Growth differentiation factor 15 is a myomitokine governing systemic energy homeostasis
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Reduced mitochondrial electron transport chain activity promotes longevity and improves energy homeostasis via cell-autonomous and –non-autonomous factors in multiple model systems. This mitohormetic effect is thought to involve the mitochondrial unfolded protein response (UPRmt), an adaptive stress-response pathway activated by mitochondrial proteotoxic stress. Using mice with skeletal muscle–specific deficiency of Crif1 (muscle-specific knockout [MKO]), an integral protein of the large mitoribosomal subunit (39S), we identified growth differentiation factor 15 (GDF15) as a UPRmt-associated cell–non-autonomous myomitokine that regulates systemic energy homeostasis. MKO mice were protected against obesity and sensitized to insulin, an effect associated with elevated GDF15 secretion after UPRmt activation. In ob/ob mice, administration of recombinant GDF15 decreased body weight and improved insulin sensitivity, which was attributed to elevated oxidative metabolism and lipid mobilization in the liver, muscle, and adipose tissue. Thus, GDF15 is a potent mitohormetic signal that safeguards against the onset of obesity and insulin resistance.
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Experimental and clinical data support a role for GDF15 in regulating body weight and energy homeostasis.
“Experimental and clinical data have supported its role in regulating body weight and energy homeostasis [[210], [211], [212], [213]] (Figure 2).”
From Hepatokines and metabolism: Deciphering communication from the liver (2021) · cites this paper as [210]
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Subramanian, A., Tamayo, P., Mootha, V. K., Mukherjee, S., Ebert, B. L., Gillette, M. A., Paulovich, A., Pomeroy, S. L., Golub, T. R., Lander, E. S., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506580102 · Cited by 53,625 · see citing works
Trapnell, C., Williams, B. A., Pertea, G., Mortazavi, A., Kwan, G., van Baren, M. J., Salzberg, S. L., Wold, B. J., & Pachter, L. (2010) · Nature Biotechnology · doi:10.1038/nbt.1621 · Cited by 15,556 · see citing works
TopHat: discovering splice junctions with RNA-Seq
Trapnell, C., Pachter, L. S., & Salzberg, S. L. (2009) · Bioinformatics · doi:10.1093/bioinformatics/btp120 · Cited by 11,477 · see citing works
Mitochondria: In Sickness and in Health
Nunnari, J., & Suomalainen, A. (2012) · Cell · doi:10.1016/j.cell.2012.02.035 · Cited by 3,479 · see citing works
Watterson, K. R., Bestow, D., Gallagher, J. R., Hamilton, D. L., Ashford, F. B., Meakin, P. J., & Ashford, M. L. J. (2012) · Neurosignals · doi:10.1159/000334144 · Cited by 3,395 · see citing works
Premature ageing in mice expressing defective mitochondrial DNA polymerase
Trifunovic, A., Wredenberg, A., Falkenberg, M., Spelbrink, J. N., Rovio, A. T., Bruder, C. E., Bohlooly-Y, M., Gidlöf, S., Oldfors, A., Wibom, R., et al. (2004) · Nature · doi:10.1038/nature02517 · Cited by 2,734 · see citing works
Mitochondrial dysfunction in the elderly: possible role in insulin resistance
Petersen, K. F., Befroy, D., Dufour, S., Dziura, J., Ariyan, C., Rothman, D. L., DiPietro, L., Cline, G. W., & Shulman, G. I. (2003) · Science · doi:10.1126/science.1082889 · Cited by 2,107 · see citing works
AMP-Activated Protein Kinase in Metabolic Control and Insulin Signaling
Towler, M. C., & Hardie, D. G. (2007) · Circulation Research · doi:10.1161/01.res.0000256090.42690.05 · Cited by 1,247 · see citing works
MIC-1, a novel macrophage inhibitory cytokine, is a divergent member of the TGF-β superfamily
