Cited by 273Metabolism, Diabetes, and CancerPI3K/AKT/mTOR signaling in cancerMuscle Physiology and Disorders

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Increased Phosphorylation of Akt Substrate of 160 kDa (AS160) in Rat Skeletal Muscle in Response to Insulin or Contractile Activity

Bruss, Matthew D., Arias, Edward B., Lienhard, Gustav E., Cartee, Gregory D.·2005·Diabetes

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Abstract

In 3T3-L1 adipocytes, insulin-stimulated GLUT4 translocation requires phosphorylation of the protein designated Akt substrate of 160 kDa (AS160). Both insulin and contractions activate Akt in skeletal muscle. Therefore, we assessed the effects in skeletal muscle of each stimulus on phosphorylation of proteins, including AS160, on the Akt phosphomotif. Isolated rat epitrochlearis muscles were incubated with insulin (for time course and dose response), stimulated to contract, or incubated with 5-aminoimidazole-4-carboxamide-1-β-d-ribofuranoside (AICAR) and used to assess the following: serine-phosphorylation of Akt (P-Akt), immunoreactivity with an antibody recognizing the Akt phosphomotif (α-phospho-[Ser/Thr] Akt substrate [PAS]), and PAS immunoreactivity of samples immunoprecipitated with anti-AS160. P-Akt peaked at 5 min of insulin, and PAS immunoreactivity subsequently peaked for proteins of 250 kDa (10 min) and 160 kDa (15 min). P-Akt, PAS-160, and PAS-250 increased significantly with 0.6 nmol/l insulin. Contractile activity led to increased P-Akt and PAS immunoreactivity of proteins of 160 and 250 kDa. The 160-kDa protein was confirmed to be AS160 based on elevated PAS immunoreactivity in AS160 immunoprecipitates. Wortmannin inhibited insulin (120 nmol/l) and contraction effects on AS160 phosphorylation. Incubation with AICAR caused increased phosphorylation of AMP-activated protein kinase and AS160 but not Akt. Our working hypothesis is that phosphorylation of these putative Akt substrates is important for some of the insulin and contraction bioeffects.

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Crossref · 10.2337/diabetes.54.1.41

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“Multiple effectors of glucose uptake stimulate AS160 phosphorylation, including insulin (10,13–19), plateletderived growth factor (14), 5-aminoimidazole-4-carboxamide-1- -d-ribofuranoside (10,11,14,17), 4-phorbol-12myristate-13-acetate (a conventional/novel PKC activator) (14), K -induced membrane depolarization (14),…”
Background
Local overexpression of the myostatin propeptide increases glucose transporter expression and enhances skeletal muscle glucose disposal
Cleasby, M. E., Jarmin, S., Eilers, W., Elashry, M. I., Andersen, D. K., Dickson, G., & Foster, K. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00586.2013 · Cited by 57
“Translocation of GLUT4 to the plasma membrane from its intracellular depot is required for insulin-stimulated glucose uptake by muscle cells, involving inhibition of the GTPase activity of the RabGTPase-activating protein Akt substrate of 160 kDa (AS160/ TBC1D4) (7), whereas GSK3 -mediated disinhibition of glycogen sy…”
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“Enhanced glucose uptake from contraction appears to be due to increased GLUT4 translocation due to several mediators: activation of myocyte enhancer factor–2 [36,37,40], activation of a Rab GTPase-activating protein (AS160) [41-43], and improved insulin signaling [44], possibly through the tuberous sclerosis complex […”
Background
Control of Akt activity and substrate phosphorylation in cells
Yudushkin, I. A. (2020) · IUBMB Life · doi:10.1002/iub.2264 · Cited by 52
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Thyfault, J. P. (2008) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00924.2007 · Cited by 53
“Contraction and insulin phosphorylate AS160 independently, and the combined treatments can act synergistically upon AS160 phosphorylation in healthy skeletal muscle (8).”
Background
Identification of a novel AS160 splice variant that regulates GLUT4 translocation and glucose-uptake in rat muscle cells
Baus, D., Heermeier, K., de Hoop, M., Metz-Weidmann, C., Gassenhuber, J., Dittrich, W., Welte, S., & Tennagels, N. (2008) · Cellular Signalling · doi:10.1016/j.cellsig.2008.08.010 · Cited by 53
“Bruss et al. 2005 could show that AMPK is able to activate full-length AS160 as well.”
