Evidence for a Mitochondrial Regulatory Pathway Defined by Peroxisome Proliferator–Activated Receptor-γ Coactivator-1α, Estrogen-Related Receptor-α, and Mitofusin 2
Abstract
Mitofusin 2 (Mfn2) is a mitochondrial membrane protein that participates in mitochondrial fusion and regulates mitochondrial metabolism in mammalian cells. Here, we show that Mfn2 gene expression is induced in skeletal muscle and brown adipose tissue by conditions associated with enhanced energy expenditure, such as cold exposure or β3-adrenergic agonist treatment. In keeping with the role of peroxisome proliferator–activated receptor-γ coactivator (PGC)-1α on energy expenditure, we demonstrate a stimulatory effect of PGC-1α on Mfn2 mRNA and protein expression in muscle cells. PGC-1α also stimulated the activity of the Mfn2 promoter, which required the integrity of estrogen-related receptor-α (ERRα)-binding elements located at −413/−398. ERRα also activated the transcriptional activity of the Mfn2 promoter, and the effects were synergic with those of PGC-1α. Mfn2 loss of function reduced the stimulatory effect of PGC-1α on mitochondrial membrane potential. Exposure to cold substantially increased Mfn2 gene expression in skeletal muscle from heterozygous Mfn2 knock-out mice, which occurred in the presence of higher levels of PGC-1α mRNA compared with control mice. Our results indicate the existence of a regulatory pathway involving PGC-1α, ERRα, and Mfn2. Alterations in this regulatory pathway may participate in the pathophysiology of insulin-resistant conditions and type 2 diabetes.
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Conditions that increase energy expenditure such as cold exposure, chronic exercise or nutraceuticals as resveratrol are associated with higher Mfn2 expression in skeletal muscle and brown adipose tissue in mice and humans.
“conditions that increase energy expenditure such as cold exposure, chronic exercise or nutraceuticals as resveratrol are associated with higher Mfn2 expression in skeletal muscle and brown adipose tissue in mice and humans (Cartoni et al., 2005; Dolinsky et al., 2013; Soriano et al., 2006).”
From Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity (2017) · cites this paper as Soriano et al., 2006
Mfn2 expression is controlled by PGC-1α.
“Similar to many mitochondrial genes, Mfn2 expression is controlled by PGC-1α (Soriano et al, 2006), suggesting that decreased PGC-1α activity explains the defects in Mfn2 observed in obese and T2DM individuals.”
From Mitochondrial response to nutrient availability and its role in metabolic disease (2014) · cites this paper as Soriano et al, 2006
PGC-1α and its downstream target gene product, ERRα, stimulate the expression of Mfn2.
“PGC-1α and its downstream target gene product, estrogen-related receptor-α (ERRα), stimulate the expression of Mfn2 (Cartoni et al., 2005; Soriano et al., 2006).”
From New insights into the role of mitochondria in aging: mitochondrial dynamics and more (2010) · cites this paper as Soriano et al., 2006
PGC-1 family members interact with ERRs to transactivate transcription of oxidative genes and mitofusins.
“PGC-1 family members interact with the family of estrogen-related nuclear receptors, or ERRs, to transactivate transcription of oxidative genes (275) and mitofusins (276).”
From The role of mitochondria in the pathogenesis of type 2 diabetes (2010) · cites this paper as [276]
Cites
Wu, Z., Puigserver, P., Andersson, U., Zhang, C., Adelmant, G., Mootha, V., Troy, A., Cinti, S., Lowell, B., Scarpulla, R. C., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80611-x · Cited by 4,139 · see citing works
A Cold-Inducible Coactivator of Nuclear Receptors Linked to Adaptive Thermogenesis
Puigserver, P., Wu, Z., Park, C. W., Graves, R., Wright, M., & Spiegelman, B. M. (1998) · Cell · doi:10.1016/s0092-8674(00)81410-5 · Cited by 3,864 · see citing works
Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1
Rodgers, J. T., Lerin, C., Haas, W., Gygi, S. P., Spiegelman, B. M., & Puigserver, P. (2005) · Nature · doi:10.1038/nature03354 · Cited by 3,160 · see citing works
Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., & Chan, D. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211046 · Cited by 2,601 · see citing works
Self-citationTranscriptional co-activator PGC-1α drives the formation of slow-twitch muscle fibres
Lin, J., Wu, H., Tarr, P. T., Zhang, C.-Y., Wu, Z., Boss, O., Michael, L. F., Puigserver, P., Isotani, E., Olson, E. N., et al. (2002) · Nature · doi:10.1038/nature00904 · Cited by 2,546 · see citing works
Puigserver, P., & Spiegelman, B. M. (2003) · Endocrine Reviews · doi:10.1210/er.2002-0012 · Cited by 2,076 · see citing works
Patti, M. E., Butte, A. J., Crunkhorn, S., Cusi, K., Berria, R., Kashyap, S., Miyazaki, Y., Kohane, I., Costello, M., Saccone, R., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1032913100 · Cited by 1,952 · see citing works
Control of hepatic gluconeogenesis through the transcriptional coactivator PGC-1
