Adipose-specific Expression, Phosphorylation of Ser794 in Insulin Receptor Substrate-1, and Activation in Diabetic Animals of Salt-inducible Kinase-2

Insulin 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

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

The c-Jun NH2-terminal kinase promotes insulin resistance during association with insulin receptor substrate-1 and phosphorylation of Ser307

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

Disordered Fat Storage and Mobilization in the Pathogenesis of Insulin Resistance and Type 2 Diabetes

Lewis, G. F., Carpentier, A. C., Adeli, K., & Giacca, A. (2002) · Endocrine Reviews · doi:10.1210/edrv.23.2.0461 · Cited by 1,370

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 1,178

Cascade regulation of terminal adipocyte differentiation by three members of the C/EBP family of leucine zipper proteins.Preprint

Yeh, W., Cao, Z. D., Classon, M., & McKnight, S. L. (1995) · Genes & Development · doi:10.1101/gad.9.2.168 · Cited by 926

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 688

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

Insulin/IGF-1 and TNF-α stimulate phosphorylation of IRS-1 at inhibitory Ser307 via distinct pathways

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 611

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

Regulation of insulin sensitivity by serine/threonine phosphorylation of insulin receptor substrate proteins IRS1 and IRS2.

Copps, K. D., & White, M. F. (2012) · Diabetologia · doi:10.1007/s00125-012-2644-8 · Cited by 1,017

Positive 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

Molecular mechanisms of insulin resistance in humans and their potential links with mitochondrial dysfunction

Morino, K., Petersen, K. F., & Shulman, G. I. (2006) · Diabetes · doi:10.2337/db06-s002 · Cited by 853

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 805

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

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

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 369

Salt-inducible kinase 2 links transcriptional coactivator p300 phosphorylation to the prevention of ChREBP-dependent hepatic steatosis in mice

Bricambert, J., Miranda, J., Benhamed, F., Girard, J. R., Postic, C., & Dentin, R. (2010) · Journal of Clinical Investigation · doi:10.1172/jci41624 · Cited by 318

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

Modulation of insulin action

Pirola, L., Johnston, A., & OBBERGHEN, E. V. (2004) · Diabetologia · doi:10.1007/s00125-003-1313-3 · Cited by 286

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 257

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

PGE2 Induces Macrophage IL-10 Production and a Regulatory-like Phenotype via a Protein Kinase A–SIK–CRTC3 Pathway

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 252

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 208

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

Activation 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

Salt-Inducible Kinase 2 Couples Ovarian Cancer Cell Metabolism with Survival at the Adipocyte-Rich Metastatic Niche

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

The LKB1-salt-inducible kinase pathway functions as a key gluconeogenic suppressor in the liver

Patel, K., 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 171

LKB1, Salt-Inducible Kinases, and MEF2C Are Linked Dependencies in Acute Myeloid Leukemia

Tarumoto, Y., Lu, B., Somerville, T. D. D., Huang, Y., Milazzo, J. P., Wu, X., Klingbeil, O., Demerdash, O. E., Shi, J., & Vakoc, C. R. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.02.011 · Cited by 154

Insulin-Like Growth Factor-I Stimulates Both Cell Growth and Lipogenesis during Differentiation of Human Mesenchymal Stem Cells into Adipocytes

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

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

Energy Depletion Inhibits Phosphatidylinositol 3-Kinase/Akt Signaling and Induces Apoptosis via AMP-activated Protein Kinase-dependent Phosphorylation of IRS-1 at Ser-794

Tzatsos, A., & Tsichlis, P. N. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610101200 · Cited by 140

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 132

Nuts and bolts of the salt-inducible kinases (SIKs)

Darling, N. J., & Cohen, P. (2021) · Biochemical Journal · doi:10.1042/bcj20200502 · Cited by 134

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 121

Phosphorylation of the insulin receptor by AMP-activated protein kinase (AMPK) promotes ligand-independent activation of the insulin signalling pathway in rodent muscle

Chopra, I., Li, H. F., Wang, H., & Webster, K. A. (2012) · Diabetologia · doi:10.1007/s00125-011-2407-y · Cited by 116

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 113

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 109

Insulin and Metabolic Stress Stimulate Multisite Serine/Threonine Phosphorylation of Insulin Receptor Substrate 1 and Inhibit Tyrosine Phosphorylation

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 120

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 103

Antioxidants: do they have a role in the treatment of insulin resistance?

