Adipose-specific Expression, Phosphorylation of Ser794 in Insulin Receptor Substrate-1, and Activation in Diabetic Animals of Salt-inducible Kinase-2
Open accessAbstract
Salt-inducible kinase (SIK), first cloned from the adrenal glands of rats fed a high salt diet, is a serine/threonine protein kinase belonging to an AMP-activated protein kinase family. Induced in Y1 cells at an early stage of ACTH stimulation, it regulated the initial steps of steroidogenesis. Here we report the identification of its isoform SIK2. When a green fluorescent protein-fused SIK2 was expressed in 3T3-L1 preadipocytes, it was mostly present in the cytoplasm. When coexpressed in cAMP-responsive element-reporter assay systems, SIK2 could repress the cAMP-responsive element-dependent transcription, although the degree of repression seemed weaker than that by SIK1. SIK2 was specifically expressed in adipose tissues. When 3T3-L1 cells were treated with the adipose differentiation mixture, SIK2 mRNA was induced within 1 h, the time of induction almost coinciding with that of c/EBPbeta mRNA. Coexpressed with human insulin receptor substrate-1 (IRS-1) in COS cells, SIK2 could phosphorylate Ser(794) of human IRS-1. Adenovirus-mediated overexpression of SIK2 in adipocytes elevated the level of phosphorylation at Ser(789), the mouse equivalent of human Ser(794). Moreover, the activity and content of SIK2 were elevated in white adipose tissues of db/db diabetic mice. These results suggest that highly expressed SIK2 in insulin-stimulated adipocytes phosphorylates Ser(794) of IRS-1 and, as a result, might modulate the efficiency of insulin signal transduction, eventually causing the insulin resistance in diabetic animals.
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IRS1 S789 phosphorylation is negatively associated with insulin signaling.
“Alternative studies show that IRS1 S789 phosphorylation is negatively associated with insulin signaling [146-149].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [148]
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1 retracted
Insulin Stimulates PKCζ-mediated Phosphorylation of Insulin Receptor Substrate-1 (IRS-1)
Liu, Y., Paz, K., Herschkovitz, A., Alt, A., Tennenbaum, T., Sampson, S. R., Ohba, M., Kuroki, T., LeRoith, D., & Zick, Y. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007281200 · Cited by 158 · see citing works
RetractedInsulin signalling and the regulation of glucose and lipid metabolism
Saltiel, A. R., & Kahn, C. R. (2001) · Nature · doi:10.1038/414799a · Cited by 5,326 · see citing works
Abnormal splicing of the leptin receptor in diabetic mice
Lee, G.-H., Proenca, R., Montez, J. M., Carroll, K. M., Darvishzadeh, J. G., Lee, J. I., & Friedman, J. M. (1996) · Nature · doi:10.1038/379632a0 · Cited by 2,327 · see citing works
Aguirre, V., Uchida, T., Yenush, L., Davis, R., & White, M. F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.12.9047 · Cited by 1,487 · see citing works
Lewis, G. F., Carpentier, A. C., Adeli, K., & Giacca, A. (2002) · Endocrine Reviews · doi:10.1210/edrv.23.2.0461 · Cited by 1,328 · see citing works
PPARγ: a Nuclear Regulator of Metabolism, Differentiation, and Cell Growth
Rosen, E. D., & Spiegelman, B. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.r100034200 · Cited by 1,174 · see citing works
Yeh, W., Cao, Z. D., Classon, M., & McKnight, S. L. (1995) · Genes & Development · doi:10.1101/gad.9.2.168 · Cited by 926 · see citing works
New Perspectives into the Molecular Pathogenesis and Treatment of Type 2 Diabetes
Saltiel, A. R. (2001) · Cell · doi:10.1016/s0092-8674(01)00239-2 · Cited by 684 · see citing works
Pref-1, a protein containing EGF-like repeats, inhibits adipocyte differentiation
Smas, C. M., & Sul, H. S. (1993) · Cell · doi:10.1016/0092-8674(93)90252-l · Cited by 677 · see citing works
Rui, L., Aguirre, V., Kim, J. K., Shulman, G. I., Lee, A., Corbould, A. M., Dunaif, A. E., & White, M. F. (2001) · Journal of Clinical Investigation · doi:10.1172/jci10934 · Cited by 600 · see citing works
The insulin signalling system and the IRS proteins
White, M. F. (1997) · Diabetologia · doi:10.1007/s001250051387 · Cited by 581 · see citing works
Haruta, T., Uno, T., Kawahara, J., Takano, A., Egawa, K., Sharma, P. M., Olefsky, J., & Kobayashi, M. (2000) · Molecular Endocrinology · doi:10.1210/mend.14.6.0446 · Cited by 437 · see citing works
Pathogenesis of skeletal muscle insulin resistance in type 2 diabetes mellitus
Petersen, K. F., & Shulman, G. I. (2002) · The American Journal of Cardiology · doi:10.1016/s0002-9149(02)02554-7 · Cited by 390 · see citing works