Yoon, J. C., Puigserver, P., Chen, G., Donovan, J., Wu, Z., Rhee, J., Adelmant, G., Stafford, J., Kahn, C. R., Granner, D. K., et al. (2001) · Nature · doi:10.1038/35093050 · Cited by 1,821 · see citing works
Insulin-regulated hepatic gluconeogenesis through FOXO1–PGC-1α interaction
Puigserver, P., Rhee, J., Donovan, J., Walkey, C. J., Yoon, J. C., Oriente, F., Kitamura, Y., Altomonte, J., Dong, H., Accili, D., et al. (2003) · Nature · doi:10.1038/nature01667 · Cited by 1,487 · see citing works
CREB regulates hepatic gluconeogenesis through the coactivator PGC-1
Herzig, S., Long, F., Jhala, U. S., Hedrick, S., Quinn, R., Bauer, A., Rudolph, D., Schutz, G., Yoon, C., Puigserver, P., et al. (2001) · Nature · doi:10.1038/35093131 · Cited by 1,440 · see citing works
Peroxisome proliferator–activated receptor γ coactivator-1 promotes cardiac mitochondrial biogenesis
Lehman, J. J., Barger, P. M., Kovacs, A., Saffitz, J. E., Medeiros, D. M., & Kelly, D. P. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10268 · Cited by 1,285 · see citing works
Defects in Adaptive Energy Metabolism with CNS-Linked Hyperactivity in PGC-1α Null Mice
Lin, J., Wu, P.-H., Tarr, P. T., Lindenberg, K. S., St-Pierre, J., Zhang, C.-Y., Mootha, V. K., Jäger, S., Vianna, C. R., Reznick, R. M., et al. (2004) · Cell · doi:10.1016/j.cell.2004.09.013 · Cited by 1,162 · see citing works
Control of mitochondrial morphology by a human mitofusin
Santel, A., & Fuller, M. T. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.5.867 · Cited by 1,012 · see citing works
Mitofusin-2 Determines Mitochondrial Network Architecture and Mitochondrial Metabolism
Bach, D., Pich, S., Soriano, F. X., Vega, N., Baumgartner, B., Oriola, J., Daugaard, J. R., Lloberas, J., Camps, M., Zierath, J. R., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212754200 · Cited by 832 · cited 9× · see citing works
“Mitofusin 2 (Mfn2) is a mitochondrial fusion protein (16–19) that is expressed mainly in tissues with high energetic requirements, such as skeletal muscle and heart (16); consequently, it shows an expression pattern similar to that of PGC-1 .”
BackgroundMethodInfluentialSelf-citationMootha, V. K., Handschin, C., Arlow, D., Xie, X., St. Pierre, J., Sihag, S., Yang, W., Altshuler, D., Puigserver, P., Patterson, N., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401401101 · Cited by 688 · see citing works
Michael, L. F., Wu, Z., Cheatham, R. B., Puigserver, P., Adelmant, G., Lehman, J. J., Kelly, D. P., & Spiegelman, B. M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.061035098 · Cited by 663 · see citing works
Schreiber, S., Emter, R., Hock, M. B., Knutti, D., Cardenas, J., Podvinec, M., Oakeley, E. J., & Kralli, A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308686101 · Cited by 657 · see citing works
Rojo, M., Legros, F., Chateau, D., & Lombès, A. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.8.1663 · Cited by 555 · see citing works
St‐Pierre, J., Lin, J. D., Krauss, S., Tarr, P. T., Yang, R., Newgard, C. B., & Spiegelman, B. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301850200 · Cited by 543 · see citing works
Schreiber, S., Knutti, D., Brogli, K., Uhlmann, T., & Kralli, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212923200 · Cited by 458 · see citing works
Pich, S., Bach, D., Briones, P., Liesa, M., Camps, M., Testar, X., Palacín, M., & Zorzano, A. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi149 · Cited by 455 · see citing works
Self-citationMitofusin-1 protein is a generally expressed mediator of mitochondrial fusion in mammalian cells
Santel, A., Frank, S., Gaume, B. R., Herrler, M., Youle, R. J., & Fuller, M. T. (2003) · Journal of Cell Science · doi:10.1242/jcs.00479 · Cited by 445 · see citing works
Mitofusins 1/2 and ERRα expression are increased in human skeletal muscle after physical exercise
Cartoni, R., Léger, B., Hock, M. B., Praz, M., Crettenand, A., Pich, S., Ziltener, J., Luthi, F., Dériaz, O., Zorzano, A., et al. (2005) · The Journal of Physiology · doi:10.1113/jphysiol.2005.092031 · Cited by 406 · see citing works
Self-citationSLADEK, R. M., Bader, J.-A., & Giguère, V. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.9.5400 · Cited by 375 · see citing works
Dysregulation of HSG triggers vascular proliferative disorders
Chen, K.-H., Guo, X., Ma, D., Guo, Y., Li, Q., Yang, D., Li, P., Qiu, X., Wen, S., Xiao, R.-P., et al. (2004) · Nature Cell Biology · doi:10.1038/ncb1161 · Cited by 370 · see citing works
Expression of <i>Mfn2</i>, the Charcot-Marie-Tooth Neuropathy Type 2A Gene, in Human Skeletal Muscle
Bach, D., Naon, D., Pich, S., Soriano, F. X., Vega, N., Rieusset, J., Laville, M., Guillet, C., Boirie, Y., Wallberg-Henriksson, H., et al. (2005) · Diabetes · doi:10.2337/diabetes.54.9.2685 · Cited by 369 · cited 2× · see citing works
“Mfn2 expression is downregulated in skeletal muscle in animal or human obesity and in type 2 diabetic patients (16,20).”
