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Regulation of the brown and white fat gene programs through a PRDM16/CtBP transcriptional complex
Open accessAbstract
Brown fat is a specialized tissue that can dissipate energy and counteract obesity through a pattern of gene expression that greatly increases mitochondrial content and uncoupled respiration. PRDM16 is a zinc-finger protein that controls brown fat determination by stimulating brown fat-selective gene expression, while suppressing the expression of genes selective for white fat cells. To determine the mechanisms regulating this switching of gene programs, we purified native PRDM16 protein complexes from fat cells. We show here that the PRDM16 transcriptional holocompex contains C-terminal-binding protein-1 (CtBP-1) and CtBP-2, and this direct interaction selectively mediates the repression of white fat genes. This repression occurs through recruiting a PRDM16/CtBP complex onto the promoters of white fat-specific genes such as resistin, and is abolished in the genetic absence of CtBP-1 and CtBP-2. In turn, recruitment of PPAR-γ-coactivator-1α (PGC-1α) and PGC-1β to the PRDM16 complex displaces CtBP, allowing this complex to powerfully activate brown fat genes, such as PGC-1α itself. These data show that the regulated docking of the CtBP proteins on PRDM16 controls the brown and white fat-selective gene programs.
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“This effect depends on the interaction of PRDM16 with PGC-1α/β, PPARγ and C/EBPβ, while binding of PRDM16 to CtBP-1 and CtBP-2 suppresses expression of white fat-selective genes 171,172.”
From Cellular bioenergetics as a target for obesity therapy (2010) · cites this paper as [171]
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Park, J. H., Hur, W., & Lee, S. B. (2015) · Frontiers in Endocrinology · doi:10.3389/fendo.2015.00124 · Cited by 16
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Metabolic characteristics and therapeutic potential of brown and ?beige? adipose tissues
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“PPAR-γ is a member of the nuclear receptor superfamily of ligand-activated transcription factors and is a prerequisite for the differentiation of both brown and white adipocytes (Kajimura et al., 2008).”
Shin, J., Méndez-López, I., Hong, M., Wang, Y., Tanji, K., Wu, W., Shugol, L., Krauss, R. S., Dauer, W. T., & Worman, H. J. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw368 · Cited by 15
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Gao, X., Deng, B., Li, X., Wang, Y., Zhang, J., Hao, X.-Y., & Zhao, J. (2021) · Frontiers in Veterinary Science · doi:10.3389/fvets.2021.661773 · Cited by 13
“Considering that PRDM16 was one of the key transcriptional factors involved in brown adipogenesis (30), the results suggested that melatonin directly regulated adipogenesis of sheep brown preadipocytes.”
BackgroundDDB1 prepares brown adipocytes for cold-induced thermogenesis
Wang, X., Liu, S.-Y., Hu, G.-S., Wang, H., Zhang, G., Cen, X., Xiang, S.-T., Liu, W., Li, P., Ye, H., et al. (2022) · Life Metabolism · doi:10.1093/lifemeta/loac003 · Cited by 13
“Indeed, histone modifiers such as EHMT1, JMJD1A, and HDAC3 [32, 37, 38] and transcriptional factors such as CREB, ATF2, PRDM16, EBF2, and ZFP516 have also been reported to be required for activation of the thermogenic genes [15, 31, 39, 40].”
Thermogenic Fat as a New Obesity Management Tool: From Pharmaceutical Reagents to Cell Therapies
Cheng, Y., Liang, S., Zhang, S., & Hui, X. H. (2024) · Biomedicines · doi:10.3390/biomedicines12071474 · Cited by 13
“It is also a coregulator of and interacts with PGC-1 α / β or CtBPs to promote brown adipocyte-specific genes while suppressing white adipocyte gene expression [76].”
BackgroundFetal programming of adipose tissue function: an evolutionary perspective
Merkestein, M., Cagampang, F. R. A., & Sellayah, D. (2014) · Mammalian Genome · doi:10.1007/s00335-014-9528-9 · Cited by 13
“In fact, many incidents of sudden infant death syndrome have been attributed to hyperactive BAT (Lean and Jennings 1989; Kajimura et al. 2008).”
