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IGF2BP2/IMP2-Deficient Mice Resist Obesity through Enhanced Translation of Ucp1 mRNA and Other mRNAs Encoding Mitochondrial Proteins
Open accessAbstract
Although variants in the IGF2BP2/IMP2 gene confer risk for type 2 diabetes, IMP2, an RNA binding protein, is not known to regulate metabolism. Imp2(-/-) mice gain less lean mass after weaning and have increased lifespan. Imp2(-/-) mice are highly resistant to diet-induced obesity and fatty liver and display superior glucose tolerance and insulin sensitivity, increased energy expenditure, and better defense of core temperature on cold exposure. Imp2(-/-) brown fat and Imp2(-/-) brown adipocytes differentiated in vitro contain more UCP1 polypeptide than Imp2(+/+) despite similar levels of Ucp1 mRNA; the Imp2(-/-)adipocytes also exhibit greater uncoupled oxygen consumption. IMP2 binds the mRNAs encoding Ucp1 and other mitochondrial components, and most exhibit increased translational efficiency in the absence of IMP2. In vitro IMP2 inhibits translation of mRNAs bearing the Ucp1 untranslated segments. Thus IMP2 limits longevity and regulates nutrient and energy metabolism in the mouse by controlling the translation of its client mRNAs.
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“Mice subjected to fasting display decreased IMP2 protein in their livers and white adipose tissue [40].”
From IMPlications of IMP2 in RNA Biology and Disease (2025) · cites this paper as [40]
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“IMP2 expression is impacted by diet and age.”
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Cites
Reduction in the incidence of type 2 diabetes with lifestyle intervention or metformin
(2002) · New England Journal of Medicine · doi:10.1056/nejmoa012512 · Cited by 19,011 · cited 1×
“Susceptibility to type 2 diabetes mellitus (T2DM) is strongly influenced by both environmental (Knowler et al., 2002) and C genetic factors (DIAGRAM Consortium, 2014).”
BackgroundBrown Adipose Tissue: Function and Physiological Significance
CANNON, B., & NEDERGAARD, J. (2004) · Physiological Reviews · doi:10.1152/physrev.00015.2003 · Cited by 6,433
Rapamycin fed late in life extends lifespan in genetically heterogeneous mice
Harrison, D. E., Strong, R., Sharp, Z. D., Nelson, J. F., Astle, C. M., Flurkey, K., Nadon, N. L., Wilkinson, J. E., Frenkel, K., Carter, C. S., et al. (2009) · Nature · doi:10.1038/nature08221 · Cited by 3,766
Genome-wide association analysis identifies loci for type 2 diabetes and triglyceride levels
Saxena, R., Voight, B. F., Lyssenko, V., Burtt, N. P., de Bakker, P. I. W., Chen, H., Roix, J. J., Kathiresan, S., Hirschhorn, J. N., Daly, M. J., et al. (2007) · Science · doi:10.1126/science.1142358 · Cited by 2,843 · cited 1×
“One of the first SNPs found by GWAS for T2DM is located in intron 2 of the gene encoding the RNA binding protein, IGF2 mRNA binding protein 2, abbrevi- ated IGF2BP2 or IMP2 (Saxena et al., 2007; Zeggini et al., 2007; Scott et al., 2007).”
BackgroundSelf-citationA genome-wide association study of type 2 diabetes in Finns detects multiple susceptibility variants
Scott, L. J., Mohlke, K. L., Bonnycastle, L. L., Willer, C. J., Li, Y., Duren, W. L., Erdos, M. R., Stringham, H. M., Chines, P. S., Jackson, A. U., et al. (2007) · Science · doi:10.1126/science.1142382 · Cited by 2,753
The Wellcome Trust Case Control Consortium, U.K.
Mossman, K. (2008) · Scientific American · doi:10.1038/scientificamerican0108-42a · Cited by 2,714
Replication of Genome-Wide Association Signals in UK Samples Reveals Risk Loci for Type 2 Diabetes
Zeggini, E., Weedon, M. N., Lindgren, C. M., Frayling, T. M., Elliott, K. S., Lango, H., Timpson, N. J., Perry, J. R. B., Rayner, N. W., Freathy, R. M., et al. (2007) · Science · doi:10.1126/science.1142364 · Cited by 2,194
Weight gain as a risk factor for clinical diabetes mellitus in women
Colditz, G. A., Willett, W. C., Rotnitzky, A., & Manson, J. E. (1995) · Annals of Internal Medicine · doi:10.7326/0003-4819-122-7-199504010-00001 · Cited by 2,064
Biomarkers of mitochondrial content in skeletal muscle of healthy young human subjects
Larsen, S., Nielsen, J., Hansen, C. N., Nielsen, L. B., Wibrand, F., Stride, N., Schroder, H. D., Boushel, R., Helge, J. W., Dela, F., et al. (2012) · The Journal of Physiology · doi:10.1113/jphysiol.2012.230185 · Cited by 1,180 · cited 2×
“Inasmuch as CS correlates much more closely with mitochondrial fractional area determined by electron microscopy than does mitochondrial DNA (Larsen et al., 2012), these data indicate that mitochondrial oxidative capacity is not different in the Imp2 / .”