BackgroundSelf-citationPGC-1, a versatile coactivator
Knutti, D., & Kralli, A. (2001) · Trends in Endocrinology and Metabolism · doi:10.1016/s1043-2760(01)00457-x · Cited by 294 · see citing works
Boss, O., Samec, S., Kühne, F., Bijlenga, P., Assimacopoulos‐Jeannet, F., Seydoux, J., Giacobino, J., & Muzzin, P. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.1.5 · Cited by 276 · see citing works
The PGC-1-related Protein PERC Is a Selective Coactivator of Estrogen Receptor α
Kressler, D., Schreiber, S., Knutti, D., & Kralli, A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201134200 · Cited by 239 · see citing works
Willy, P. J., Murray, I., Qian, J., Busch, B. B., Stevens, W. C., Martin, R., Mohan, R., Zhou, S., Ordentlich, P., Wei, P. Y., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401420101 · Cited by 195 · see citing works
Laganière, J., Tremblay, G. B., Dufour, C. R., Giroux, S., Rousseau, F., & Giguère, V. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313543200 · Cited by 162 · see citing works
Activation of cardiac Cdk9 represses PGC‐1 and confers a predisposition to heart failure
Sano, M., Wang, S. C., Shirai, M., Scaglia, F., Xie, M., Sakai, S., Tanaka, T., Kulkarni, P. A., Barger, P. M., Youker, K. A., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600351 · Cited by 156 · see citing works
Suppression of β Cell Energy Metabolism and Insulin Release by PGC-1α
Yoon, J. C., Xu, G., Deeney, J. T., Yang, S.-N., Rhee, J., Puigserver, P., Levens, A. R., Yang, R., Zhang, C.-Y., Lowell, B. B., et al. (2003) · Developmental Cell · doi:10.1016/s1534-5807(03)00170-9 · Cited by 143 · see citing works
Boss, O., Bachman, E. S., Vidal‐Puig, A., Zhang, C., Peroni, O. D., & Lowell, B. B. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1145 · Cited by 100 · see citing works
Orphan Nuclear Receptor Nur77 Is Involved in Caspase-independent Macrophage Cell Death
Kim, S. O., Ono, K., Tobias, P. S., & Han, J. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20021842 · Cited by 87 · see citing works
Santalucı́a, T., Moreno, H., Palacı́n, M., Yacoub, M. H., Brand, N. J., & Zorzano, A. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5091 · Cited by 83 · see citing works
Self-citationMingrone, G., Manco, M., Calvani, M., Castagneto, M., Naon, D., & Zorzano, A. (2005) · Diabetologia · doi:10.1007/s00125-005-1918-9 · Cited by 68 · see citing works
Self-citationMoreno, H., Serrano, A. L., Santalucı́a, T., Gumà, A., Cantó, C., Brand, N. J., Palacı́n, M., Schiaffino, S., & Zorzano, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306609200 · Cited by 54 · see citing works
Self-citationGómez‐Ambrosi, J., Frühbeck, G., & Martínez, J. A. (2001) · Molecular and Cellular Endocrinology · doi:10.1016/s0303-7207(01)00451-8 · Cited by 43 · see citing works
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Liesa, M., & Shirihai, O. S. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.03.002 · Cited by 1,341 · see citing works
“…of increased energy demand (i.e., exercise and cold exposure) and downregulated in type-2-diabetic patients (nutrient excess), involving the transcriptional coactivators PGC-1a and PGC-1b (Cartoni et al., 2005; Liesa et al., 2008; Soriano et al., 2006; Mootha et al., 2003; Patti et al., 2003).”
BackgroundSelf-citationMitochondrial Dynamics in Mammalian Health and Disease
Liesa, M., Palacín, M., & Zorzano, A. (2009) · Physiological Reviews · doi:10.1152/physrev.00030.2008 · Cited by 953 · see citing works
Self-citationTranscriptional control of mitochondrial biogenesis: the central role of PGC-1
Ventura-Clapier, R., Garnier, A., & Veksler, V. (2008) · Cardiovascular Research · doi:10.1093/cvr/cvn098 · Cited by 932 · see citing works
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Coffey, V. G., & Hawley, J. A. (2007) · Sports Medicine · doi:10.2165/00007256-200737090-00001 · Cited by 756 · see citing works
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Misrani, A., Tabassum, S., & Yang, L. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.617588 · Cited by 654 · see citing works
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Eisner, V., Picard, M., & Hajnóczky, G. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0133-0 · Cited by 622 · see citing works
PGC-1 α , Inflammation, and Oxidative Stress: An Integrative View in Metabolism
Rius‐Pérez, S., Torres-Cuevas, I., Millán, I., Ortega, Á., & Pérez, S. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/1452696 · Cited by 648 · see citing works
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Romanello, V., Guadagnin, E., Gomes, L., Roder, I., Sandri, C., Petersen, Y., Milan, G., Masiero, E., Del Piccolo, P., Foretz, M., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.60 · Cited by 596 · see citing works
“…| All Rights Reserved 0261-4189/10 www.embojournal.org The EMBO Journal VOL 29 | NO 10 | 2010 &2010 European Molecular Biology Organization EMBO THE JOURNAL 1774 implicated in apoptosis as well as in the regulation of muscle metabolism (Soriano et al, 2006) or of cell cycle (Taguchi et al, 2007).”
BackgroundTranscriptional Control of Energy Homeostasis by the Estrogen-Related Receptors
Giguère, V. (2008) · Endocrine Reviews · doi:10.1210/er.2008-0017 · Cited by 584 · see citing works
Signaling pathways controlling skeletal muscle mass
Egerman, M. A., & Glass, D. J. (2014) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.857291 · Cited by 555 · see citing works
“In addition to the transcriptional co-activator PGC1a, the expression of genes important for mitochondrial biogenesis is also in part controlled by the estrogen-related receptor (ERR) subfamily of nuclear receptors (Soriano et al., 2006).”