Özeş, O. N., Akça, H., Mayo, L. D., Gustin, J. A., Maehama, T., Dixon, J. E., & Donner, D. B. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.051042298 · Cited by 383 · see citing works
Distinct Transcriptional Profiles of Adipogenesisin Vivo and in Vitro
Soukas, A. A., Socci, N. D., Saatkamp, B. D., Novelli, S. E., & Friedman, J. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104421200 · Cited by 368 · see citing works
The IRS-Signaling System: A Network of Docking Proteins That Mediate Insulin and Cytokine Action
White, M. F., & Yenush, L. (1998) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-80481-6_8 · Cited by 360 · see citing works
CREB Activation Induces Adipogenesis in 3T3-L1 Cells
Reusch, J. E. B., Colton, L. A., & Klemm, D. J. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.3.1008-1020.2000 · Cited by 341 · see citing works
Phosphorylation of insulin receptor substrate 1 by glycogen synthase kinase 3 impairs insulin action
Eldar-Finkelman, H., & Krebs, E. G. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.18.9660 · Cited by 319 · see citing works
Insulin resistance: a phosphorylation-based uncoupling of insulin signaling
Zick, Y. (2001) · Trends in Cell Biology · doi:10.1016/s0962-8924(01)02129-8 · Cited by 302 · see citing works
De Fea, K., & Roth, R. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.50.31400 · Cited by 298 · see citing works
Jakobsen, S. N., Hardie, D. G., Morrice, N., & Tornqvist, H. E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100483200 · Cited by 238 · see citing works
Ravichandran, L. V., Esposito, D. L., Chen, J. Y. ‐., & Quon, M. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007231200 · Cited by 217 · see citing works
Insulin-induced Adipocyte Differentiation
Klemm, D. J., Leitner, J. W., Watson, P., Nesterova, A., Reusch, J. E. B., Goalstone, M. L., & Draznin, B. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103382200 · Cited by 212 · see citing works
Li, J., DeFea, K., & Roth, R. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.14.9351 · Cited by 196 · see citing works
Paz, K., Liu, Y., Shorer, H., Hemi, R., LeRoith, D., Quan, M., Kanety, H., Seger, R., & Zick, Y. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.40.28816 · Cited by 191 · see citing works
Ogihara, T., Isobe, T., Ichimura, T., Taoka, M., Funaki, M., Sakoda, H., Onishi, Y., Inukai, K., Anai, M., Fukushima, Y., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.40.25267 · Cited by 162 · see citing works
Self-citationCloning of a novel kinase (SIK) of the SNF1/AMPK family from high salt diet‐treated rat adrenal1
Wang, Z.-N., Takemori, H., Halder, S. K., Nonaka, Y., & Okamoto, M. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00708-5 · Cited by 161 · see citing works
Self-citationEngelman, J. A., Berg, A. H., Lewis, R. Y., Lisanti, M. P., & Scherer, P. E. (2000) · Molecular Endocrinology · doi:10.1210/mend.14.10.0542 · Cited by 138 · see citing works
Insulin Resistance With Enhanced Insulin Signaling in High-Salt Diet–Fed Rats
Ogihara, T., Asano, T., Ando, K., Chiba, Y., Sekine, N., Sakoda, H., Anai, M., Onishi, Y., Fujishiro, M., Ono, H., et al. (2001) · Diabetes · doi:10.2337/diabetes.50.3.573 · Cited by 120 · see citing works
Self-citationInsulin resistance: a phosphorylation-based uncoupling of insulin signaling
Zick, Y. (2001) · Trends in Cell Biology · doi:10.1016/s0962-8924(01)81297-6 · Cited by 109 · see citing works
Qiao, L.-Y., Zhande, R., Jetton, T. L., Zhou, G., & Sun, X. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201494200 · Cited by 104 · see citing works
Self-citationHalder, S. K., Takemori, H., Hatano, O., Nonaka, Y., Wada, A., & Okamoto, M. (1998) · Endocrinology · doi:10.1210/endo.139.7.6081 · Cited by 102 · see citing works
Self-citationAnai, M., Funaki, M., Ogihara, T., Kanda, A., Onishi, Y., Sakoda, H., Inukai, K., Nawano, M., Fukushima, Y., Yazaki, Y., et al. (1999) · Diabetes · doi:10.2337/diabetes.48.1.158 · Cited by 99 · see citing works
Self-citationBelmonte, N., Phillips, B. W., Massiéra, F., Villageois, P., Wdziekonski, B., Saint-Marc, P., Nichols, J., Aubert, J., Saeki, K., Yuo, A., et al. (2001) · Molecular Endocrinology · doi:10.1210/mend.15.11.0721 · Cited by 98 · see citing works
Greene, M. W., & Garofalo, R. S. (2002) · Biochemistry · doi:10.1021/bi015992f · Cited by 88 · see citing works
Virtual cloning, functional expression, and gating analysis of human connexin31.9
White, T. W., Srinivas, M., Ripps, H., Salinaro, A. T., Condorelli, D. F., & Bruzzone, R. (2002) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00163.2002 · Cited by 84 · see citing works
Phosphorylation of the insulin receptor substrate IRS-1 by casein kinase II.
