonphosphorylatable AS160 (4P-AS160) virtually abolished the net surface GLUT4myc gains elicited by insulin, PDGF, K+ depolarization, or 5-aminoimidazole-4-carboxamide-1-β-d-ribofuranoside but partly, yet significantly, inhibited the effects of 4-phorbol-12-myristate-13-acetate. However, the hypertonicity or 2,4-dinitrophenol–dependent gains in surface GLUT4myc were unaffected by 4P-AS160. RK-AS160 (GTPase-activating protein [GAP] inactive) or 4PRK-AS160 (GAP inactive, nonphosphorylatable) had no effect on surface GLUT4myc elicited by all stimuli. Collectively, these results indicate that activation of Akt, c/n PKC, or α2-AMPK intersect at AS160 to regulate GLUT4 traffic, as well as highlight the potential of AS160 as a therapy target to increase muscle glucose uptake.
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Cites
Characterization of AMP-activated protein kinase γ-subunit isoforms and their role in AMP binding
CHEUNG, P. C. F., SALT, I. P., DAVIES, S. P., HARDIE, D. G., & CARLING, D. (2000) · Biochemical Journal · doi:10.1042/bj3460659 · Cited by 637
Jørgensen, S. B., Viollet, B., Andreelli, F., Frøsig, C., Birk, J. B., Schjerling, P., Vaulont, S., Richter, E. A., & Wojtaszewski, J. F. P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m306205200 · Cited by 553
Kramer, H. F., Witczak, C. A., Fujii, N., Jessen, N., Taylor, E. B., Arnolds, D. E., Sakamoto, K., Hirshman, M. F., & Goodyear, L. J. (2006) · Diabetes · doi:10.2337/db06-0150 · Cited by 315
Bruss, M. D., Arias, E. B., Lienhard, G. E., & Cartee, G. D. (2005) · Diabetes · doi:10.2337/diabetes.54.1.41 · Cited by 273 · cited 3×
“Insulin increases AS160 phosphorylation in 3T3-L1 adipocytes (2) and skeletal muscle (8,9).”
BackgroundRyder, J. W., Yang, J., Galuska, D., Rincón, J., Björnholm, M., Krook, A., Lund, S., Pedersen, O., Wallberg-Henriksson, H., Zierath, J. R., et al. (2000) · Diabetes · doi:10.2337/diabetes.49.4.647 · Cited by 216
Fujii, N., Hirshman, M. F., Kane, E. M., Ho, R. C., Peter, L. E., Seifert, M. M., & Goodyear, L. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504208200 · Cited by 177
Role of Akt2 in contraction-stimulated cell signaling and glucose uptake in skeletal muscle
Sakamoto, K., Arnolds, D. E., Fujii, N., Kramer, H. F., Hirshman, M. F., & Goodyear, L. J. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00204.2006 · Cited by 63
Role of AMP-Activated Protein Kinase in the Control of Glucose Homeostasis
Barnes, B., & Zierath, J. (2005) · Current Molecular Medicine · doi:10.2174/1566524053766103 · Cited by 45 · cited 1×
“Moreover, AMPK has emerged as a viable pharmacological target in the treatment of type 2 diabetes (36,37), and chronic treatment of obese rodents with an AMPK activator improved glucose tolerance (38).”
Background
Cited by
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
Role of Skeletal Muscle in Insulin Resistance and Glucose Uptake
Merz, K. E., & Thurmond, D. C. (2020) · Comprehensive Physiology · doi:10.1002/cphy.c190029 · Cited by 494
Emerging role for AS160/TBC1D4 and TBC1D1 in the regulation of GLUT4 traffic
Sakamoto, K., & Holman, G. D. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90331.2008 · Cited by 481
The many actions of insulin in skeletal muscle, the paramount tissue determining glycemia
Sylow, L., Tokarz, V. L., Richter, E. A., & Klip, A. (2021) · Cell Metabolism · doi:10.1016/j.cmet.2021.03.020 · Cited by 366
Self-citationTaylor, E. B., An, D., Kramer, H. F., Yu, H., Fujii, N. L., Roeckl, K. S. C., Bowles, N., Hirshman, M. F., Xie, J., Feener, E. P., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708839200 · Cited by 269
Metadata
- Authors
- Thong, F. S. L., Bilan, P. J., & Klip, A.
- Venue
- Diabetes
- Publisher
- American Diabetes Association
- Published
- 2007-02-01
- Volume
- 56
- Issue
- 2
- Pages
- 414-423
- ISSN
- 0012-1797 (ISSN-L)
- 1939-327X
- OpenAlex
- W2119950193
- Cited by
- 242
- References
- 8
- FWCI
- 8.86
- Type
- journal article
- Language
- en
- Open access
- closed
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- Thong, F. S. L., Bilan, P. J., & Klip, A. (2007). The Rab GTPase-Activating Protein AS160 Integrates Akt, Protein Kinase C, and AMP-Activated Protein Kinase Signals Regulating GLUT4 Traffic. Diabetes. https://doi.org/10.2337/db06-0900
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