BackgroundThe role of mitochondria in the pathogenesis of type 2 diabetes
Patti, M.-E., & Corvera, S. (2010) · Endocrine Reviews · doi:10.1210/er.2009-0027 · Cited by 551 · see citing works
Mitochondrial-nuclear communications
Ryan, M. T., & Hoogenraad, N. J. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.052305.091720 · Cited by 575 · see citing works
New insights into the role of mitochondria in aging: mitochondrial dynamics and more
Seo, A. Y., Joseph, A.-M., Dutta, D., Hwang, J. C. Y., Aris, J. P., & Leeuwenburgh, C. (2010) · Journal of Cell Science · doi:10.1242/jcs.070490 · Cited by 522 · see citing works
“PGC-1 and its downstream target gene product, estrogenrelated receptor- (ERR), stimulate the expression of Mfn2 (Cartoni et al., 2005; Soriano et al., 2006).”
BackgroundMitofusins, from Mitochondria to Metabolism
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“Mfn1 and Mfn2 have both been shown to be direct ERRα/PGC-1α gene targets (Soriano et al. 2006; Martin et al. 2014).”
BackgroundMitochondrial quality control and muscle mass maintenance.
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“Moreover, PGC-1α and PGC-1β control mitochondrial dynamics by stimulating Mfn1 and Mfn2 gene expression in a ERRα-dependent manner (Soriano et al., 2006; Russell et al., 2013).”
BackgroundMitochondria and ageing: Role in heart, skeletal muscle and adipose tissue
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Pharmacological approaches to restore mitochondrial function
Andreux, P. A., Houtkooper, R. H., & Auwerx, J. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4023 · Cited by 383 · see citing works
Lu, Q., Zhu, Y., Deng, C., Liang, Z., Chen, J., Chen, Y., Wang, X., Liu, Y., Tian, Y., & Yang, Y. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01756-w · Cited by 360 · see citing works
Foxo1 integrates insulin signaling with mitochondrial function in the liver
Cheng, Z., Guo, S., Copps, K., Dong, X., Kollipara, R., Rodgers, J. T., Depinho, R. A., Puigserver, P., & White, M. F. (2009) · Nature Medicine · doi:10.1038/nm.2049 · Cited by 321 · see citing works
Forever young: SIRT3 a shield against mitochondrial meltdown, aging, and neurodegeneration
Kincaid, B., & Bossy‐Wetzel, E. (2013) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2013.00048 · Cited by 314 · see citing works
“Interestingly, PGC-1α directly regulates mitochondrial dynamics by increasing MFN2 expression (Soriano et al., 2006).”
BackgroundPGC-1α and PGC-1Β Regulate Mitochondrial Density in Neurons
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Gan, Z., Fu, T., Kelly, D. P., & Vega, R. B. (2018) · Cell Research · doi:10.1038/s41422-018-0078-7 · Cited by 287 · see citing works
Zechner, C., Lai, L., Zechner, J. F., Geng, T., Yan, Z., Rumsey, J. W., Collia, D., Chen, Z., Wozniak, D. F., Leone, T. C., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.11.008 · Cited by 274 · see citing works
“Others have recently shown that PGC-1a and PGC-1b are capable of activating transcription of the Mfn2 gene by coacti- vating the nuclear receptor ERRa (Soriano et al., 2006; Liesa et al., 2008).”
BackgroundMitochondrial Biogenesis through Activation of Nuclear Signaling ProteinsPreprint
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BackgroundERRα: a metabolic function for the oldest orphan
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“Chromatin immunoprecipitation, electrophoretic mobility shift assays and transfection analyses indicated that this specific region of the Mfn2 promoter binds to and is activated by the nuclear hormone estrogen-related receptor ERRα, and is further coactivated by PGC-1α (Soriano et al., 2006).”
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White, J. P., Puppa, M. J., Sato, S., Gao, S., Price, R., Baynes, J., Kostek, M., Matesic, L., & Carson, J. (2012) · Skeletal Muscle · doi:10.1186/2044-5040-2-14 · Cited by 217 · see citing works
Song, W., Song, Y., Kincaid, B., Bossy, B., & Bossy‐Wetzel, E. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.07.004 · Cited by 215 · see citing works
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Wang, X. X., Herman‐Edelstein, M., Gafter, U., Qiu, L., Luo, Y., Dobrinskikh, E., Lucia, S. M., Adorini, L., D’Agati, V. D., Levi, J., et al. (2015) · Journal of the American Society of Nephrology · doi:10.1681/asn.2014121271 · Cited by 211 · see citing works
Martin, O. J., Lai, L., Soundarapandian, M. M., Leone, T. C., Zorzano, A., Keller, M. P., Attie, A., Muoio, D. M., & Kelly, D. P. (2013) · Circulation Research · doi:10.1161/circresaha.114.302562 · Cited by 213 · see citing works
Self-citationRole of mitochondrial dynamics proteins in the pathophysiology of obesity and type 2 diabetes
Zorzano, A., Liesa, M., & Palacín, M. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.02.004 · Cited by 209 · see citing works
Self-citationMonga, A., Fulke, A. B., & Dasgupta, D. (2022) · Journal of Hazardous Materials Advances · doi:10.1016/j.hazadv.2022.100113 · Cited by 217 · see citing works
Eichner, L. J., & Giguère, V. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.03.121 · Cited by 200 · see citing works
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Zorzano, A., Liesa, M., Sebastián, D., Segalés, J., & Palacı́n, M. (2010) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2010.01.002 · Cited by 193 · see citing works
Self-citationPGC1α-mediated Mitofusin-2 Deficiency in Female Rats and Humans with Pulmonary Arterial Hypertension
Ryan, J. J., Marsboom, G., Fang, Y.-H., Tóth, P. T., Morrow, E., Luo, N., Piao, L. H., Hong, Z., Ericson, K. J., Zhang, H. J., et al. (2013) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201209-1687oc · Cited by 194 · see citing works
Diet impact on mitochondrial bioenergetics and dynamics
Putti, R., Sica, R., Migliaccio, V., & Lionetti, L. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00109 · Cited by 192 · see citing works
“…line with this suggestion, conditions characterized by increased energy expenditure (such as cold exposure, administration of β3 adrenergic agonist, chronic exercise) are associated with higher Mfn2 expression in skeletal muscle and brown adipose tissue (Cartoni et al., 2005; Soriano et al., 2006).”