Tanasijevic, M. J., Myers, M. G., Thoma, R. S., Crimmins, D. L., White, M. F., & Sacks, D. B. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)46824-4 · Cited by 83 · see citing works
ACTH-induced Nucleocytoplasmic Translocation of Salt-inducible Kinase
Takemori, H., Katoh, Y., Horike, N., Doi, J., & Okamoto, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204602200 · Cited by 79 · see citing works
Self-citationReusch, J. E. B., & Klemm, D. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107923200 · Cited by 78 · see citing works
Lin, X., Takemori, H., Katoh, Y., Doi, J., Horike, N., Makino, A., Nonaka, Y., & Okamoto, M. (2001) · Molecular Endocrinology · doi:10.1210/mend.15.8.0675 · Cited by 68 · see citing works
Self-citationAMP-activated protein kinase kinase: detection with recombinant AMPK α1 subunit
Hamilton, S. R., O’Donnell, J. B., Hammet, A., Stapleton, D., Habinowski, S. A., Means, A. R., Kemp, B. E., & Witters, L. A. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00312-1 · Cited by 58 · see citing works
Doi, J., Takemori, H., Lin, X., Horike, N., Katoh, Y., & Okamoto, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109365200 · Cited by 57 · see citing works
Self-citation14-3-3 Facilitates Insulin-Stimulated Intracellular Trafficking of Insulin Receptor Substrate 1
Xiang, X., Yuan, M., Song, Y., Ruderman, N. B., Wen, R., & Luo, Z. (2002) · Molecular Endocrinology · doi:10.1210/mend.16.3.0790 · Cited by 53 · see citing works
Identification of Functional Domains of Rat Intestinal Phospholipase B/Lipase
Takemori, H., Zolotaryov, F. N., Lü, T., Tchoua, U., Komatsubara, T., Hatano, O., Okamoto, M., & Tojo, H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.4.2222 · Cited by 48 · see citing works
Self-citationRegulation of Fat Synthesis and Adipose Differentiation
Sul, H. S., Smas, C. M., Wang, D., & Chen, L. (1998) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(08)60896-x · Cited by 41 · see citing works
Kurebayashi, S., Sumitani, S., Kasayama, S., JETTE, A. M., & Hirose, T. (2001) · Endocrine Journal · doi:10.1507/endocrj.48.249 · Cited by 32 · see citing works
Self-citationYamamoto, H., Kurebayashi, S., Hirose, T., Kouhara, H., & Kasayama, S. (2002) · Journal of Cell Science · doi:10.1242/jcs.00044 · Cited by 31 · see citing works
Self-citationDoi, J., Takemori, H., Ohta, M., Nonaka, Y., & Okamoto, M. (2001) · Journal of Endocrinology · doi:10.1677/joe.0.1680087 · Cited by 21 · see citing works
Self-citation
Flagged first, then by citations
Research works printed but not linked: 2
- Eldar-Finkelman, H., and Krebs, E. G. (1997) Proc. Natl. Acad. Sci. U. S. A. 94, 9660 -9664
- Ozes, O. N., Akca, H., Mayo, L. D., Gustin, J. A., Maehama, T., Dixon, J. E., and Donner, D. B. (2001) Proc. Natl. Acad. Sci. U. S. A. 98, 4640 -4645
Cited by
Sorted by citations
LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR‐1
Lizcano, J. M., Göransson, O., Toth, R., Deak, M., Morrice, N. A., Boudeau, J., Hawley, S. A., Udd, L., Mäkelä, T. P., Hardie, D. G., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600110 · Cited by 1,381 · see citing works
Copps, K. D., & White, M. F. (2012) · Diabetologia · doi:10.1007/s00125-012-2644-8 · Cited by 1,017 · see citing works
“S789 of IRS1 when co-expressed in cells [143].”
BackgroundPositive and negative regulation of insulin signaling through IRS-1 phosphorylation
Gual, P., Le Marchand-Brustel, Y., & Tanti, J.-F. (2005) · Biochimie · doi:10.1016/j.biochi.2004.10.019 · Cited by 912 · see citing works
Morino, K., Petersen, K. F., & Shulman, G. I. (2006) · Diabetes · doi:10.2337/db06-s002 · Cited by 853 · see citing works
LKB1-Dependent Signaling Pathways
Alessi, D. R., Sakamoto, K., & Bayascas, J. R. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142702 · Cited by 783 · see citing works
Phosphorylation of IRS proteins, insulin action, and insulin resistance
Boura-Halfon, S., & Zick, Y. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90437.2008 · Cited by 598 · see citing works
The Molecular Basis for Oxidative Stress-Induced Insulin Resistance
Evans, J. L., Maddux, B. A., & Goldfine, I. D. (2005) · Antioxidants & Redox Signaling · doi:10.1089/ars.2005.7.1040 · Cited by 587 · see citing works
Restraining PI3K: mTOR signalling goes back to the membrane
Harrington, L. S., Findlay, G. M., & Lamb, R. F. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.11.003 · Cited by 362 · see citing works
Bricambert, J., Miranda, J., Benhamed, F., Girard, J. R., Postic, C., & Dentin, R. (2010) · Journal of Clinical Investigation · doi:10.1172/jci41624 · Cited by 299 · see citing works
AMPK and Exercise: Glucose Uptake and Insulin Sensitivity
O'Neill, H. M. (2013) · Diabetes & Metabolism Journal · doi:10.4093/dmj.2013.37.1.1 · Cited by 295 · see citing works
Pirola, L., Johnston, A., & OBBERGHEN, E. V. (2004) · Diabetologia · doi:10.1007/s00125-003-1313-3 · Cited by 281 · see citing works