BackgroundRibosomal Protein S6 Kinase 1 Signaling Regulates Mammalian Life Span
Selman, C., Tullet, J. M. A., Wieser, D., Irvine, E., Lingard, S. J., Choudhury, A. I., Claret, M., Al-Qassab, H., Carmignac, D., Ramadani, F., et al. (2009) · Science · doi:10.1126/science.1177221 · Cited by 1,120 · cited 1×
“…mouse models with sustained increases in EE also exhibit a lean, obesity-resistant phenotype and prolonged lifespan (e.g., inactivation of Rps6kb1 [Selman et al., 2009], transgenic expres- sion of UCP1 in skeletal muscle [Gates et al., 2007], and low- dose treatment with 2,4 dinitrophenol…”
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Li, S., Li, X., Xue, W., Zhang, L., Yang, L.-Z., Cao, S.-M., Lei, Y.-N., Liu, C.-X., Guo, S.-K., Shan, L., et al. (2020) · Nature Methods · doi:10.1038/s41592-020-01011-4 · Cited by 365
Degrauwe, N., Suvà, M.-L., Janiszewska, M., Riggi, N., & Stamenkovic, I. (2016) · Genes & Development · doi:10.1101/gad.287540.116 · Cited by 324
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Fabbri, L., Chakraborty, A., Robert, C., & Vagner, S. (2021) · Nature reviews. Cancer · doi:10.1038/s41568-021-00380-y · Cited by 286
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Wang, J., Chen, L., & Qiang, P. (2021) · Cancer Cell International · doi:10.1186/s12935-021-01799-x · Cited by 217
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IGF2BP3 From Physiology to Cancer: Novel Discoveries, Unsolved Issues, and Future Perspectives
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Wang, X., Ji, Y., Feng, P., Liu, R., Li, G., Zheng, J., Xue, Y., Wei, Y., Ji, C., Chen, D., et al. (2021) · Advanced Science · doi:10.1002/advs.202100209 · Cited by 147
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Sun, C., Cao, D., Du, B.-B., Chen, C., & Liu, D. (2022) · International Journal of Biological Sciences · doi:10.7150/ijbs.70458 · Cited by 103
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Zhou, Y., Yan, J., Huang, H., Liu, L., Ren, L., Hu, J., Jiang, X., Zheng, Y., Xu, L., Zhong, F., et al. (2024) · Cell Death & Disease · doi:10.1038/s41419-024-06509-9 · Cited by 92
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Wu, L., Song, W., Xie, Y., Hu, L., Hou, X., Wang, R., Gao, Y., Zhang, J.-N., Zhang, L., Li, W., et al. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0045-0 · Cited by 92
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Kessler, S. M., Laggai, S., Barghash, A., Schultheiss, C. S., Lederer, E., Artl, M., Helms, V., Haybaeck, J., & Kiemer, A. K. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.241 · Cited by 90
Bechara, R., Amatya, N., Bailey, R. D., Li, Y., Aggor, F. E. Y., Li, D.-D., Jawale, C. V., Coleman, B. M., Dai, N., Gokhale, N. S., et al. (2021) · Science Immunology · doi:10.1126/sciimmunol.abd1287 · Cited by 89
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Barghash, A., Golob‐Schwarzl, N., Helms, V., Haybaeck, J., & Kessler, S. M. (2016) · Oncotarget · doi:10.18632/oncotarget.10439 · Cited by 67
Carneiro, M., Hu, D., Archer, J. P., Feng, C., Afonso, S., Chen, C., Blanco, J., Garreau, H., Boucher, S., Ferreira, P. G., et al. (2016) · Genetics · doi:10.1534/genetics.116.196667 · Cited by 65
Ravanidis, S., Kattan, F.-G., & Doxakis, E. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082280 · Cited by 70
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Regué, L., Zhao, L., Ji, F., Wang, H., Avruch, J., & Dai, N. (2021) · Molecular Metabolism · doi:10.1016/j.molmet.2021.101209 · Cited by 60
Self-citationPerochon, J., Yu, Y., Aughey, G., Medina, A. B., Southall, T. D., & Cordero, J. B. (2021) · Nature Cell Biology · doi:10.1038/s41556-021-00676-z · Cited by 60
Regué, L., Minichiello, L., Avruch, J., & Dai, N. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.008778 · Cited by 58
Self-citationSuo, M., Rommelfanger, M. K., Chen, Y., Amro, E. M., Han, B., Chen, Z., Szafranski, K., Chakkarappan, S. R., Boehm, B. O., MacLean, A. L., et al. (2022) · Blood · doi:10.1182/blood.2021012197 · Cited by 57