Background
Contraction-related stimuli regulate GLUT4 traffic in C2C12-GLUT4mycskeletal muscle cells
Niu, W., Bilan, P. J., Ishikura, S., Schertzer, J. D., Contreras‐Ferrat, A. E., Fu, Z., Liu, J., Boguslavsky, S., Foley, K. P., Liu, Z., et al. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00773.2009 · Cited by 51
“How could AMPK and contraction regulate GLUT4 traffic? Recently, several laboratories have shown that contraction or AICAR administration leads to phosphorylation of the RabGAP AS160/Tbc1d4 in cultured cells (13, 67), rodent muscle (2, 38, 69), and human muscle (23, 64).”
Background
PI3K/Akt pathway mediates high glucose-induced lipogenesis and extracellular matrix accumulation in HKC cells through regulation of SREBP-1 and TGF-β1
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“Considering that Akt phosphorylation is a very rapid process (Bruss et al. 2005) and the subsequent physiological effects need a certain period of time, we chose 48 h as observation time of cellular lipid metabolism.”
Background
Ciliary Neurotrophic Factor Stimulates Muscle Glucose Uptake by a PI3-Kinase–Dependent Pathway That Is Impaired With Obesity
Steinberg, G. R., Watt, M. J., Ernst, M., Birnbaum, M. J., Kemp, B. E., & Jørgensen, S. B. (2009) · Diabetes · doi:10.2337/db08-0659 · Cited by 54
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Lai, Y., Zarrinpashneh, E., & Jensen, J. (2010) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00401.2009 · Cited by 52
“AS160 and its closely related protein TBC1D1 have been shown to be phosphorylated by AMPK and have been proposed to mediate contraction-stimulated GLUT4 translocation (9, 12, 62, 64).”
Background
The effect of exercise and insulin on AS160 phosphorylation and 14-3-3 binding capacity in human skeletal muscle
Howlett, K. F., Mathews, A., Garnham, A., & Sakamoto, K. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00542.2007 · Cited by 47
“Given that AS160 is phosphorylated by exercise in humans (4, 28, 32) and in rodents after in vivo (1) and in vitro muscle contraction (2, 16, 17), AS160 has been proposed to be a point of convergence.”
Background
Sustained postexercise increases in AS160 Thr642and Ser588phosphorylation in skeletal muscle without sustained increases in kinase phosphorylation
Schweitzer, G. G., Arias, E. B., & Cartee, G. D. (2012) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00619.2012 · Cited by 47
“Insulin leads to increased AS160 phosphorylation in skeletal muscle (3), and this increase is important for insulinstimulated glucose transport (33).”
BackgroundSelf-citation
Therapeutic targeting of insulin-regulated aminopeptidase: Heads and tails?
Albiston, A. L., Peck, G. R., Yeatman, H. R., Fernando, R. N., Ye, S., & Chai, S. Y. (2007) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2007.07.006 · Cited by 46
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Rider, M. H. (2015) · Journal of Comparative Physiology B · doi:10.1007/s00360-015-0920-x · Cited by 44
“…glycolysis by phosphorylating components of the glucose transporter GLUT4 translocation machinery, such as the Akt substrate of 160 kDa (AS160) (Bruss et al. 2005; Kramer et al. 2006) and via phosphorylation of the key glycolytic control enzyme, 6-phosphofructo-2-kinase/fructose-2,6-bis-…”
Background
Stimulation of glucose transport in response to activation of distinct AMPK signaling pathways
Jing, M. X., Cheruvu, V. K., & Ismail‐Beigi, F. (2008) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00040.2008 · Cited by 44
“AS160 is a novel Rab GTPase-activating protein with two phosphotyrosine domains, a COOH-terminal Rab-GAP domain, and six phosphorylation motifs (RXRXXS*/T*) targeted by Akt and other kinases (7).”
Background
How is AMPK activity regulated in skeletal muscles during exercise?
Jørgensen, S. B. (2008) · Frontiers in bioscience · doi:10.2741/3102 · Cited by 45
“Studies of resting (non-contracting), fully differentiated rodent skeletal muscle and cultured muscle cells have shown that AMPK promotes ATPsynthesis by increasing GLUT4 translocation (13, 75, 136) and glucose uptake (45, 81, 85), as well as uptake and βoxidation of fatty acids (11, 80, 81, 148).”