Insulin Resistance Due to Phosphorylation of Insulin Receptor Substrate-1 at Serine 302
Werner, E. D., Lee, J., Hansen, L., Yuan, M., & Shoelson, S. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405203200 · Cited by 252 · see citing works
A Hormone-Dependent Module Regulating Energy Balance
Wang, B., Moya, N., Niessen, S., Hoover, H. S., Mihaylova, M. M., Shaw, R. J., Yates, J. R., Fischer, W. H., Thomas, J. B., & Montminy, M. (2011) · Cell · doi:10.1016/j.cell.2011.04.013 · Cited by 242 · see citing works
MacKenzie, K. F., Clark, K., Naqvi, S., McGuire, V. A., Nöehren, G., Kristariyanto, Y. A., van den Bosch, M., Mudaliar, M., McCarthy, P. C., Pattison, M. J., et al. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1202462 · Cited by 244 · see citing works
The regulation and function of mammalian AMPK‐related kinases
Bright, N. J., Thornton, C., & Carling, D. (2009) · Acta Physiologica · doi:10.1111/j.1748-1716.2009.01971.x · Cited by 200 · see citing works
Silencing the constitutive active transcription factor CREB by the LKB1‐SIK signaling cascade
Katoh, Y., Takemori, H., Lin, X., Tamura, M., Muraoka, M., Satoh, T., Tsuchiya, Y., Li, M., Doi, J., Miyauchi, A., et al. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2006.05291.x · Cited by 173 · see citing works
Self-citationActivation of AMPKα2 in adipocytes is essential for nicotine-induced insulin resistance in vivo
Wu, Y., Song, P., Zhang, W., Liu, J., Dai, X., Liu, Z., Lu, Q., Ouyang, C., Xie, Z., Zhao, Z., et al. (2015) · Nature Medicine · doi:10.1038/nm.3826 · Cited by 169 · see citing works
Miranda, F., Mannion, D., Liu, S., Zheng, Y., Mangala, L. S., Redondo, C., Herrero‐González, S., Xu, R., Taylor, C., Fotso, D. C., et al. (2016) · Cancer Cell · doi:10.1016/j.ccell.2016.06.020 · Cited by 167 · see citing works
The LKB1-salt-inducible kinase pathway functions as a key gluconeogenic suppressor in the liver
Patel, K. A., Foretz, M., Marion, A., Campbell, D. G., Gourlay, R., Boudaba, N., Tournier, E., Titchenell, P. M., Peggie, M. W., Deák, M., et al. (2014) · Nature Communications · doi:10.1038/ncomms5535 · Cited by 162 · see citing works
LKB1, Salt-Inducible Kinases, and MEF2C are linked dependencies in acute myeloid leukemia
Tarumoto, Y., Lu, B., Somerville, T., Huang, Y.-H., Milazzo, J. P., Wu, X.-L. S., Klingbeil, O., Demerdash, O. E., Shi, J.-W., & Vakoc, C. R. (2018) · Molecules and Cells · doi:10.1016/j.molcel.2018.02.011 · Cited by 132 · see citing works
Scavo, L. M., Karas, M., Murray, M., & LeRoith, D. (2004) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2003-031682 · Cited by 157 · see citing works
Salt-Inducible Kinases: Physiology, Regulation by cAMP, and Therapeutic Potential
Wein, M. N., Foretz, M., Fisher, D. E., Xavier, R. J., & Kronenberg, H. M. (2018) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2018.08.004 · Cited by 138 · see citing works
Tzatsos, A., & Tsichlis, P. N. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610101200 · Cited by 139 · see citing works
The potent roles of salt-inducible kinases (SIKs) in metabolic homeostasis and tumorigenesis
Sun, Z., Jiang, Q., Li, J., & Guo, J. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00265-w · Cited by 130 · see citing works
Nuts and bolts of the salt-inducible kinases (SIKs)
Darling, N. J., & Cohen, P. (2021) · Biochemical Journal · doi:10.1042/bcj20200502 · Cited by 134 · see citing works
14-3-3 cooperates with LKB1 to regulate the activity and localization of QSK and SIK
Al-Hakim, A., Göransson, O., Deák, M., Toth, R. L., Campbell, D. G., MORRICE, N. A., Prescott, A. R., & Alessi, D. R. (2005) · Journal of Cell Science · doi:10.1242/jcs.02670 · Cited by 117 · see citing works
Chopra, I., Li, H. F., Wang, H., & Webster, K. A. (2012) · Diabetologia · doi:10.1007/s00125-011-2407-y · Cited by 116 · see citing works
The LKB1 tumor suppressor kinase in human disease
Katajisto, P., Vallenius, T., Vaahtomeri, K., Ekman, N., Udd, L., Tiainen, M., & Mäkelä, T. P. (2006) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2006.08.003 · Cited by 107 · see citing works
Salt-inducible kinases regulate growth through the Hippo signalling pathway in Drosophila
Wehr, M. C., Holder, M. V., Gailite, I., Saunders, R. E., Maile, T. M., Ciirdaeva, E., Instrell, R., Jiang, M., Howell, M. T., Rossner, M. J., et al. (2012) · Nature Cell Biology · doi:10.1038/ncb2658 · Cited by 108 · see citing works
Hançer, N. J., Qiu, W., Cherella, C. E., Li, Y., Copps, K. D., & White, M. F. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.554162 · Cited by 107 · see citing works
Salt-inducible kinase (SIK) isoforms: their involvement in steroidogenesis and adipogenesis
Katoh, Y., Takemori, H., Horike, N., Doi, J., Muraoka, M., Li, M., & Okamoto, M. (2003) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2003.10.016 · Cited by 102 · see citing works
Self-citationAntioxidants: do they have a role in the treatment of insulin resistance?