BackgroundDevelopment and Validation of a Metabolic-related Prognostic Model for Hepatocellular Carcinoma
Huo, J., Wu, L., & Zang, Y. (2021) · Journal of Clinical and Translational Hepatology · doi:10.14218/jcth.2020.00114 · Cited by 13
Brown fat tissue – a potential target to combat obesity
GINTER, E., & Simko, V. (2012) · Bratislavské lekárske listy/Bratislava medical journal · doi:10.4149/bll_2012_013 · Cited by 13
“Whether we entered an era of successful engineering of brown fat in the battle against obesity remains to be seen (8, 23, 40, 41).”
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Bastarrachea, R. A., Chen, J., Kent, J. W., Nava‐González, E. J., Rodríguez-Ayala, E., Daadi, M. M., Jorge, B. C., Laviada‐Molina, H., Comuzzie, A. G., Chen, S., et al. (2017) · IUBMB Life · doi:10.1002/iub.1658 · Cited by 14
PRDM16, a new kid on the block in cardiovascular health and disease
Wauwe, J. V., Kemps, H., Vrancaert, P., Mahy, A., Schellingen, R., Grootaert, M. O. J., Beerens, M., & Luttun, A. (2025) · Cardiovascular Research · doi:10.1093/cvr/cvaf089 · Cited by 12
“8 regulates the differentiation of adipocyte progenitors into BAT by repressing the WAT gene signature in adipocyte precursors 19,20 and the gene programme of skeletal myoblasts in myogenic factor-5 (MYF5)-expressing precursors to favour BAT lineage identity.”
Wang, Y., Li, J., Lu, D., Meng, Q., Song, N., Zhou, H., Xiao, X., Sun, L., & Zhu, H. (2022) · Journal of Proteomics · doi:10.1016/j.jprot.2022.104500 · Cited by 12
Neuropeptide Y – Its role in human performance and extreme environments
Kienast, C., Gunga, H., & Steinach, M. (2019) · REACH · doi:10.1016/j.reach.2019.100032 · Cited by 12
PRDM16, LRP1 and TRPM8 genetic polymorphisms are risk factor for Pakistani migraine patients
Zafar, R., Saleem, T., Sheikh, N., Maqbool, H., Mukhtar, M., & Abbasi, M. H. (2021) · Saudi Journal of Biological Sciences · doi:10.1016/j.sjbs.2021.06.028 · Cited by 12
“, 1995) and subsequently, its transcriptional role in brown fat development was also delineated (Kajimura et al., 2008).”
BackgroundZhang, J. H., Li, N. F., Yan, Z. T., Zhang, D. L., Wang, H. M., Guo, Y. Y., & Ling, Z. (2012) · Endocrine · doi:10.1007/s12020-011-9547-1 · Cited by 11
“After the discovery of PRDM16 [3], the protein has become a potential target for the development of obesityrelated therapeutics, including the possibility that its genetic variation may contribute to disease.”
BackgroundConstruction of a doxycycline inducible adipogenic lentiviral expression system
Liu, Q., Hill, P. J., Karamitri, A., Ryan, K. J. P., Chen, H., & Lomax, M. A. (2012) · Plasmid · doi:10.1016/j.plasmid.2012.10.001 · Cited by 11
“C/EBPb (Plasmid 12557) and pcDNA-PPARc (Plasmid 8895) were also from Addgene.”
InfluentialRepin1 deficiency in adipose tissue improves whole-body insulin sensitivity, and lipid metabolism
Hesselbarth, N., Kunath, A., Kern, M., Gericke, M. T., Mejhert, N., Rydén, M., Stümvoll, M., Blüher, M., & Klöting, N. (2017) · International Journal of Obesity · doi:10.1038/ijo.2017.172 · Cited by 11
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Camptothecin and topotecan inhibit adipocyte differentiation by inducing degradation of PPARγ
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Minimal genotype–phenotype correlation for small deletions within distal 1p36
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GRIM19 Impedes Obesity by Regulating Inflammatory White Fat Browning and Promoting Th17/Treg Balance
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“PRDM16, regulated by p53, plays an important role in the development of BAT [35,36].”