Peng, T., Liu, M., Hu, L., Guo, D., Wang, D., Qi, B., Ren, G., Hu, C., Zhang, F., Chun, H. J., et al. (2022) · Biology Direct · doi:10.1186/s13062-022-00346-6 · Cited by 57
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Zhang, X., Xue, C., Lin, J. J., Ferguson, J. F., Weiner, A. K., Liu, W., Han, Y., Hinkle, C. C., Li, W., Jiang, H., et al. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aar5987 · Cited by 56
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Yoshizawa, T., Sato, Y., Sobuz, S. U., Mizumoto, T., Tsuyama, T., Karim, M. F., Miyata, K., Tasaki, M., Yamazaki, M., Kariba, Y., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-35219-z · Cited by 38
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Xiao, P., Meng, Q., Liu, Q., Lang, Q., Yin, Z., Li, G., Li, Z., Xu, Y., Yu, Z., Geng, Q., et al. (2023) · Cancer Letters · doi:10.1016/j.canlet.2023.216075 · Cited by 33
Shao, J., Wang, M., Zhang, A., Liu, Z., Jiang, G., Tang, T., Wang, J., Jia, X., & Lai, S. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-04899-1 · Cited by 32
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CPEB2‐dependent translation of long 3′‐UTR Ucp1 mRNA promotes thermogenesis in brown adipose tissue
Chen, H., Hsu, C., & Huang, Y. (2018) · The EMBO Journal · doi:10.15252/embj.201899071 · Cited by 31
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Lu, H., Ye, Z., Zhai, Y., Wang, L., Liu, Y., Wang, J., Zhang, W., Luo, W., Lu, Z., & Chen, J. (2020) · The EMBO Reports · doi:10.15252/embr.201947929 · Cited by 29
Zhou, Z., Chen, S., Wu, T., Chen, Y., Cao, Y., Huang, Y., & Liu, D. (2022) · Journal of Cellular Physiology · doi:10.1002/jcp.30919 · Cited by 30
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Chen, B. H., Hivert, M., Peters, M. J., Pilling, L. C., Hogan, J., Pham, L., Harries, L. W., Fox, C. S., Bandinelli, S., Dehghan, A., et al. (2016) · Diabetes · doi:10.2337/db16-0470 · Cited by 28
Ji, L., Zhao, Y., He, L., Zhao, J., Gao, T., Liu, F., Qi, B., Kang, F., Wang, G., Zhao, Y., et al. (2021) · Advanced Science · doi:10.1002/advs.202002794 · Cited by 27
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Metadata
- Authors
- Dai, N., Zhao, L., Wrighting, D., Krämer, D., Majithia, A., Wang, Y., Cracan, V., Borges-Rivera, D., Mootha, V. K., Nahrendorf, M., Thorburn, D. R., Minichiello, L., Altshuler, D., & Avruch, J.
- Affiliations
- Harvard University (US)
- Broad Institute (US)
- European Molecular Biology Laboratory (IT)
- Massachusetts General Hospital (US)
- Royal Children's Hospital (AU)
- University of Oxford (GB)
- Corresponding author
- Altshuler, David
- Avruch, Joseph
- ORCID
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2015-04
- Volume
- 21
- Issue
- 4
- Pages
- 609-621
- ISSN
- 1550-4131 (ISSN-L)
- PMC
- PMC4663978
- OpenAlex
- W2019615270
- Cited by
- 188
- References
- 38
- Citations by year
- 2026: 17 · 2025: 18 · 2024: 17 · 2023: 19 · 2022: 36 · 2021: 21 · 2020: 13 · 2019: 12 · 2018: 12 · 2017: 11 · 2016: 11 · 2015: 1
- FWCI
- 8.60
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Health and Medical Research Council
- National Institute of General Medical Sciences (T32GM007287)
- National Institute of Diabetes and Digestive and Kidney Diseases (P30DK057521, R37DK017776, R37DK17776, P30DK043351, P30DK040561)
- Topics
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Keywords
- IGF2BP2, RNA-binding proteins, diet-induced obesity, brown adipocytes, UCP1, mitochondrial translation, translational regulation, mRNA untranslated regions, energy expenditure, glucose tolerance, insulin sensitivity, hepatic steatosis, lifespan, cold tolerance, type 2 diabetes risk
- MeSH terms
- Uncoupling Protein 1, Analysis of Variance, Animals, Base Sequence, Body Temperature Regulation, Adipose Tissue, Brown, Energy Metabolism, Gene Expression Regulation, Insulin Resistance, Ion Channels, Molecular Sequence Data, Obesity, RNA-Binding Proteins, Sequence Analysis, RNA, Mice, Knockout, Mitochondrial Proteins, Mice
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