Bootcov, M. R., Bauskin, A. R., Valenzuela, S. M., Moore, A. G., Bansal, M., He, X. Y., Zhang, H. P., Donnellan, M., Mahler, S. M., Pryor, K., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.21.11514 · Cited by 1,180 · see citing works
Rates of Behavior and Aging Specified by Mitochondrial Function During Development
Dillin, A., Hsu, A.-L., Arantes-Oliveira, N., Lehrer-Graiwer, J., Hsin, H., Fraser, A. G., Kamath, R. S., Ahringer, J., & Kenyon, C. (2002) · Science · doi:10.1126/science.1077780 · Cited by 1,121 · see citing works
The Cell Non-Autonomous Nature of Electron Transport Chain-Mediated Longevity
Durieux, J., Wolff, S., & Dillin, A. (2011) · Cell · doi:10.1016/j.cell.2010.12.016 · Cited by 1,059 · see citing works
Mitonuclear protein imbalance as a conserved longevity mechanism
Houtkooper, R. H., Mouchiroud, L., Ryu, D., Moullan, N., Katsyuba, E., Knott, G., Williams, R. W., & Auwerx, J. (2013) · Nature · doi:10.1038/nature12188 · Cited by 1,035 · see citing works
Self-citationA mitochondrial specific stress response in mammalian cells
Zhao, Q., Wang, J., Levichkin, I. V., Stasinopoulos, S., Ryan, M. T., & Hoogenraad, N. J. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf445 · Cited by 1,026 · see citing works
Wang, X., & Ron, D. (1996) · Science · doi:10.1126/science.272.5266.1347 · Cited by 885 · see citing works
Morino, K., Petersen, K. F., & Shulman, G. I. (2006) · Diabetes · doi:10.2337/db06-s002 · Cited by 853 · see citing works
Kim, K. H., Jeong, Y. T., Oh, H., Kim, S. H., Cho, J. M., Kim, Y.-N., Kim, S. S., Kim, D. H., Hur, K. Y., Kim, H. K., et al. (2013) · Nature Medicine · doi:10.1038/nm.3014 · Cited by 774 · see citing works
Self-citationMitochondrial Electron Transport Is a Key Determinant of Life Span in Caenorhabditis elegans
Feng, J., Bussière, F., & Hekimi, S. (2001) · Developmental Cell · doi:10.1016/s1534-5807(01)00071-5 · Cited by 675 · see citing works
Kempf, T., Eden, M., Strelau, J., Naguib, M., Willenbockel, C., Tongers, J., Heineke, J., Kotlarz, D., Xu, J., Molkentin, J. D., et al. (2006) · Circulation Research · doi:10.1161/01.res.0000202805.73038.48 · Cited by 651 · see citing works
Rebbapragada, A., Benchabane, H., Wrana, J. L., Celeste, A. J., & Attisano, L. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.20.7230-7242.2003 · Cited by 566 · see citing works
New roles for mitochondrial proteases in health, ageing and disease
Quirós, P. M., Langer, T., & López-Otı́n, C. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3984 · Cited by 546 · see citing works
Kempf, T., Zarbock, A., Widera, C., Butz, S., Stadtmann, A., Rossaint, J., Bolomini-Vittori, M., Korf-Klingebiel, M., Napp, L. C., Hansen, B., et al. (2011) · Nature Medicine · doi:10.1038/nm.2354 · Cited by 518 · see citing works
Xu, J., Kimball, T. R., Lorenz, J. N., Brown, D. A., Bauskin, A. R., Klevitsky, R., Hewett, T. E., Breit, S. N., & Molkentin, J. D. (2006) · Circulation Research · doi:10.1161/01.res.0000202804.84885.d0 · Cited by 507 · see citing works
Nargund, A. M., Fiorese, C. J., Pellegrino, M. W., Deng, P., & Haynes, C. M. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.02.008 · Cited by 463 · see citing works
Suomalainen, A., Elo, J. M., Pietiläinen, K. H., Hakonen, A. H., Sevastianova, K., Korpela, M., Isohanni, P., Marjavaara, S. K., Tyni, T., Kiuru-Enari, S., et al. (2011) · The Lancet Neurology · doi:10.1016/s1474-4422(11)70155-7 · Cited by 427 · see citing works
Pospisilik, J. A., Knauf, C., Joza, N., Benit, P., Orthofer, M., Cani, P. D., Ebersberger, I., Nakashima, T., Sarao, R., Neely, G., et al. (2007) · Cell · doi:10.1016/j.cell.2007.08.047 · Cited by 404 · see citing works
Muscle Mitohormesis Promotes Longevity via Systemic Repression of Insulin Signaling