Background
Electrical pulse stimulation induces GLUT4 translocation in C 2 C 12 myotubes that depends on Rab8A, Rab13, and Rab14
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“Previous studies have showed that isolated rat epitrochlearis muscle was exposed to AICAR, which induced increase of AS160 phosphorylation [23].”
Background
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Kny, M., & Fielitz, J. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.878755 · Cited by 48
“In addition, activation of the insulin receptor via the Akt substrate of 160 kDa leads to translocation of the glucose transporter (GLUT)-4 into the plasma membrane, which increases cellular glucose uptake (99).”
Background
Role of Akt isoforms in neuronal insulin signaling and resistance
Sharma, M., & Dey, C. S. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03993-6 · Cited by 47
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Jain, S. S., Luiken, J. J. F. P., Snook, L. A., Han, X. X., Holloway, G. P., Glatz, J. F. C., & Bonen, A. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.08.010 · Cited by 43
“Hence, insulin and contraction stimulate GLUT4 translocation via distinct signaling pathways: insulin-stimulated, but not contraction-stimulated, GLUT4 translocation is dependent on Akt2 [2,4,26,27].”
Background
Effect of Insulin on Proximal Tubules Handling of Glucose: A Systematic Review
Moreira, R. P., & Muscelli, E. (2020) · Journal of Diabetes Research · doi:10.1155/2020/8492467 · Cited by 40
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“One AMPK target is the protein Tbc1d4/ AS160 (Treebak et al. 2006, Thong et al. 2007), which is also a target of Akt downstream of the insulin receptor (Sano et al. 2003, Bruss et al. 2005).”
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Ouwens, D. M., & Diamant, M. (2007) · Archives of Physiology and Biochemistry · doi:10.1080/13813450701422633 · Cited by 41
“AS160 is phosphorylated in response to insulin on multiple consensus PKB/Akt phosphor- ylation sites in adipocytes (Kane et al., 2002), and skeletal muscle (Bruss et al., 2005; Karlsson et al., 2005).”
Background
Oligomeric resistin impairs insulin and AICAR-stimulated glucose uptake in mouse skeletal muscle by inhibiting GLUT4 translocation
Jørgensen, S. B., Honeyman, J. E., Oakhill, J. S., Fazakerley, D. J., Stöckli, J., Kemp, B. E., & Steinberg, G. R. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90744.2008 · Cited by 44
Phospholipase D1 Mediates AMP-Activated Protein Kinase Signaling for Glucose Uptake
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“Recent reports have revealed that AS 160, which is a known substrate for AKT, is also a downstream molecule of AMPK in contraction-stimulated glucose uptake [28-30].”
Background
Lipid-induced insulin resistance is prevented in lean and obese myotubes by AICAR treatment
Bikman, B. T., Zheng, D., Reed, M. A., Hickner, R. C., Houmard, J. A., & Dohm, G. L. (2010) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00190.2009 · Cited by 42
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Overexpression of Interleukin-15 exhibits improved glucose tolerance and promotes GLUT4 translocation via AMP-Activated protein kinase pathway in skeletal muscle
Fujimoto, T., Sugimoto, K., Takahashi, T., Yasunobe, Y., Keyu, X., Tanaka, M., Ohnishi, Y., Yoshida, S., Kurinami, H., Akasaka, H., et al. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.01.024 · Cited by 40
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Dreyer, H. C., Drummond, M. J., Glynn, E. L., Fujita, S., Chinkes, D. L., Volpi, E., & Rasmussen, B. B. (2008) · Journal of Applied Physiology · doi:10.1152/japplphysiol.90562.2008 · Cited by 42
“On the other hand, muscle contraction-induced phosphorylation of AS160 in isolated rat epitrochlearis muscle is inhibited by wortmannin (4), whereas wortmannin only partially inhibits the contraction-induced increase in AS160 phosphorylation in isolated mouse extensor digitorum longus muscle (20).”