BackgroundKang, X., Amevor, F. K., Zhang, L.-G., Shah, A. M., Zhu, Q. C., Tian, Y., Shu, G., Wang, Y., & Zhao, X. (2022) · Brazilian Journal of Poultry Science · doi:10.1590/1806-9061-2020-1373 · Cited by 10
Effect of LCORL gene polymorphism on body size traits in horse populations
Mostafavi, A., Fozi, M. A., Koshkooieh, A. E., Mohammadabadi, M., Babenko, O., & Klopenko, N. (2019) · Acta Scientiarum Animal Sciences · doi:10.4025/actascianimsci.v42i1.47483 · Cited by 10
“On the other hand, it has been shown that the regulated docking of the CtBP proteins on PRDM16 controls the brown and white fat-selective gene programs (Kajimura et al., 2008).”
BackgroundLu, K.-Y., Lin, S., Dass, K. T. P., Lin, W.-J., Liu, S., & Harn, H. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111687 · Cited by 12
Weng, J. S., Nakamura, T., Moriizumi, H., Takano, H., Yao, R., & Takekawa, M. (2019) · Communications Biology · doi:10.1038/s42003-019-0478-3 · Cited by 10
Li, L., Geng, J., Yu, W. B., Zhou, F., Zheng, Z., Fu, K., Kong, J., & Feng, X. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1205030 · Cited by 9
“Traditionally, AT has been divided into two types: WAT, best known for storing excess energy in the form of triglycerides, and BAT, which oxidizes chemical energy to produce heat to protect against hypothermia and obesity (Kajimura et al., 2008; Seale et al., 2008; Seale et al., 2011).”
Background5-Aza-2′-Deoxycytidine Regulates White Adipocyte Browning by Modulating miRNA-133a/Prdm16
Liang, J., Jia, Y., Yu, H., Yan, H., Shen, Q., Xu, Y., Li, Y., & Yang, M. (2022) · Metabolites · doi:10.3390/metabo12111131 · Cited by 8
Liang, X., Sun, J., Guan, H., Zhu, Q., & Yao, W. (2022) · Biomedicines · doi:10.3390/biomedicines10123131 · Cited by 9
“It has been reported that the interactions of CtBP1 with PRDM16 or C/EBPα suppress the white genes and induce the brown phenotype [16,24].”
BackgroundX-box Binding Protein 1: An Adaptor in the Pathogenesis of Atherosclerosis
Wang, T., Zhou, J., Zhang, X., Wu, Y., Jin, K., Wang, Y., Xu, R., Yang, G., Li, W., & Jiao, L. (2022) · Aging and Disease · doi:10.14336/ad.2022.0824 · Cited by 9
“The high expression of XBP1 is a characteristic of embryonic adipose deposits [6] and white adipose cells [123], whereas the in vitro inhibition of XBP1 in preadipocytes causes deficient adipogenesis[124].”
BackgroundThe miRNA Contribution in Adipocyte Maturation
Giammona, A., Franco, S. D., Dico, A. L., & Stassi, G. (2024) · Non-Coding RNA · doi:10.3390/ncrna10030035 · Cited by 8
“Two PPAR γ isoforms have been described: PPAR γ 1, which is constitutively expressed, and the expression of which is characteristic of fat tissues; and PPAR γ 2, regulated by the previous one, which regulates mainly adipocyte differentiation [25,26].”
BackgroundSerotonin Prevents Differentiation of Brown Adipocytes by Interfering with Their Clock
Rozenblit‐Susan, S., Chapnik, N., & Froy, O. (2019) · Obesity · doi:10.1002/oby.22606 · Cited by 8
“org Obesity | VOLUME 27 | NUMBER 12 | DECEMBER 2019 2019 protein 1 (UCP1), a protein that is localized on the inner membrane of mitochondria and uncouples electron transport from ATP production (18,19).”