Owusu-Ansah, E., Song, W., & Perrimon, N. (2013) · Cell · doi:10.1016/j.cell.2013.09.021 · Cited by 395 · see citing works
The complete structure of the 55 S mammalian mitochondrial ribosome
Greber, B. J., Bieri, P., Leibundgut, M., Leitner, A., Aebersold, R. H., Boehringer, D., & Ban, N. (2015) · Science · doi:10.1126/science.aaa3872 · Cited by 395 · see citing works
Mitochondrial UPR-regulated innate immunity provides resistance to pathogen infection
Pellegrino, M. W., Nargund, A. M., Kirienko, N. V., Gillis, R., Fiorese, C. J., & Haynes, C. M. (2014) · Nature · doi:10.1038/nature13818 · Cited by 369 · see citing works
Mitochondrial myopathy induces a starvation-like response
Tyynismaa, H., Carroll, C. J., Raimundo, N., Ahola-Erkkilä, S., Wenz, T., Ruhanen, H., Guse, K., Hemminki, A., Peltola-Mjøsund, K. E., Tulkki, V., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq310 · Cited by 300 · see citing works
Niclosamide ethanolamine–induced mild mitochondrial uncoupling improves diabetic symptoms in mice
Tao, H., Zhang, Y., Zeng, X., Shulman, G. I., & Jin, S. (2014) · Nature Medicine · doi:10.1038/nm.3699 · Cited by 288 · see citing works
Controlled-release mitochondrial protonophore reverses diabetes and steatohepatitis in rats
Perry, R. J., Zhang, D., Zhang, X.-M., Boyer, J. L., & Shulman, G. I. (2015) · Science · doi:10.1126/science.aaa0672 · Cited by 283 · see citing works
A SIRT7-Dependent Acetylation Switch of GABPβ1 Controls Mitochondrial Function
Ryu, D., Jo, Y. S., Sasso, G. L., Stein, S., Zhang, H., Perino, A., Lee, J. U., Zeviani, M., Romand, R., Hottiger, M. O., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.08.001 · Cited by 258 · see citing works
Self-citationThe complete structure of the large subunit of the mammalian mitochondrial ribosome
Greber, B. J., Boehringer, D., Leibundgut, M., Bieri, P., Leitner, A., Schmitz, N., Aebersold, R. H., & Ban, N. (2014) · Nature · doi:10.1038/nature13895 · Cited by 257 · see citing works
Multilayered Genetic and Omics Dissection of Mitochondrial Activity in a Mouse Reference Population
Wu, Y., Williams, E. G., Dubuis, S., Mottis, A., Jovaisaite, V., Houten, S. M., Argmann, C. A., Faridi, P., Wolski, W., Kutalik, Z., et al. (2014) · Cell · doi:10.1016/j.cell.2014.07.039 · Cited by 244 · see citing works
Self-citationSkeletal muscle mitochondria as a target to prevent or treat type 2 diabetes mellitus
Hesselink, M. K. C., Schrauwen-Hinderling, V., & Schrauwen, P. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2016.104 · Cited by 242 · see citing works
NAG-1/GDF-15 prevents obesity by increasing thermogenesis, lipolysis and oxidative metabolism
Chrysovergis, K., Wang, X., Kosak, J., Lee, S.-H., Kim, J. S., Foley, J. F., Travlos, G., Singh, S., Baek, S. J., & Eling, T. E. (2014) · International Journal of Obesity · doi:10.1038/ijo.2014.27 · Cited by 241 · see citing works
Self-citationPerry, R. J., Kim, T.-H., Zhang, X., Lee, H., Pesta, D. H., Popov, V., Zhang, D., Rahimi, Y., Jurczak, M. J., Cline, G. W., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.10.004 · Cited by 230 · see citing works
Architecture of the large subunit of the mammalian mitochondrial ribosome
Greber, B. J., Boehringer, D., Leitner, A., Bieri, P., Voigts-Hoffmann, F., Erzberger, J. P., Leibundgut, M., Aebersold, R. H., & Ban, N. (2013) · Nature · doi:10.1038/nature12890 · Cited by 225 · see citing works
Andreux, P. A., Williams, E. G., Koutníková, H., Houtkooper, R. H., Champy, M., Henry, H., Schoonjans, K., Williams, R. W., & Auwerx, J. H. (2012) · Cell · doi:10.1016/j.cell.2012.08.012 · Cited by 224 · see citing works