BackgroundTur, J., Pereira‐Lopes, S., Vico, T., Marín, E., Muñoz, J. P., Hernández‐Álvarez, M. I., Cardona, P.-J., Antonio Zorzano, A., Lloberas, J., & Celada, A. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108079 · Cited by 192 · see citing works
Self-citationRangwala, S. M., Wang, X., Calvo, J. A., Lindsley, L., Zhang, Y., Deyneko, G., Beaulieu, V., Gao, J., Turner, G. M., & Markovits, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.125401 · Cited by 192 · see citing works
Hernández-Alvarez, M. I., Thabit, H., Burns, N., Shah, S., Brema, I., Hatunic, M., Finucane, F., Liesa, M., Chiellini, C., Naon, D., et al. (2010) · Diabetes Care · doi:10.2337/dc09-1305 · Cited by 189 · see citing works
Self-citationLoss of Mitofusin 2 Promotes Endoplasmic Reticulum Stress
Ngoh, G. A., Papanicolaou, K. N., & Walsh, K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.359174 · Cited by 183 · see citing works
Konopka, A. R., Suer, M. K., Wolff, C. A., & Harber, M. P. (2014) · The Journals of Gerontology: Series A · doi:10.1093/gerona/glt107 · Cited by 187 · see citing works
Mitochondrial Fission in Human Diseases
Serasinghe, M. N., & Chipuk, J. E. (2016) · Handbook of experimental pharmacology · doi:10.1007/164_2016_38 · Cited by 180 · see citing works
“Mfn2 has also shown to have hormone responsive transcriptional regulation as Estrogen-Related Receptor-alpha (ERRα) binds to the human Mfn2 promoter and stimulates transcription (Scarpulla et al. 2012; Soriano et al. 2006).”
PGC-1α modulates denervation-induced mitophagy in skeletal muscle
Vainshtein, A., Desjardins, E. M., Armani, A., Sandri, M., & Hood, D. A. (2015) · Skeletal Muscle · doi:10.1186/s13395-015-0033-y · Cited by 181 · see citing works
Recent progress toward understanding the molecular mechanisms that regulate skeletal muscle mass
Goodman, C. A., Mayhew, D. L., & Hornberger, T. A. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2011.07.013 · Cited by 178 · see citing works
The Good and the Bad of Mitochondrial Breakups
Sprenger, H., & Langer, T. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.08.003 · Cited by 173 · see citing works
Mitochondrial Fusion Is Increased by the Nuclear Coactivator PGC-1β
Liesa, M., Borda-d'Agua, B., Medina‐Gómez, G., Lelliott, C. J., Paz, J. C., Rojo, M., Palacı́n, M., Vidal‐Puig, A., & Zorzano, A. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003613 · Cited by 175 · see citing works
Self-citationReduced mitochondrial density in the vastus lateralis muscle of patients with COPD
Gosker, H. R., Hesselink, M. K. C., Duimel, H., Ward, K., & Schols, A. M. W. J. (2007) · European Respiratory Journal · doi:10.1183/09031936.00146906 · Cited by 172 · see citing works
“One of the target genes of PGC-1a is mitofusin2, which, as its name indicates, plays an important role in the fusion of mitochondria and thus in mitochondrial maintenance [ 21 ].”
BackgroundThe Nuclear Receptor ESRRA Protects from Kidney Disease by Coupling Metabolism and Differentiation
Dhillon, P., Park, J., del Pozo, C. H., Li, L., Doke, T., Huang, S., Zhao, J., Kang, H. M., Shrestra, R., Balzer, M. S., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.11.011 · Cited by 171 · see citing works
Chen, L., Qin, Y. H., Liu, B., Gao, M. Q., Li, A., Li, X., & Gong, G. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.871357 · Cited by 172 · see citing works
The role of PGC-1α on mitochondrial function and apoptotic susceptibility in muscle
Adhihetty, P. J., Uguccioni, G., Leick, L., Hidalgo, J., Pilegaard, H., & Hood, D. A. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00070.2009 · Cited by 168 · see citing works
Cannavino, J., Brocca, L., Sandri, M., Grassi, B., Bottinelli, R., & Pellegrino, M. A. (2015) · The Journal of Physiology · doi:10.1113/jphysiol.2014.286740 · Cited by 166 · see citing works
“Maintenance of a normal expression of Mfn2 is critical for the stimulatory effect of PGC-1α on mitochondrial membrane potential (Soriano et al. 2006) and PGC-1α may regulate mitochondrial fusion/fission events and hence mitochondrial function (Soriano et al. 2006).”