BackgroundSelective activation of PPARα maintains thermogenic capacity of beige adipocytes
Egusa, G., Ohno, H., Nagano, G., Sagawa, J., Shinjo, H., Yamamoto, Y., Himeno, N., Morita, Y., Kanai, A., Baba, R., et al. (2023) · iScience · doi:10.1016/j.isci.2023.107143 · Cited by 9
“Immunoprecipitation using anti-Sur2 (BD Pharmingen# 550429) was carried out as previously described.(58,59) The nuclear extracts were prepared in a buffer containing 50 mM Tris (pH 8.”
MethodLee, S.-H., Lee, S.-H., Park, H.-B., & Kim, J. (2022) · Meat Science · doi:10.1016/j.meatsci.2022.109015 · Cited by 7
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Derivation and characterization of a UCP1 reporter human ES cell line
Mukherjee, S., Zhang, T., Lacko, L. A., Tan, L., Xiang, J., Butler, J. M., & Chen, S. (2018) · Stem Cell Research · doi:10.1016/j.scr.2018.04.007 · Cited by 7
“Additionally, mCherry negative cells preferentially express white preadipocyte and adipocyte selective genes such as TCF21, SPHK1, DPT, Serpina3, and EDNRA (Kajimura et al., 2008; Sharp et al., 2012; Timmons et al., 2007) (Fig.”
BackgroundLihua, W., Jia, L., Wei, H., Guoping, R., Yanji, Z., Yue, Z., Yiting, J., & Zhongyu, Z. (2018) · 世界针灸杂志：英文版 · doi:10.1016/j.wjam.2018.05.007 · Cited by 7
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LSD1—a pivotal epigenetic regulator of brown and beige fat differentiation and homeostasisPreprint
Lin, J. Z., & Farmer, S. R. (2016) · Genes & Development · doi:10.1101/gad.288720.116 · Cited by 7
“In particular, PRDM16, a key transcriptional coregulator, has been shown to control this process through the induction of BAT-specific genes and repression of select WAT genes most abundantly expressed in visceral WAT (Seale et al. 2007; Kajimura et al. 2008).”
BackgroundUnamuno, X., Frühbeck, G., & Catalán, V. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.65163-2 · Cited by 7
PRDM16 determines specification of ventricular cardiomyocytes by suppressing alternative cell fates
Wauwe, J. V., Mahy, A., Craps, S., Ekhteraei‐Tousi, S., Vrancaert, P., Kemps, H., Dheedene, W., Puertas, R. D., Trenson, S., Roderick, H. L., et al. (2024) · Life Science Alliance · doi:10.26508/lsa.202402719 · Cited by 8
“This dual activity of PRDM16 has been reported in other cell types, including ECs, SMCs, neurons, and adipocytes (Kajimura et al, 2008; Aranguren et al, 2013; Baizabal et al, 2018; Wang et al, 2023).”
InfluentialWang, Y., Zheng, S., Gao, H., Wang, Y., Chen, Y., & Han, A. (2025) · Cellular Signalling · doi:10.1016/j.cellsig.2025.111634 · Cited by 6
The impact of exercise training on adipose tissue remodelling in cancer cachexia
Ferreira, R. M., Nogueira‐Ferreira, R., Vitorino, R. M. P., Santos, L. L., & Moreira‐Gonçalves, D. (2017) · Porto Biomedical Journal · doi:10.1016/j.pbj.2017.02.006 · Cited by 8
Non-invasive Imaging Methods for Brown Adipose Tissue Detection and Function Evaluation
Zhang, Y., Hu, X., Hu, S., Scotti, A., Cai, K., Wang, J., Zhou, X., Ding, Y., Figini, M., Pan, L., et al. (2018) · Internal Medicine Open Access · doi:10.4172/2165-8048.1000299 · Cited by 6
“Specifically, recruitment of PGC-1α to PRDM1, a transcription regulator of BAT formation, leads to powerful activation of BAT-selective gene expression and suppression of WAT-specific gene expression [19,20].”
BackgroundCardiac ischemia modulates white adipose tissue in a depot-specific manner
Wang, L., Zabri, H., Gorreßen, S., Semmler, D., Hundhausen, C., Fischer, J. W., & Bottermann, K. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.1036945 · Cited by 5
“, 2007), was shown to repress resistin gene expression by interacting with C-terminal binding proteins (CtBPs) (Kajimura et al., 2008).”