Self-citationDoğan, Ş. A., Pujol, C., Maiti, P., Kukat, A., Wang, S., Hermans, S., Senft, K., Wibom, R., Rugarli, E. I., & Trifunović, A. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.02.004 · Cited by 222 · see citing works
Macia, L., Tsai, V. W.-W., Nguyen, A. D., Johnen, H., Kuffner, T., Shi, Y.-C., Lin, S., Herzog, H., Brown, D. A., Breit, S. N., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0034868 · Cited by 211 · see citing works
Horibe, T., & Hoogenraad, N. J. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000835 · Cited by 209 · see citing works
Pharmacological targeting of endoplasmic reticulum stress signaling in cancer
Schönthal, A. H. (2012) · Biochemical Pharmacology · doi:10.1016/j.bcp.2012.09.012 · Cited by 180 · see citing works
Kempf, T., Guba-Quint, A., Torgerson, J., Magnone, M. C., Haefliger, C., Bobadilla, M., & Wollert, K. C. (2012) · European Journal of Endocrinology · doi:10.1530/eje-12-0466 · Cited by 176 · see citing works
Moisoi, N., Klupsch, K., Fedele, V., East, P., Sharma, S., Renton, A. E., Plun‐Favreau, H., Edwards, R., Teismann, P., Esposti, M. D., et al. (2008) · Cell Death and Differentiation · doi:10.1038/cdd.2008.166 · Cited by 175 · see citing works
CaMKII?-cre transgene expression and recombination patterns in the mouse brain
Dragatsis, I., & Zeitlin, S. O. (2000) · genesis · doi:10.1002/(sici)1526-968x(200002)26:2 · Cited by 171 · see citing works
GDF15, a Cardioprotective TGF-β Superfamily Protein
Ago, T., & Sadoshima, J. (2006) · Circulation Research · doi:10.1161/01.res.0000207919.83894.9d · Cited by 166 · see citing works
Mitochondrial Proteostasis in the Control of Aging and Longevity
Jensen, M. B., & Jasper, H. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.05.006 · Cited by 162 · see citing works
The diverse roles of nonsteroidal anti-inflammatory drug activated gene (NAG-1/GDF15) in cancer
Wang, X., Baek, S. J., & Eling, T. E. (2012) · Biochemical Pharmacology · doi:10.1016/j.bcp.2012.11.025 · Cited by 154 · see citing works
The Role of Mitochondria in the Pathophysiology of Skeletal Muscle Insulin Resistance
Pagel-Langenickel, I., Bao, J., Pang, L., & Sack, M. N. (2010) · Endocrine Reviews · doi:10.1210/er.2009-0003 · Cited by 154 · see citing works
Respiratory chain dysfunction in skeletal muscle does not cause insulin resistance
Wredenberg, A., Freyer, C., Sandström, M. E., Katz, A., Wibom, R., Westerblad, H., & Larsson, N.-G. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.09.029 · Cited by 141 · see citing works
Bernstein, S. H., Venkatesh, S., Li, M., Lee, J., Lü, B., Hilchey, S. P., Morse, K. M., Metcalfe, H. M., Skalska, J., Andreeff, M., et al. (2012) · Blood · doi:10.1182/blood-2011-02-340075 · Cited by 137 · see citing works
Intertissue Control of the Nucleolus via a Myokine-Dependent Longevity Pathway
Demontis, F., Patel, V. K., Swindell, W. R., & Perrimon, N. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.05.001 · Cited by 131 · see citing works
GDF15 is a novel biomarker to evaluate efficacy of pyruvate therapy for mitochondrial diseases
Fujita, Y., Ito, M., Kojima, T., Yatsuga, S., Koga, Y., & Tanaka, M. (2015) · Mitochondrion · doi:10.1016/j.mito.2014.10.006 · Cited by 128 · see citing works
Human cDNA Encoding a Novel TGF- Superfamily Protein Highly Expressed in Placenta
Yokoyama-Kobayashi, M., Saeki, M., Sekine, S., & Kato, S. (1997) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a021798 · Cited by 116 · see citing works
Kim, S. J., Kwon, M.-C., Ryu, M. J., Chung, H. K., Tadi, S., Kim, Y. K., Kim, J. M., Lee, S. E., Park, J. H., Kweon, G. R., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.06.012 · Cited by 115 · see citing works
Self-citationThe General Occurrence of 55 S Ribosomes in Mammalian Liver Mitochondria