Evans, J. L. (2007) · PubMed · Cited by 99 · see citing works
The Salt-Inducible Kinases: Emerging Metabolic Regulators
Sakamoto, K., Bultot, L., & Göransson, O. (2018) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2018.09.007 · Cited by 99 · see citing works
Walkinshaw, D. R., Weist, R., Kim, G.-W., You, L., Xiao, L., Nie, J., Li, C. S., Zhao, S., Xu, M., & Yang, X. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.456996 · Cited by 98 · see citing works
Sjöström, M., Stenström, K., Eneling, K., Zwiller, J., Katz, A. I., Takemori, H., & Bertorello, A. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706838104 · Cited by 94 · see citing works
Self-citationSalt-inducible kinase in steroidogenesis and adipogenesis
Okamoto, M., Takemori, H., & Katoh, Y. (2003) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2003.11.002 · Cited by 89 · see citing works
Self-citationNing, J., & Clemmons, D. R. (2010) · Molecular Endocrinology · doi:10.1210/me.2009-0474 · Cited by 89 · see citing works
Darling, N. J., Toth, R. L., Arthur, J. S. C., & Clark, K. (2016) · Biochemical Journal · doi:10.1042/bcj20160646 · Cited by 87 · see citing works
van der Linden, A. M., Nolan, K. M., & Sengupta, P. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601479 · Cited by 87 · see citing works
Regulation of AMP‐activated protein kinase by LKB1 and CaMKK in adipocytes
Gormand, A., Henriksson, E., Ström, K., Jensen, T. E., Sakamoto, K., & Göransson, O. (2011) · Journal of Cellular Biochemistry · doi:10.1002/jcb.23053 · Cited by 83 · see citing works
Phosphorylation of microtubule‐associated protein tau by AMPK‐related kinases
Yoshida, H., & Goedert, M. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07523.x · Cited by 85 · see citing works
Regulation of CREB-mediated gene expression by salt inducible kinase
Takemori, H., & Okamoto, M. (2007) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2007.09.006 · Cited by 85 · see citing works
Self-citationSalt-inducible kinase 2 regulates CRTCs, HDAC4 and glucose uptake in adipocytes
Henriksson, E., Säll, J., Gormand, A., Wasserström, S., Morrice, N. A., Fritzen, A. M., Foretz, M., Campbell, D. G., Sakamoto, K., Ekelund, M., et al. (2014) · Journal of Cell Science · doi:10.1242/jcs.153932 · Cited by 85 · see citing works
Leclerc, G. M., Leclerc, G. J., Fu, G., & Barredo, J. C. (2010) · Journal of Molecular Signaling · doi:10.1186/1750-2187-5-15 · Cited by 84 · see citing works
A UV-Independent Topical Small-Molecule Approach for Melanin Production in Human Skin
Mujahid, N., Liang, Y., Murakami, R., Choi, H. G., Dobry, A. S., Wang, J., Suita, Y., Weng, Q. Y., Allouche, J., Kemény, L. V., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.05.042 · Cited by 81 · see citing works
Beichman, A. C., Koepfli, K., Li, G., Murphy, W. J., Dobrynin, P., Kliver, S. F., Tinker, M. T., Murray, M. J., Johnson, J., Lindblad‐Toh, K., et al. (2019) · Molecular Biology and Evolution · doi:10.1093/molbev/msz101 · Cited by 78 · see citing works
RegPhos: a system to explore the protein kinase–substrate phosphorylation network in humans
Lee, T.-Y., Hsu, J. B., Chang, W., & Huang, H. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq970 · Cited by 78 · see citing works
Katoh, Y., Takemori, H., Li, M., Muraoka, M., Doi, J., Horike, N., & Okamoto, M. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04372.x · Cited by 77 · see citing works
Self-citationDownregulation of SIK2 expression promotes the melanogenic program in mice
Horike, N., Kumagai, A., Shimono, Y., Onishi, T., Itoh, Y., Sasaki, T., Kitagawa, K., Hatano, O., Takagi, H., Susumu, T., et al. (2010) · Pigment Cell & Melanoma Research · doi:10.1111/j.1755-148x.2010.00760.x · Cited by 76 · see citing works
Self-citationThe AMP-activated protein kinase: more than an energy sensor
Hue, L., & Rider, M. H. (2007) · Essays in Biochemistry · doi:10.1042/bse0430121 · Cited by 74 · see citing works
Zheng, Y., Zhang, W., Pendleton, E., Leng, S.-H., Wu, J., Chen, R., & Sun, X. (2009) · Journal of Endocrinology · doi:10.1677/joe-09-0181 · Cited by 73 · see citing works
Self-citationIRS‐1 Regulation in Health and Disease
Schmitz‐Peiffer, C., & Whitehead, J. P. (2003) · IUBMB Life · doi:10.1080/1521654031000138569 · Cited by 73 · see citing works