BackgroundCPEB2-activated Prdm16 translation promotes brown adipocyte function and prevents obesity
Lu, W.-H., Chen, H., King, P.-C., Peng, C., & Huang, Y. (2024) · Molecular Metabolism · doi:10.1016/j.molmet.2024.102034 · Cited by 5
“…regulator for the maintenance of BAT identity by promoting BAT-selective gene expression while suppressing WAT-speci fi c gene expression [25,50], so PRDM16-cKO Myf5 mice show adult-onset loss of thermogenic activity and BAT dysfunction with increased expression of many WAT genes and…”
Chrysin inhibits adipogenesis by modulating PPARγ: in silico and in vitro studies
Soumya, S. J., Abhinand, C. S., Nair, A. S., Sonu, P. S., Nair, G. M., Gangaprasad, A. N., Nair, A. S., & Nair, A. J. (2023) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2023.2262596 · Cited by 5
“PPAR c is a member of the nuclear receptor superfamily of ligand-activated transcription factors and is a prerequisite for the differentiation of both brown and white adipocytes (Kajimura et al., 2008).”
Sequence variants in the bovine PRDM16 gene associated with body weight in Chinese cattle breeds
Wang, J., Wang, C., Tian, R., Huang, Y.-Z., Lai, X.-S., Lan, X., Wang, J.-Q., & Chen, H. (2012) · Genetics and Molecular Research · doi:10.4238/2012.march.22.5 · Cited by 5
“Previous studies showed that regulated docking of the CtBP proteins on the PRDM16 protein controls the brown and white fat determination (Kajimura et al., 2008).”
BackgroundRemodeling of rat stromal-vascular cells to brite/beige adipocytes by prolyl-hydroxyproline
MINAGUCHI, J. A., OGATA, S., Takahashi, N., Hirose, T., Ueda, H. H., & TAKEHANA, K. (2017) · Journal of Veterinary Medical Science · doi:10.1292/jvms.16-0163 · Cited by 5
“In contrast, the mRNA expression of several genes that are selectively enriched in white adipocytes [10, 11, 19, 40], including Cbp, Fabp and Serpina3k, were suppressed in the Pro-Hyp group.”
BackgroundKeeley, T. S., Kirov, A., Koh, W. Y., DeMambro, V., Bergquist, I., Cotter, J. A., Caradonna, P. A., Siviski, M. E., Best, B., Henderson, T., et al. (2019) · Physiological Reports · doi:10.14814/phy2.14034 · Cited by 4
“Taqman assays used for these studies are as follows: murine PPARc (Mm00440940_m1); murine UCP1 (Mm01244861_m1) and murine PRDM16 (Mm00712556_m1).”
BackgroundDifferential chromatin accessibility and Gene Expression Associated with Backfat Deposition in pigs
Zhang, Z., Chang, L., Wang, B., Wei, Y., Li, X., Li, X., Zhang, Y., Wang, K., Qiao, R., Yang, F., et al. (2024) · BMC Genomics · doi:10.1186/s12864-024-10805-1 · Cited by 4
“CTBP2, acting as a transcriptional repressor, forms a transcriptional repressor complex with KLF3 to suppress the expression of key adipogenic regulators including C/EBPα and PPARγ [39, 40].”
BackgroundGenetic and functional analyses of CTBP2 in anorexia nervosa and body weight regulation
Giuranna, J., Zheng, Y., Brandt, M., Jall, S., Mukherjee, A., Shankhwar, S., Renner, S., Kurapati, N. K., May, C., Peters, T., et al. (2024) · Molecular Psychiatry · doi:10.1038/s41380-024-02791-3 · Cited by 4
“In fact, CTBP2-L/S together with CTBP1/BARS regulate the brown adipogenic program by building a complex with the proline-rich (PR) domain-containing protein 16 (PRDM16) and repressing the expression of white adipose tissue genes like resistin [26, 27].”