O’Brien, T. W. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62239-2 · Cited by 108 · see citing works
hNAG-1 increases lifespan by regulating energy metabolism and insulin/IGF-1/mTOR signaling
Wang, X., Chrysovergis, K., Kosak, J., Kissling, G., Streicker, M., Moser, G., Li, R., & Eling, T. E. (2014) · Aging · doi:10.18632/aging.100687 · Cited by 106 · see citing works
Zheng, X., Zheng, X., Wang, X., Ma, Z., Gupta Sunkari, V, Botusan, I., Takeda, T., Björklund, A., Inoue, M., Catrina, S.-B., et al. (2012) · Cell Death & Disease · doi:10.1038/cddis.2012.66 · Cited by 99 · see citing works
Muscle mitochondrial stress adaptation operates independently of endogenous FGF21 action
Ost, M., Coleman, V., Voigt, A., van Schothorst, E. M., Keipert, S., van der Stelt, I., Ringel, S., Graja, A., Ambrosi, T., Kipp, A. P., et al. (2016) · Molecular Metabolism · doi:10.1016/j.molmet.2015.11.002 · Cited by 75 · see citing works
Mitochondrial Plasticity in Obesity and Diabetes Mellitus
Jeleník, T., & Roden, M. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4910 · Cited by 72 · see citing works
Deficiency of the Mitochondrial Electron Transport Chain in Muscle Does Not Cause Insulin Resistance
Han, D.-H., Hancock, C. R., Jung, S. R., Higashida, K., Kim, S. H., & Holloszy, J. O. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019739 · Cited by 71 · see citing works
Self-citationGDF-15 protects from macrophage accumulation in a mousemodel of advanced atherosclerosis
Preusch, M. R., Baeuerle, M., Albrecht, C., Blessing, E., Bischof, M., Katus, H. A., & Bea, F. (2013) · European journal of medical research · doi:10.1186/2047-783x-18-19 · Cited by 70 · see citing works
Quintens, R., Singh, S., Lemaire, K., Bock, K. D., Granvik, M., Schraenen, A., Vroegrijk, I. O. C. M., Costa, V., Noten, P. V., Lambrechts, D., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056719 · Cited by 69 · see citing works
Growth/differentiation factor-15: prostate cancer suppressor or promoter?
Vaňhara, P., Hampl, A., Kozubı́k, A., & Souček, K. (2012) · Prostate Cancer and Prostatic Diseases · doi:10.1038/pcan.2012.6 · Cited by 67 · see citing works
Crif1 is a novel transcriptional coactivator of STAT3
Kwon, M. C., Koo, B., Moon, J.-S., Kim, Y. Y., Park, K. C., Kim, N.-S., Kwon, M. Y., Kong, M.-P., Yoon, K., Im, S.-K., et al. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601986 · Cited by 66 · see citing works
Self-citationDefects in mitochondrial DNA replication and oxidative damage in muscle of mtDNA mutator mice
Kolesar, J. E., Safdar, A., Abadi, A., MacNeil, L., Crane, J. D., Tarnopolsky, M. A., & Kaufman, B. A. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.07.038 · Cited by 63 · see citing works
High-fat diet and FGF21 cooperatively promote aerobic thermogenesis in mtDNA mutator mice
Wall, C. E., Whyte, J., Suh, J. M., Fan, W., Collins, B. L., Liddle, C., Yu, R. T., Atkins, A. R., Naviaux, J. C., Li, K., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1509930112 · Cited by 61 · see citing works
Self-citationRyu, M. J., Kim, S. J., Kim, Y. K., Choi, M. J., Tadi, S., Lee, M. H., Lee, S. E., Chung, H. K., Jung, S. B., Kim, H. J., et al. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003356 · Cited by 61 · see citing works
Self-citationDomínguez‐Rodríguez, A., Abreu-González, P., & y, P. A. (2014) · The American Journal of Cardiology · doi:10.1016/j.amjcard.2014.06.020 · Cited by 56 · see citing works
Dumas, J., Simard, G., Flamment, M., Ducluzeau, P., & Ritz, P. (2009) · Diabetes & Metabolism · doi:10.1016/j.diabet.2009.02.002 · Cited by 55 · see citing works
Activins in adipogenesis and obesity
Dani, C. (2012) · International Journal of Obesity · doi:10.1038/ijo.2012.28 · Cited by 53 · see citing works