BackgroundMethodMitochondrial dynamics in pulmonary arterial hypertension
Ryan, J. J., Dasgupta, A., Huston, J., Chen, K., & Archer, S. L. (2015) · Journal of Molecular Medicine · doi:10.1007/s00109-015-1263-5 · Cited by 163 · see citing works
Muscle oxidative capacity during IL-6-dependent cancer cachexia.
White, J. P., Baltgalvis, K. A., Puppa, M. J., Sato, S., Baynes, J., & Carson, J. (2011) · American Journal of Physiology. Regulatory Integrative and Comparative Physiology · doi:10.1152/ajpregu.00300.2010 · Cited by 162 · see citing works
“Interestingly, Mfn2 gene expression has been shown to be controlled by PGC-1 and PGC-1 in conjunction with the estrogen-related receptor- (33, 51).”
BackgroundPearen, M. A., Myers, S., Raichur, S., Ryall, J. G., Lynch, G. S., & Muscat, G. E. O. (2008) · Endocrinology · doi:10.1210/en.2007-1202 · Cited by 156 · see citing works
Splice variants of mitofusin 2 shape the endoplasmic reticulum and tether it to mitochondria
Naón, D., Hernández‐Álvarez, M. I., Shinjo, S., Wieczór, M., Ivanova, S., de Brito, O. M., Quintana, A., Hidalgo, J., Palacı́n, M., Aparicio, P., et al. (2023) · Science · doi:10.1126/science.adh9351 · Cited by 158 · see citing works
“Tissues used for RNA purification, protein extraction, or histology were prepared as described (64, 65).”
MethodSelf-citationMitochondrial coupling defect in Charcot–Marie–Tooth type 2A disease
Loiseau, D., Chevrollier, A., Verny, C., Guillet, V., Guéguen, N., de Crescenzo, M. P., Ferré, M., Malinge, M., Guichet, A., Nicolas, G., et al. (2007) · Annals of Neurology · doi:10.1002/ana.21086 · Cited by 156 · see citing works
Lokireddy, S., Wijesoma, I. W., Teng, S., Bonala, S., Gluckman, P. D., McFarlane, C., Sharma, M., & Kambadur, R. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.10.005 · Cited by 154 · see citing works
RetractedDing, H., Jiang, N., Liu, H., Liu, X., Liu, D., Zhao, F., Wen, L., Liu, S., Ji, L. L., & Zhang, Y. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.08.007 · Cited by 149 · see citing works
Dusabimana, T., Kim, S. R., Kim, H. J., Park, S. W., & Kim, H. (2019) · Experimental & Molecular Medicine · doi:10.1038/s12276-019-0245-z · Cited by 150 · see citing works
Mitochondrial response to nutrient availability and its role in metabolic disease
Gao, A. W., Cantó, C., & Houtkooper, R. H. (2014) · EMBO Molecular Medicine · doi:10.1002/emmm.201303782 · Cited by 148 · see citing works
“Similar to many mitochondrial genes, Mfn2 expression is controlled by PGC-1 a (Soriano et al , 2006), suggesting that decreased PGC-1 a activity explains the defects in Mfn2 observed in obese and T2DM individuals.”
Bartolomé, A., García-Aguilar, A., Asahara, S.-I., Kido, Y., Guillén, C., Pajvani, U. B., & Benito, M. (2017) · Molecular and Cellular Biology · doi:10.1128/mcb.00441-17 · Cited by 141 · see citing works
Human Dendritic Cell Subsets Undergo Distinct Metabolic Reprogramming for Immune Response
Basit, F., Mathan, T. S. M., Sancho, D., & de Vries, I. J. M. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02489 · Cited by 133 · see citing works
Functional and physiological genomics of estrogen-related receptors (ERRs) in health and disease
Deblois, G., & Giguère, V. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2010.12.009 · Cited by 135 · see citing works
Physiological Mitochondrial Fragmentation Is a Normal Cardiac Adaptation to Increased Energy Demand
Coronado, M. J., Fajardo, G., Nguyen, K., Zhao, M., Kooiker, K. B., Jung, G., Hu, D., Reddy, S., Sandoval, E., Stotland, A. B., et al. (2017) · Circulation Research · doi:10.1161/circresaha.117.310725 · Cited by 134 · see citing works
Down-regulation of mitofusin-2 expression in cardiac hypertrophy in vitro and in vivo
Lu, F. Y., Moore, X., Gao, X., Dart, A. M., Lim, Y. L., & Du, X. (2007) · Life Sciences · doi:10.1016/j.lfs.2007.04.003 · Cited by 135 · see citing works
Transcriptional control of energy metabolism by nuclear receptors
Scholtes, C., & Giguère, V. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00486-7 · Cited by 129 · see citing works
The NR3B Subgroup: An Overrview
Tremblay, A., & Giguère, V. (2007) · Nuclear Receptor Signaling · doi:10.1621/nrs.05009 · Cited by 134 · see citing works
“…2004], phosphoenolpyruvate carboxykinase (PEPCK) [Herzog et al., 2006], surfactant protein A (SP-A) [Liu et al., 2006], RIP-140/Nrip1 [Nichol et al., 2006], mitofusin 2 [Soriano et al., 2006], Polo-like kinase 2 (Plk2) [Park et al., 2007] and uncoupling protein 1 (UCP-1) [Debevec et al., 2007].”