The AMPK-related kinase SIK2 is regulated by cAMP via phosphorylation at Ser358 in adipocytes
Henriksson, E., Jones, H. A., Patel, K., Peggie, M. W., Morrice, N. A., Sakamoto, K., & Göransson, O. (2012) · Biochemical Journal · doi:10.1042/bj20111932 · Cited by 68 · see citing works
TORC‐SIK cascade regulates CREB activity through the basic leucine zipper domain
Takemori, H., Kajimura, J., & Okamoto, M. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.05889.x · Cited by 67 · see citing works
Self-citationWeigert, C., Kron, M., Kalbacher, H., Pohl, A. K., Runge, H., Häring, H., Schleicher, E. D., & Lehmann, R. (2008) · Molecular Endocrinology · doi:10.1210/me.2008-0102 · Cited by 66 · see citing works
Inactivation of HDAC5 by SIK1 in AICAR-treated C2C12 Myoblasts
Takemori, H., HASHIMOTO, Y. K., Nakae, J., Olson, E. N., & Okamoto, M. (2009) · Endocrine Journal · doi:10.1507/endocrj.k08e-173 · Cited by 66 · see citing works
Self-citationProtein kinase A suppresses the differentiation of 3T3-L1 preadipocytes
Li, F., Wang, D., Zhou, Y., Zhou, B. O., Yang, Y., Chen, H., & Song, J. (2008) · Cell Research · doi:10.1038/cr.2008.12 · Cited by 64 · see citing works
Intracellular sodium sensing: SIK1 network, hormone action and high blood pressure
Jaitovich, A., & Bertorello, A. M. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2010.03.009 · Cited by 61 · see citing works
Salt-Inducible Kinase 2 Regulates Mitotic Progression and Transcription in Prostate Cancer
Bon, H., Wadhwa, K., Schreiner, A., Osborne, M., Carroll, T. D., Ramos‐Montoya, A., Ross‐Adams, H., Visser, M., Hoffmann, R., Ahmed, A. A., et al. (2014) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-13-0182-t · Cited by 60 · see citing works
Paulo, E., Wu, D., Wang, Y., Zhang, Y., Wu, Y., Swaney, D. L., Soucheray, M., Jimenez-Morales, D., Chawla, A., Krogan, N. J., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-29333-6 · Cited by 59 · see citing works
The multiple roles of salt-inducible kinases in regulating physiology
Jagannath, A., Taylor, L., Ru, Y., Wakaf, Z., Akpobaro, K., Vasudevan, S. R., & Foster, F. (2023) · Physiological Reviews · doi:10.1152/physrev.00023.2022 · Cited by 59 · see citing works
Skeletal muscle salt inducible kinase 1 promotes insulin resistance in obesity
Nixon, M., Stewart-Fitzgibbon, R., Fu, J., Akhmedov, D., Rajendran, K., Mendoza‐Rodriguez, M. G., Rivera-Molina, Y. A., Gibson, M., Berglund, E. D., Justice, N. J., et al. (2015) · Molecular Metabolism · doi:10.1016/j.molmet.2015.10.004 · Cited by 57 · see citing works
Chapter 13 Phosphorylation of IRS Proteins
Sun, X., & Liu, F. (2009) · Vitamins and hormones · doi:10.1016/s0083-6729(08)00613-4 · Cited by 56 · see citing works
Self-citationHashimoto, Y. K., Satoh, T., Okamoto, M., & Takemori, H. (2008) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21737 · Cited by 56 · see citing works
Self-citationKim, J.-Y., Jo, K.-J., Kim, O., Kim, B.-J., Kang, D., Lee, K., Baik, H., Han, M. S., & Lee, S. (2010) · Life Sciences · doi:10.1016/j.lfs.2010.07.009 · Cited by 54 · see citing works
Reversible Acetylation Regulates Salt-inducible Kinase (SIK2) and Its Function in Autophagy*
Yang, F.-C., Tan, B. C., Chen, W.-H., Lin, Y.-H., Huang, J.-Y., Chang, H.-Y., Sun, H.-Y., Hsu, P., Liou, G., Shen, J., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.431239 · Cited by 55 · see citing works
Muraoka, M., Fukushima, A., Viengchareun, S., Lombès, M., Kishi, F., Miyauchi, A., Kanematsu, M., Doi, J., Kajimura, J., Nakai, R., et al. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00024.2009 · Cited by 54 · see citing works
Self-citationOsteocalcin triggers Fas/FasL-mediated necroptosis in adipocytes via activation of p300
Otani, T., Matsuda, M., Mizokami, A., Kitagawa, N., Takeuchi, H., Jimi, E., Inai, T., & Hirata, M. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-1257-7 · Cited by 54 · see citing works
Salt-Inducible Kinase 2: An Oncogenic Signal Transmitter and Potential Target for Cancer Therapy
Chen, F., Chen, L., Qin, Q., & Sun, X. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.00018 · Cited by 53 · see citing works
Self-citationSalt-inducible Kinase 3 Signaling Is Important for the Gluconeogenic Programs in Mouse Hepatocytes