Dong, B., Zhou, H., Han, C., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0110944 · Cited by 52 · see citing works
Gleyzer, N., & Scarpulla, R. C. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.291575 · Cited by 49 · see citing works
Samocha‐Bonet, D., Heilbronn, L. K., Lichtenberg, D. A., & Campbell, L. V. (2009) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2009.09.008 · Cited by 36 · see citing works
Chung, H. K., Kim, Y. K., Park, J., Ryu, M. J., Chang, J. Y., Hwang, J. H., Lee, C., Kim, S., Kim, H. J., Kweon, G. R., et al. (2014) · Liver International · doi:10.1111/liv.12741 · Cited by 32 · see citing works
Self-citationHashimoto, O., & Funaba, M. (2011) · Vitamins and hormones · doi:10.1016/b978-0-12-385961-7.00011-1 · Cited by 29 · see citing works
Activin A increases Pax4 gene expression in pancreatic β cell lines
Ueda, Y. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01914-1 · Cited by 28 · see citing works
Kim, Y. K., Joung, K. H., Ryu, M. J., Kim, S. J., Kim, H., Chung, H. K., Lee, M. H., Lee, S. E., Choi, M. J., Chang, J. Y., et al. (2015) · Diabetologia · doi:10.1007/s00125-015-3506-y · Cited by 24 · see citing works
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GFRAL is the receptor for GDF15 and the ligand promotes weight loss in mice and nonhuman primates
Mullican, S. E., Lin-Schmidt, X., Chin, C.-N., Chavez, J. A., Furman, J. L., Armstrong, A. A., Beck, S. C., South, V. J., Dinh, T. Q., Cash-Mason, T. D., et al. (2017) · Nature Medicine · doi:10.1038/nm.4392 · Cited by 774 · see citing works
GDF15 mediates the effects of metformin on body weight and energy balance
Coll, A. P., Chen, M., Taskar, P., Rimmington, D., Patel, S., Tadross, J. A., Cimino, I., Yang, M., Welsh, P., Virtue, S., et al. (2020) · Nature · doi:10.1038/s41586-019-1911-y · Cited by 584 · see citing works
GDF15 Provides an Endocrine Signal of Nutritional Stress in Mice and Humans
Patel, S., Alvarez-Guaita, A., Melvin, A., Rimmington, D., Dattilo, A., Miedzybrodzka, E. L., Cimino, I., Maurin, A.-C., Roberts, G. P., Meek, C. L., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2018.12.016 · Cited by 509 · see citing works
Justice, J. N., Ferrucci, L., Newman, A. B., Aroda, V. R., Bahnson, J. L., Divers, J., Espeland, M. A., Marcovina, S., Pollak, M. N., Kritchevsky, S. B., et al. (2018) · GeroScience · doi:10.1007/s11357-018-0042-y · Cited by 359 · see citing works
Repairing mitochondrial dysfunction in disease
Sorrentino, V., Menzies, K. J., & Auwerx, J. (2018) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010716-104908 · Cited by 337 · see citing works
Hepatokines and metabolism: Deciphering communication from the liver
Jensen-Cody, S. O., & Potthoff, M. J. (2021) · Molecular Metabolism · doi:10.1016/j.molmet.2020.101138 · Cited by 252 · see citing works
GDF15: a hormone conveying somatic distress to the brain
Lockhart, S. M., Saudek, V., & O’Rahilly, S. (2020) · Endocrine Reviews · doi:10.1210/endrev/bnaa007 · Cited by 256 · see citing works
Baek, S. J., & Eling, T. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2019.02.008 · Cited by 194 · see citing works
Moon, J. S., Goeminne, L. J. E., Kim, J. T., Tian, J. W., Kim, S., Nga, H. T., Kang, S. G., Kang, B. E., Byun, J., Lee, Y., et al. (2020) · Aging Cell · doi:10.1111/acel.13195 · Cited by 141 · see citing works
Self-citationLaurens, C., Parmar, A., Murphy, E., Carper, D., Lair, B., Maes, P., Vion, J., Boulet, N., Fontaine, C., Marquès, M., et al. (2020) · JCI Insight · doi:10.1172/jci.insight.131870 · Cited by 135 · see citing works
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Yi, H.-S., Chang, J. Y., & Shong, M. (2018) · Journal of Molecular Endocrinology · doi:10.1530/jme-18-0005 · Cited by 99 · see citing works