Crosstalk between mitochondrial (dys)function and mitochondrial abundance
Michel, S., Wanet, A., Pauw, A. D., Rommelaere, G., Arnould, T., & Renard, P. (2011) · Journal of Cellular Physiology · doi:10.1002/jcp.23021 · Cited by 132 · see citing works
“Several lines of evidence indicate that PGC-1a and PGC1b stimulate Mfn2 expression through ERRa transcription factor (Soriano et al., 2006; Liesa et al., 2008).”
BackgroundWang, T., McDonald, C., Petrenko, N. B., Leblanc, M., Wang, T., Giguère, V., Evans, R. M., Patel, V. V., & Pei, L. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.01156-14 · Cited by 131 · see citing works
Oxygen delivery and fetal-placental growth: Beyond a question of supply and demand?
Murray, A. J. (2012) · Placenta · doi:10.1016/j.placenta.2012.06.006 · Cited by 129 · see citing works
Zhang, L., Zhou, Y., Wu, W., Hou, L., Chen, H., Zuo, B., Xiong, Y., & Yang, J. (2017) · International Journal of Biological Sciences · doi:10.7150/ijbs.20132 · Cited by 131 · see citing works
Miret‐Casals, L., Sebastián, D., Brea, J. M., Rico-Leo, E. M., Palacı́n, M., Fernández‐Salguero, P. M., Loza, M. I., Alberício, F., & Antonio Zorzano, A. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.12.001 · Cited by 129 · see citing works
Self-citationMitochondrial dysfunction and skeletal muscle atrophy: Causes, mechanisms, and treatment strategies
Kubat, G. B., Bouhamida, E., Ülger, Ö., Türkel, İ., Pedriali, G., Ramaccini, D., Ekinci, Ö., Özerkliğ, B., Atalay, Ö., Patergnani, S., et al. (2023) · Mitochondrion · doi:10.1016/j.mito.2023.07.003 · Cited by 128 · see citing works
The many roles of PGC-1α in muscle — recent developments
Chan, M. C., & Arany, Z. P. (2014) · Metabolism · doi:10.1016/j.metabol.2014.01.006 · Cited by 125 · see citing works
PGC-1 coactivators in the cardiovascular system
Patten, I. S., & Arany, Z. P. (2011) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2011.09.007 · Cited by 119 · see citing works
Multi-site control and regulation of mitochondrial energy production
Bénard, G., Bellancé, N., José, C., Melser, S., Nouette‐Gaulain, K., & Rossignol, R. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.02.030 · Cited by 118 · see citing works
Joseph, A.-M., Joanisse, D. R., Baillot, R. G., & Hood, D. A. (2011) · Experimental Diabetes Research · doi:10.1155/2012/642038 · Cited by 117 · see citing works
Relationship between Human Aging Muscle and Oxidative System Pathway
Doria, E., Buonocore, D., Focarelli, A., & Marzatico, F. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/830257 · Cited by 117 · see citing works
Ye, X., Feng, D., Tao, K. X., Wang, R., Shi, Y., Qin, H., Murphy, M. P., Yang, Q., & Zhao, G. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.05.018 · Cited by 117 · see citing works
Supramolecular Induction of Mitochondrial Aggregation and Fusion
Sun, C., Wang, Z., Yue, L., Huang, Q., Cheng, Q., & Wang, R. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c06783 · Cited by 116 · see citing works
Update on mitochondria and muscle aging: All wrong roads lead to sarcopenia
Picca, A., Calvani, R., Bossola, M., Allocca, E., Menghi, A., Pesce, V., Lezza, A. M. S., Bernabei, R., Landi, F., & Marzetti, E. (2018) · Biological Chemistry · doi:10.1515/hsz-2017-0331 · Cited by 116 · see citing works
“Suffice is to say that the transcriptional coactivators PGC-1α and PGC-1β control the protein expression of mitochondrial Mfn1 and Mfn2 (Soriano et al., 2006) and fine tune autophagy during some forms of disuse atrophy (Vainshtein et al., 2015).”
BackgroundInfluentialXu, X., Wang, D., Zheng, C., Gao, B., Fan, J., Cheng, P., Liu, B., Yang, L., & Luo, Z. (2019) · Theranostics · doi:10.7150/thno.30658 · Cited by 115 · see citing works
Linking the Metabolic State and Mitochondrial DNA in Chronic Disease, Health, and Aging
Picard, M. A., & Turnbull, D. M. (2013) · Diabetes · doi:10.2337/db12-1203 · Cited by 114 · see citing works
Mfn2 downregulation in excitotoxicity causes mitochondrial dysfunction and delayed neuronal death
Riera, A. M., Segarra‐Mondejar, M., Muñoz, J. P., Ginet, V., Olloquequi, J., Pérez‐Clausell, J., Palacı́n, M., Reina, M., Puyal, J., Zorzano, A., et al. (2014) · The EMBO Journal · doi:10.15252/embj.201488327 · Cited by 112 · see citing works
Self-citationMechanisms of obesity-induced metabolic and vascular dysfunctions
Caldwell, R. W. (2019) · Frontiers in bioscience · doi:10.2741/4758 · Cited by 112 · see citing works
“During conditions of increased energy expenditure, expression of MFN-2 is increased in skeletal muscles and brown adipose tissue (261, 262).”