Itoh, Y., Sanosaka, M., Fuchino, H., Yahara, Y., Kumagai, A., Takemoto, D., Kagawa, M., Doi, J., Ohta, M., Tsumaki, N., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.640821 · Cited by 52 · see citing works
Self-citationDu, J., Qiu, C., Takemori, H., & Xu, H. (2008) · Obesity · doi:10.1038/oby.2007.98 · Cited by 51 · see citing works
Self-citationWeigert, C., Hennige, A. M., Brischmann, T., Beck, A., Moeschel, K., Schaüble, M., Brodbeck, K., Häring, H.-U., Schleicher, E. D., & Lehmann, R. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506134200 · Cited by 50 · see citing works
Uebi, T., Tamura, M., Horike, N., Hashimoto, Y. K., & Takemori, H. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00525.2009 · Cited by 48 · see citing works
Self-citationChapter 12 Serine Kinases of Insulin Receptor Substrate Proteins
Boura‐Halfon, S., & Zick, Y. (2009) · Vitamins and hormones · doi:10.1016/s0083-6729(08)00612-2 · Cited by 46 · see citing works
Salt Induces Adipogenesis/Lipogenesis and Inflammatory Adipocytokines Secretion in Adipocytes
Lee, M., Sorn, S. R., Lee, Y., & Kang, I. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20010160 · Cited by 46 · see citing works
The diverse oncogenic and tumor suppressor roles of salt-inducible kinase (SIK) in cancer
Du, W., Zheng, J., & Pei, D. (2015) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2016.1101452 · Cited by 45 · see citing works
Characterization of an Alternative Splice Variant of LKB1
Denison, F. C., Hiscock, N. J., Carling, D., & Woods, A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806153200 · Cited by 44 · see citing works
Charoenfuprasert, S., Yang, Y.-Y., Lee, Y.-C., Chao, K.-C., Chu, P.-Y., Lai, C.-R., Hsu, K.-F., Chang, K.-C., Chen, Y.-C., Chen, L.-T., et al. (2011) · Oncogene · doi:10.1038/onc.2011.77 · Cited by 45 · see citing works
Egawa, T., Tsuda, S., Ma, X., Hamada, T., & Hayashi, T. (2011) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00249.2011 · Cited by 45 · see citing works
Induction of melanogenesis by 4′-O-methylated flavonoids in B16F10 melanoma cells
Horibe, I., Satoh, Y., Shiota, Y., Kumagai, A., Horike, N., Takemori, H., Uesato, S., Sugie, S., Obata, K., Kawahara, H., et al. (2012) · Journal of Natural Medicines · doi:10.1007/s11418-012-0727-y · Cited by 43 · see citing works
Self-citationKim, M.-J., Park, S.-K., Lee, J., Jung, C.-Y., Sung, D. J., Park, J.-H., Yoon, Y.-S., Park, J., Park, K., Song, D., et al. (2015) · Diabetes · doi:10.2337/db14-1240 · Cited by 42 · see citing works
Säll, J., Pettersson, A. M. L., Björk, C., Henriksson, E., Wasserström, S., Linder, W., Zhou, Y., Hansson, O., Andersson, D. P., Ekelund, M., et al. (2016) · Diabetologia · doi:10.1007/s00125-016-4141-y · Cited by 42 · see citing works
Loss of the conserved PKA sites of SIK1 and SIK2 increases sleep need
Park, M., Miyoshi, C., Fujiyama, T., Kakizaki, M., Ikkyu, A., Honda, T., Choi, J., Asano, F., Mizuno, S., Takahashi, S., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-65647-0 · Cited by 42 · see citing works
Inazuka, F., Sugiyama, N., Tomita, M., Abe, T., Shioi, G., & Esumi, H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.302687 · Cited by 42 · see citing works
Negative regulation of adipogenesis from human mesenchymal stem cells by Jun N-terminal kinase
Tominaga, S., Yamaguchi, T., Takahashi, S., Hirose, F., & Osumi, T. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.11.056 · Cited by 41 · see citing works
Hoffmann, B. R., El‐Mansy, M. F., Sem, D. S., & Greene, A. S. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm301204r · Cited by 41 · see citing works
Kumagai, A., Horike, N., Satoh, Y., Uebi, T., Sasaki, T., Itoh, Y., Hirata, Y., Uchio‐Yamada, K., Kitagawa, K., Uesato, S., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026148 · Cited by 39 · see citing works
Self-citationIn vivo, ex vivo, and in vitro studies on apelin's effect on myocardial glucose uptake
Xu, S., Han, P., Huang, M., Wu, J. C., Chang, C.-P., Tsao, P. S., & Yue, P. (2012) · Peptides · doi:10.1016/j.peptides.2012.08.004 · Cited by 38 · see citing works
C. elegans serine-threonine kinase KIN-29 modulates TGFβ signaling and regulates body size formation