Self-citationThe Interplay between Mitochondrial Morphology and Myomitokines in Aging Sarcopenia
Romanello, V. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms22010091 · Cited by 101 · see citing works
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Arkoumani, M., Papadopoulou-Marketou, N., Nicolaides, N. C., Kanaka-Gantenbein, C., Tentolouris, N., & Papassotiriou, I. (2020) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408363.2019.1678565 · Cited by 64 · see citing works
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Ouyang, J., Isnard, S., Lin, J., Fombuena, B., Peng, X., Chen, Y., & Routy, J.-P. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.581839 · Cited by 39 · see citing works
- Authors
- Chung, H. K., Ryu, D., Kim, K. S., Chang, J. Y., Kim, Y. K., Yi, H.-S., Kang, S. G., Choi, M. J., Lee, S. E., Jung, S.-B., Ryu, M. J., Kim, S. J., Kweon, G. R., Kim, H., Hwang, J. H., Lee, C.-H., Lee, S.-J., Wall, C. E., Downes, M., Evans, R. M., Auwerx, J., & Shong, M.
- Affiliations
- Chungnam National University (KR)
- École Polytechnique Fédérale de Lausanne (CH)
- Research Center for Endocrine and Metabolic Diseases, Chungnam National University School of Medicine, Daejeon 301-721, South Korea 1
- Johns Hopkins University (US)
- Korea Advanced Institute of Science and Technology (KR)
- Korea Research Institute of Bioscience and Biotechnology (KR)
- Salk Institute for Biological Studies (US)
- Corresponding author
- Auwerx, Johan
- Shong, Minho
- ORCID
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2016-12-16
- Volume
- 216
- Issue
- 1
- Pages
- 149-165
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC5223607
- OpenAlex
- W2574687372
- Cited by
- 357
- References
- 79
- Citations by year
- 2026: 33 · 2025: 37 · 2024: 41 · 2023: 34 · 2022: 48 · 2021: 39 · 2020: 57 · 2019: 30 · 2018: 23 · 2017: 14 · 2013: 1
- FWCI
- 23.77
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- KRIBB Repository (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
- Minerva Access (University of Melbourne) (submittedVersion, cc-by-nc-sa)
- Funders
- Ministry of Science, ICT and Future Planning (NRF-2015R1A2A1A13000951, NRF-2014M3A9D8034464)
- Ministry of Education (NRF-2013R1A1A2058889)
- École Polytechnique Fédérale de Lausanne
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (31003A-140780)
- Krebsliga Schweiz (KFS-3082-02-2013)
- National Institutes of Health (R01AG043930, DK057978, DK090962, HL088093, HL105278, ES010337)
- Howard Hughes Medical Institute
- Glenn Foundation for Medical Research
- Leona M. and Harry B. Helmsley Charitable Trust (2012-PG-MED002)
- Topics
- Health Sciences › Medicine › Rheumatology › GDF15 and Related Biomarkers
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Keywords
- growth differentiation factor 15, mitochondrial unfolded protein response, mitohormesis, energy homeostasis, obesity, insulin resistance, skeletal muscle, CRIF1, mitochondrial ribosome, oxidative metabolism, lipid mobilization, ob/ob mice
- MeSH terms
- Adipose Tissue, Animals, Energy Metabolism, Homeostasis, Insulin Resistance, Lipolysis, Liver, Male, Mice, Inbred C57BL, Mice, Obese, Mitochondria, Liver, Mitochondria, Muscle, Obesity, Oxidation-Reduction, Oxidative Phosphorylation, Phenotype, Recombinant Proteins, Time Factors, Transfection, Signal Transduction, Weight Gain, Mice, Knockout, Muscle, Skeletal, Cell Cycle Proteins, Genetic Predisposition to Disease, Leptin, RNA Interference, 3T3-L1 Cells, Mice, Transcription Factor CHOP, Growth Differentiation Factor 15, Unfolded Protein Response
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