Mitochondrial Dynamics: The Intersection of Form and Function
Ferree, A. W., & Shirihai, O. S. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-3573-0_2 · Cited by 110 · see citing works
Mfn2 deletion in brown adipose tissue protects from insulin resistance and impairs thermogenesis
Mahdaviani, K., Benador, I. Y., Su, S., Gharakhanian, R., Stiles, L., Trudeau, K. M., Cardamone, M. D., Enriquez-Zarralanga, V., Ritou, E., Aprahamian, T. R., et al. (2017) · EMBO Reports · doi:10.15252/embr.201643827 · Cited by 109 · see citing works
Self-citationWhittington, H. J., Hall, A. R., McLaughlin, C., Hausenloy, D. J., Yellon, D. M., & Mocanu, M. M. (2012) · Cardiovascular Drugs and Therapy · doi:10.1007/s10557-012-6425-x · Cited by 106 · see citing works
“Soriano et al. 2006 showed that overexpression of PGC-1α in cultured muscle cells induced both Mfn2 mRNA and protein expression above the levels of other genes typically enhanced by PGC-1α.”
BackgroundMitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity
López-Lluch, G. (2017) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2016.12.005 · Cited by 103 · see citing works
“…conditions that increase energy expenditure such as cold exposure, chronic exercise or nutraceuticals as resveratrol are 21 associated with higher Mfn2 expression in skeletal muscle and brown adipose tissue in mice and humans (Cartoni et al., 2005; Dolinsky et al., 2013; Soriano et al., 2006).”
BackgroundCarson, J. A., Hardee, J. P., & VanderVeen, B. N. (2015) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2015.11.005 · Cited by 104 · see citing works
Bal, N. C., Maurya, S. K., Singh, S. K., Wehrens, X. H. T., & Periasamy, M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.728188 · Cited by 103 · see citing works
Izzo, A., Nitti, M. P., Mollo, N., Paladino, S., Procaccini, C., Faicchia, D., Calı̀, G., Genesio, R., Bonfiglio, F., Cicatiello, R., et al. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx016 · Cited by 100 · see citing works
Xiong, W., Ma, Z., An, D., Liu, Z., Cai, W., Bai, Y., Zhan, Q., Lai, W., Zeng, Q., Ren, H., et al. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00411 · Cited by 100 · see citing works
“PGC-1α stimulated the activity of the Mfn2 promoter, a process that required the integrity of estrogen-related receptorα (ERRα)-binding elements (Soriano et al., 2006).”
BackgroundKai, J., Xiang, Y., Wang, Z., Wang, F., Jia, Y., Wang, S., Tan, S., Chen, A., Shao, J., Zhang, F., et al. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.03.031 · Cited by 101 · see citing works
Mitochondrial metabolism and diabetes
Kwak, S. H., Park, K. S., Lee, K., & Lee, H. K. (2010) · Journal of Diabetes Investigation · doi:10.1111/j.2040-1124.2010.00047.x · Cited by 97 · see citing works
Huertas, J. R., Casuso, R. A., Hernansanz‐Agustín, P., & Cogliati, S. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/7058350 · Cited by 100 · see citing works
“In fact, exercise-induced PGC-1α translocation to the skeletal muscle nucleus is known to induce MFN1 and MFN2 expression in human skeletal muscle in an ERR-dependent manner [116].”
Background
- Authors
- Soriano, F. X., Liesa, M., Bach, D., Chan, D. C., Palacín, M., & Zorzano, A.
- Affiliations
- Institute for Research in Biomedicine (ES)
- California Institute of Technology (US)
- Institute for Research in Biomedicine (IRB), Scientific Park of Barcelona, and Department of Biochemistry and Molecular Biology, Faculty of Biology, University of Barcelona, Barcelona, Spain
- Venue
- Diabetes
- Publisher
- American Diabetes Association
- Published
- 2006-06-01
- Volume
- 55
- Issue
- 6
- Pages
- 1783-1791
- ISSN
- 0012-1797 (ISSN-L)
- 1939-327X
- OpenAlex
- W2109879006
- Semantic Scholar
- 17041cc2388633b2d920ee981de5eb2d025199be
- Cited by
- 343
- References
- 39
- Citations by year
- 2026: 4 · 2025: 14 · 2024: 13 · 2023: 12 · 2022: 20 · 2021: 13 · 2020: 24 · 2019: 18 · 2018: 25 · 2017: 20 · 2016: 24 · 2015: 19 · 2014: 19 · 2013: 21 · 2012: 27
- FWCI
- 7.51
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Diabetes (publishedVersion)
- PubMed (publishedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion)
- Funders
- Johns Hopkins University
- Generalitat de Catalunya
- Instituto Danone
- Instituto de Salud Carlos III
- Topics
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- mitofusin 2, PGC-1α, estrogen-related receptor alpha, mitochondrial fusion, mitochondrial metabolism, energy expenditure, cold exposure, beta3-adrenergic agonists, skeletal muscle, brown adipose tissue, transcriptional regulation, mitochondrial membrane potential, insulin resistance, type 2 diabetes
- MeSH terms
- Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha, Animals, Adipose Tissue, Brown, Cells, Cultured, Cold Temperature, Dioxoles, Heat-Shock Proteins, HeLa Cells, Humans, Male, Membrane Proteins, Mitochondria, Muscle, Protein Binding, RNA, Messenger, Transcription Factors, Transfection, Blotting, Western, Signal Transduction, Gene Expression, Rats, Wistar, Muscle, Skeletal, GTP Phosphohydrolases, Mitochondrial Proteins, Electrophoretic Mobility Shift Assay, Chromatin Immunoprecipitation, Estrogen Receptor alpha, Mice, Rats
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