Evans, J. L. (2007) · PubMed · Cited by 99

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 97

The Tumor Suppressor Kinase LKB1 Activates the Downstream Kinases SIK2 and SIK3 to Stimulate Nuclear Export of Class IIa Histone Deacetylases

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 96

SIK1 is part of a cell sodium-sensing network that regulates active sodium transport through a calcium-dependent process

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

Salt-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 88

AMP-Activated Protein Kinase Inhibits IGF-I Signaling and Protein Synthesis in Vascular Smooth Muscle Cells via Stimulation of Insulin Receptor Substrate 1 S794 and Tuberous Sclerosis 2 S1345 Phosphorylation

Ning, J., & Clemmons, D. R. (2010) · Molecular Endocrinology · doi:10.1210/me.2009-0474 · Cited by 89

Inhibition of SIK2 and SIK3 during differentiation enhances the anti-inflammatory phenotype of macrophages

Darling, N. J., Toth, R. L., Arthur, J. S. C., & Clark, K. (2016) · Biochemical Journal · doi:10.1042/bcj20160646 · Cited by 89

KIN‐29 SIK regulates chemoreceptor gene expression via an MEF2 transcription factor and a class II HDAC

van der Linden, A. M., Nolan, K. M., & Sengupta, P. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601479 · Cited by 87

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 85

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

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

Salt-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 87

AMPK-induced activation of Akt by AICAR is mediated by IGF-1R dependent and independent mechanisms in acute lymphoblastic leukemia

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 87

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 84

Aquatic Adaptation and Depleted Diversity: A Deep Dive into the Genomes of the Sea Otter and Giant Otter

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 80

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

Salt‐inducible kinase‐1 represses cAMP response element‐binding protein activity both in the nucleus and in the cytoplasm

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

Downregulation 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 78

The AMP-activated protein kinase: more than an energy sensor

Hue, L., & Rider, M. H. (2007) · Essays in Biochemistry · doi:10.1042/bse0430121 · Cited by 75

Improved insulin sensitivity by calorie restriction is associated with reduction of ERK and p70S6K activities in the liver of obese Zucker rats

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 74

IRS‐1 Regulation in Health and Disease

Schmitz‐Peiffer, C., & Whitehead, J. P. (2003) · IUBMB Life · doi:10.1080/1521654031000138569 · Cited by 78

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 69

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 66

Interplay and Effects of Temporal Changes in the Phosphorylation State of Serine-302, -307, and -318 of Insulin Receptor Substrate-1 on Insulin Action in Skeletal Muscle Cells

Weigert, 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 68

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 67

Protein 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 65

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

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

Sympathetic inputs regulate adaptive thermogenesis in brown adipose tissue through cAMP-Salt inducible kinase axis

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

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 64

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

Chapter 13 Phosphorylation of IRS Proteins

Sun, X., & Liu, F. (2009) · Vitamins and hormones · doi:10.1016/s0083-6729(08)00613-4 · Cited by 57

Importance of autophosphorylation at Ser186 in the A‐loop of salt inducible kinase 1 for its sustained kinase activity

Hashimoto, Y. K., Satoh, T., Okamoto, M., & Takemori, H. (2008) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21737 · Cited by 57

Parenteral 17beta-estradiol decreases fasting blood glucose levels in non-obese mice with short-term ovariectomy

Kim, 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 55

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

Involvement of SIK2/TORC2 signaling cascade in the regulation of insulin-induced PGC-1 α and UCP-1 gene expression in brown adipocytes

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 56

Osteocalcin 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 55

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

Salt-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 51

SIK2 Can be Activated by Deprivation of Nutrition and It Inhibits Expression of Lipogenic Genes in Adipocytes