Maduzia, L. L., Roberts, A. F., Wang, H., Lin, X., Chin, L. J., Zimmerman, C. M., Cohen, S., Feng, X., & Padgett, R. W. (2005) · BMC Developmental Biology · doi:10.1186/1471-213x-5-8 · Cited by 30 · see citing works
AMPKα-like proteins as LKB1 downstream targets in cell physiology and cancer
Molina, E., Hong, L., & Chefetz, I. (2021) · Journal of Molecular Medicine · doi:10.1007/s00109-021-02040-y · Cited by 28 · see citing works
Zohrap, N., Saatci, Ö., Özeş, B., Çoban, İ., Atay, H. M., Battaloğlu, E., Şahin, Ö., & Buğra, K. (2018) · Oncotarget · doi:10.18632/oncotarget.25082 · Cited by 28 · see citing works
Kim, J.-Y., Jo, K.-J., Kim, B.-J., Baik, H., & Lee, S. (2012) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2012.1070 · Cited by 27 · see citing works
He, C., Zhao, X., Lei, Y., Nie, J., Lu, X., Song, J., Wang, L., Li, H., Liu, F., Zhang, Y., et al. (2021) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2021.11.010 · Cited by 26 · see citing works
Meerzaman, D. M., Yan, C., Chen, Q., Edmonson, M. N., Schaefer, C. F., Clifford, R., Dunn, B. K., Dong, L., Finney, R. P., Cultraro, C. M., et al. (2014) · PubMed · Cited by 24 · see citing works
Role of Salt-Inducible Kinase 1 in the Activation of MEF2-Dependent Transcription by BDNF
Finsterwald, C., Carrard, A., & Martin, J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0054545 · Cited by 23 · see citing works
Raab, M., Rak, M., Tesch, R., Gasimli, K., Becker, S., Knapp, S., Strebhardt, K., & Sanhaji, M. (2021) · Cancers · doi:10.3390/cancers13153658 · Cited by 22 · see citing works
Popov, S., Takemori, H., Tokudome, T., Mao, Y., Otani, K., Mochizuki, N., Pires, N. M., Pinho, M. J., Franco‐Cereceda, A., Torielli, L., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0095771 · Cited by 22 · see citing works
Self-citationJin, H. Y., Tudor, Y., Choi, K., Shao, Z., Sparling, B. A., McGivern, J. G., & Symons, A. (2019) · SLAS DISCOVERY · doi:10.1177/2472555219893277 · Cited by 20 · see citing works
Shi, F., Silva, F. D. F., Liu, D., Patel, H. U., Xu, J. T., Zhang, W., Türk, C., Krüger, M., & Collins, S. (2023) · Molecular Metabolism · doi:10.1016/j.molmet.2023.101753 · Cited by 20 · see citing works
Abali, G. K., Özcan, F., Uğurlu, A., Uysal, A., Fuss, S. H., & Bugra–Bilge, K. (2013) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.12-10729 · Cited by 20 · see citing works
- Authors
- Horike, N., Takemori, H., Katoh, Y., Doi, J., Min, L., Asano, T., Sun, X. J., Yamamoto, H., Kasayama, S., Muraoka, M., Nonaka, Y., & Okamoto, M.
- Affiliations
- The University of Osaka (JP)
- Senri Kinran University (JP)
- The University of Tokyo (JP)
- University of Vermont (US)
- Koshien University (JP)
- Corresponding author
- Okamoto, Mitsuhiro
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-05
- Volume
- 278
- Issue
- 20
- Pages
- 18440-18447
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2168780144
- Cited by
- 161
- References
- 48
- Citations by year
- 2026: 4 · 2025: 7 · 2024: 7 · 2023: 11 · 2022: 4 · 2021: 11 · 2020: 5 · 2019: 4 · 2018: 7 · 2017: 1 · 2016: 4 · 2015: 7 · 2014: 9 · 2013: 8 · 2012: 12
- FWCI
- 2.41
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Dartmouth College
- Uehara Memorial Foundation (CREST)
- Salt Science Research Foundation
- Japan Society for the Promotion of Science (CREST)
- Core Research for Evolutional Science and Technology
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Health Sciences › Medicine › Epidemiology › Adipokines, Inflammation, and Metabolic Diseases
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Keywords
- SIK2, IRS-1, adipose tissue, adipogenesis, C/EBPβ, insulin resistance, type 2 diabetes, db/db mice, insulin signaling
- MeSH terms
- Cyclic AMP, Adipose Tissue, Amino Acid Sequence, Animals, Cell Differentiation, Cell Line, Cloning, Molecular, Escherichia coli, Humans, Insulin Resistance, Male, Mice, Inbred C57BL, Molecular Sequence Data, Phosphoproteins, Phosphorylation, Plasmids, Precipitin Tests, RNA, Messenger, Serine, Tissue Distribution, Blotting, Northern, 3T3 Cells, Protein Serine-Threonine Kinases, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Adipocytes, DNA, Complementary, COS Cells, Protein Isoforms, Mice, Insulin Receptor Substrate Proteins
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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