BackgroundInfluential
Electrical vs Manual Acupuncture Stimulation in a Rat Model of Polycystic Ovary Syndrome: Different Effects on Muscle and Fat Tissue Insulin Signaling
Johansson, J., Mannerås-Holm, L., Shao, R., Olsson, A., Lönn, M., Billig, H., & Stener‐Victorin, E. (2013) · PLoS ONE · doi:10.1371/journal.pone.0054357 · Cited by 39
Astragalus polysaccharide stimulates glucose uptake in L6 myotubes through AMPK activation and AS160/TBC1D4 phosphorylation
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Resistance exercise and insulin regulate AS160 and interaction with 14-3-3 in human skeletal muscle
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“AS160 phosphorylation is increased in rodent skeletal muscle by contraction (13) and AICAR (5-aminoimidazole4-carboxamide riboside, a pharmacological activator of AMPK), and from AMPK transgenic animal studies, this effect is regulated, at least in part, through AMPK (14,15).”
Background
Spexin ameliorates skeletal muscle insulin resistance through activation of GAL2 receptor
Yu, M., Wang, M., Han, S., Han, L., Kan, Y., Zhao, J., Yu, X., Yan, J., Yu, J. Z., Zhang, Z., et al. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.174731 · Cited by 38
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Self-citation
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Østergård, T., Jessen, N., Schmitz, O., & Mandarino, L. J. (2007) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/h07-031 · Cited by 36
“AS160 is also expressed in skeletal muscles, and is activated by insulin stimulation (Bruss et al. 2005); however, it is not known whether AS160 is required for insulin-stimulated glucose transport in skeletal muscle.”
Background
Motor End Plate Innervation Loss in Diabetes and the Role of Insulin
Francis, G. J., Martinez, J. A., Liu, W. Q., Zochodne, D. W., Hanson, L. R., Frey, W. H., & Toth, C. C. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e318215669a · Cited by 36
“Insulin upregulates proteinYtyrosine phosphorylation (43) through downstream activation of IRS-2 (44), thereby promoting the activation of Akt and phosphorylation of Akt substrates (45).”
Background
Thr649Ala-AS160 knock-in mutation does not impair contraction/AICAR-induced glucose transport in mouse muscle
Ducommun, S., Wang, H. Y., Sakamoto, K., MacKintosh, C., & Chen, S. (2012) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00379.2011 · Cited by 35
“(2) reported a PAS signal from AS160 immunoprecipi-”
Background
Reactive Oxygen and Nitrogen Species (RONS) and Cytokines—Myokines Involved in Glucose Uptake and Insulin Resistance in Skeletal Muscle
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“The AS160 protein has a GTPase-activating domain which promotes GLUT4 translocation from GLUT4 storage vesicles (GSVs) to the plasma membrane (PM) to enhance glucose uptake [56].”
BackgroundInfluential
Energetic adaptations: Metabolic control of endocytic membrane traffic
Rahmani, S., Defferrari, M. S., Wakarchuk, W. W., & Antonescu, C. N. (2019) · Traffic · doi:10.1111/tra.12705 · Cited by 36
Recycling of IRAP from the plasma membrane back to the insulin-responsive compartment requires the Q-SNARE syntaxin 6 but not the GGA clathrin adaptors
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“, 2003), AS160 has generated substantial interest because it harbors a Rab GAP (GTPase-activating protein) domain that might participate in regulating one or more steps of IRAP/GLUT4 trafficking (Arias et al., 2007; Bruss et al., 2005; Eguez et al., 2005; Ishikura et al., 2007; Kramer et al., 2006; Larance et al., 200…”
Background
Insulin regulates alveolar epithelial function by inducing Na+/K+-ATPase translocation to the plasma membrane in a process mediated by the action of Akt
Comellas, A. P., Kelly, A. M., Bittar, H. E. T., Briva, A., Lee, J. S., Sznajder, J. I., & Dada, L. A. (2010) · Journal of Cell Science · doi:10.1242/jcs.066464 · Cited by 34
“to maintain the Rab proteins in their inactive state (Bruss et al., 2005; Eguez et al., 2005; Thong et al., 2007).”
Background
AS160 Phosphotyrosine-binding Domain Constructs Inhibit Insulin-stimulated GLUT4 Vesicle Fusion with the Plasma Membrane
Koumanov, F., Richardson, J. D., Murrow, B. A., & Holman, G. D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.226092 · Cited by 33
Novel d -Xylose Derivatives Stimulate Muscle Glucose Uptake by Activating AMP-Activated Protein Kinase α
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Exercise-induced phospho-proteins in skeletal muscle
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“8 Insulin stimulation of skeletal muscle leads to phosphorylation of AS160, a process dependent on Akt”
Background
Akt Links Insulin Signaling to Albumin Endocytosis in Proximal Tubule Epithelial Cells
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Contraction-stimulated glucose transport in rat skeletal muscle is sustained despite reversal of increased PAS-phosphorylation of AS160 and TBC1D1
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“In an earlier study, our laboratory found that a brief and discontinuous tetanic stimulation protocol (10-s tetanus duration, 2 tetani/min for 5 min), which induced a large activation of Akt, can also increase AS160 phosphorylation (3).”