Du, J., Qiu, C., Takemori, H., & Xu, H. (2008) · Obesity · doi:10.1038/oby.2007.98 · Cited by 51

The Phosphorylation of Ser318 of Insulin Receptor Substrate 1 Is Not per se Inhibitory in Skeletal Muscle Cells but Is Necessary to Trigger the Attenuation of the Insulin-stimulated Signal

Weigert, 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

Phosphorylation of the CREB-specific coactivator TORC2 at Ser307 regulates its intracellular localization in COS-7 cells and in the mouse liver

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

Chapter 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 53

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

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

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 52

Identification of salt-inducible kinase 3 as a novel tumor antigen associated with tumorigenesis of ovarian cancer

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

Caffeine modulates phosphorylation of insulin receptor substrate-1 and impairs insulin signal transduction in rat skeletal muscle

Egawa, T., Tsuda, S., Ma, X., Hamada, T., & Hayashi, T. (2011) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00249.2011 · Cited by 46

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

Salt-Inducible Kinase 1 Terminates cAMP Signaling by an Evolutionarily Conserved Negative-Feedback Loop in β-Cells

Kim, 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

Salt-inducible kinase 2 and -3 are downregulated in adipose tissue from obese or insulin-resistant individuals: implications for insulin signalling and glucose uptake in human adipocytes

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

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

Muscle-specific Knock-out of NUAK Family SNF1-like Kinase 1 (NUAK1) Prevents High Fat Diet-induced Glucose Intolerance

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 43

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

Chemical Proteomics-Based Analysis of Off-Target Binding Profiles for Rosiglitazone and Pioglitazone: Clues for Assessing Potential for Cardiotoxicity

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

A Potent Inhibitor of SIK2, 3, 3′, 7-Trihydroxy-4′-Methoxyflavon (4′-O-Methylfisetin), Promotes Melanogenesis in B16F10 Melanoma Cells

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

In 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 40

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

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 29

SIK2 attenuates proliferation and survival of breast cancer cells with simultaneous perturbation of MAPK and PI3K/Akt pathways

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

17β-estradiol induces an interaction between adenosine monophosphate-activated protein kinase and the insulin signaling pathway in 3T3-L1 adipocytes

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

Whole-transcriptome analysis of aluminum-exposed rat hippocampus and identification of ceRNA networks to investigate neurotoxicity of Al

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

Genome-wide transcriptional sequencing identifies novel mutations in metabolic genes in human hepatocellular carcinoma.

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

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

The Small-Molecule Inhibitor MRIA9 Reveals Novel Insights into the Cell Cycle Roles of SIK2 in Ovarian Cancer Cells

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

Lack of Salt-Inducible Kinase 2 (SIK2) Prevents the Development of Cardiac Hypertrophy in Response to Chronic High-Salt Intake

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

High-Throughput Implementation of the NanoBRET Target Engagement Intracellular Kinase Assay to Reveal Differential Compound Engagement by SIK2/3 Isoforms

Jin, 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

Salt-inducible kinase inhibition promotes the adipocyte thermogenic program and adipose tissue browning

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

SIK2 Is Involved in the Negative Modulation of Insulin-Dependent Müller Cell Survival and Implicated in Hyperglycemia-Induced Cell Death

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

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 103

Insulin induces Thr484 phosphorylation and stabilization of SIK2 in adipocytes

Säll, J., Negoita, F., Hansson, B., Kopietz, F., Linder, W., Pettersson, A. M. L., Ekelund, M., Laurencikiene, J., Degerman, E., Stenkula, K. G., et al. (2018) · Cellular Signalling · doi:10.1016/j.cellsig.2018.12.011 · Cited by 5

Salt‐inducible kinases are required for glucose uptake and insulin signaling in human adipocytes

Säll, J., Lindahl, M., Fritzen, A. M., Fryklund, C., Kopietz, F., Nyberg, E., Warvsten, A., Morén, B., Foretz, M., Kiens, B., et al. (2023) · Obesity · doi:10.1002/oby.23858 · Cited by 5

Salt-inducible kinases in adipose tissue

Säll, J. (2017) · Lund University Publications (Lund University)

Salt-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 88