BackgroundResultInfluentialSelf-citation
Activation of phosphatidylinositol-3 kinase, AMP-activated kinase and Akt substrate-160 kDa by trans-10, cis-12 conjugated linoleic acid mediates skeletal muscle glucose uptake
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“Moreover, the unique behaviour of CLA isomers on Akt-independent phosphorylation of AS160 resembles the effect of AICAR on skeletal muscle cells [52].”
Background
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Leptin Reduces the Expression and Increases the Phosphorylation of the Negative Regulators of GLUT4 Traffic TBC1D1 and TBC1D4 in Muscle of ob/ob Mice
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“…to be a site of signal integration for insulin- and contractionstimulated signalling to GLUT4 translocation, and AS160 is also phosphorylated in rat skeletal muscle (Bruss et al. 2005) and in human skeletal muscle (Deshmukh et al. 2006) in response to contraction concomitant to Akt phosphorylation.”
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“response to either insulin or contractile activity [39-42].”
Background
Immobilization rapidly induces muscle insulin resistance together with the activation of MAPK s ( JNK and p38) and impairment of AS 160 phosphorylation
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“Our second hypothesis regarding the mechanism of muscle insulin resistance linked to acute inactivity is the decreased phosphorylation of Rab-GTPase-activating protein (GAP), that is, AS160 (Akt substrate of 160 kDa; also known as TBC1D4) and its paralog TBC1D1 (tre-2/USP6, BUB2, cdc 16 domain…”
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Background
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Background
The effect of acute exercise on glycogen synthesis rate in obese subjects studied by 13C MRS
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“In addition, it has been reported that in muscle cells, contraction increased AS160 phosphorylation ( Bruss et al. 2005; Deshmukh et al. 2006), and in a cell-free assay, heterotrimeric AMPK complexes are able to phosphorylate AS160 (Treebak et al. 2006).”
Background
A robust assay measuring GLUT4 translocation in rat myoblasts overexpressing GLUT4-myc and AS160_v2
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Authors: Bruss, M. D., Arias, E. B., Lienhard, G. E., & Cartee, G. D.
Affiliations: University of Wisconsin–Madison (US)
University of Michigan (US)
Dartmouth College (US)
ORCID: Arias, Edward B.
Cartee, Gregory D.
Venue: Diabetes
Publisher: American Diabetes Association
Published: 2005-01-01
Volume: 54
Issue: 1
Pages: 41-50
ISSN: 0012-1797 (ISSN-L)
1939-327X
DOI: 10.2337/diabetes.54.1.41
OpenAlex: W2148321229
Cited by: 273
References: 30
Citations by year: 2025: 2 · 2023: 1 · 2022: 14 · 2021: 9 · 2020: 5 · 2019: 10 · 2018: 11 · 2017: 7 · 2016: 7 · 2015: 16 · 2014: 16 · 2013: 11 · 2012: 20
FWCI: 9.97
Type: journal article
Language: en
Open access: closed
Locations: Diabetes (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Institute on Aging (AG 10026)
National Institute of Diabetes and Digestive and Kidney Diseases (R01DK025336, DK-25336, R56DK042816)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Keywords: AS160, Akt phosphorylation, skeletal muscle, insulin signaling, muscle contraction, GLUT4 translocation, AMPK, wortmannin, epitrochlearis muscle
MeSH terms: Aminoimidazole Carboxamide, Animals, Insulin, Kinetics, Male, Muscle Contraction, Muscle Proteins, Phosphorylation, Proto-Oncogene Proteins, Ribonucleotides, Rats, Wistar, Protein Serine-Threonine Kinases, Muscle, Skeletal, Proto-Oncogene Proteins c-akt, Rats

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Increased Phosphorylation of Akt Substrate of 160 kDa (AS160) in Rat Skeletal Muscle in Response to Insulin or Contractile Activity

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