Mao, Y., Hong, K., Bhandari, S., Li, L., Liao, W., Kim, S., Xiong, Y., Nam, I.-K., Choe, S., & Kwak, S. (2021) · Oriental Pharmacy and Experimental Medicine · doi:10.1007/s13596-021-00580-9 · Cited by 4
Obesity and metabolic syndrome: Future therapeutics based on novel molecular pathways
Gutiérrez-Salmeán, G., Ceballos, G. M., & Ramírez‐Sánchez, I. (2012) · Clínica e Investigación en Arteriosclerosis · doi:10.1016/j.arteri.2011.11.002 · Cited by 4
Enzymatically Modified Isoquercitrin Attenuates High-Fat Diet-Induced Obesity
Min, Y., & Park, T. (2016) · Journal of the Korean Society of Food Science and Nutrition · doi:10.3746/jkfn.2016.45.4.474 · Cited by 4
Wauwe, J. V., Craps, S., Kc, A., Asuncion, L., Vrancaert, P., Daems, M., Finck, C., Wright, S. H., Müller, C., Leigh, N. D., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.05.471275 · Cited by 4
“17,18,34 We detected 441 differentially expressed genes (DEGs, FDR < 0.05 and logFC > |1”
BackgroundInfluentialNguyen, H. P., Sheng, R. R., Murray, E., Ito, Y., Brück, M., Biellak, C., An, K., Lynce, F. C., Dillon, D. A. R., Magbanua, M. J. M., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.03.28.534564 · Cited by 4
“Here, we set out to develop a novel cancer therapeutic approach, termed adipose manipulation transplantation (AMT) that utilizes two unique abilities of white adipose tissue (WAT): 1) They can be readily extracted via liposuction and implanted via reconstructive surgery; 2) they can change into a BAT-like tissue, call…”
A distal enhancer with ETV4 binding is critical for UCP1 expression and thermogenesis in brown fatPreprint
Xue, P., Holloway, N. D., Tran, A., Lin, F., Dinh, J., Yang, C., Wang, Y., Yi, D., & Sul, H. S. (2025) · Genes & Development · doi:10.1101/gad.352748.125 · Cited by 7
Genomic Crosstalk Between Nuclear Receptors in Hormone-dependent Cancers
Campbell, M. J. (2025) · Endocrinology · doi:10.1210/endocr/bqaf149 · Cited by 3
“…PPAR γ can cycle through intermediate (although weaker) cofactor accessible conformations (64), including not only with classical co-activators (66) and corepressors (67) but also with PPAR γ exclusive coregulators such as PGC-1 α (68) and tissue-specific partners such as PRDM16 (66, 69).”
Liuli, A., Zhang, T., & Feng, Z. (2026) · Frontiers in Endocrinology · doi:10.3389/fendo.2026.1822659 · Cited by 3
“PR domain containing 16 ( PRDM16 ) is a key regulator of beige and brown adipocyte identity and is closely involved in maintaining thermogenic competence in subcutaneous fat (24, 25, 198).”
PRDM16 functions as a co-repressor in the BMP pathway to suppress neural stem cell proliferation
He, L., Wen, J., & Dai, Q. (2025) · eLife · doi:10.7554/elife.104076.3 · Cited by 2
Ye, Z., Zhao, Y., Cui, Y., Xu, B., Wang, F., Zhao, D., Dong, G., Wang, Z., & Wu, R. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1386794 · Cited by 3
Fernández‐Rhodes, M., Suárez, M., Molet, I., Suárez‐Garcia, S., Arola, L., Sze, S. K., Gallart‐Palau, X., & Serra, A. (2025) · ACS Omega · doi:10.1021/acsomega.5c02274 · Cited by 3
Brown Fat and Its Thermoregulatory Role in the Human Neonate
Dv, M., Muralidhara, K. D., & Zubaidi, A. L. A. (2010) · Journal of Physiological and Biomedical Sciences · Cited by 2
Pervin, S., Wilson, N. Y. A. H., Reddy, S. T., & Singh, R. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.88294 · Cited by 3
“Coincident with these changes, PRDM16 expression also led to suppression of several white fat and muscle-selective markers [29].”
BackgroundRecent advances in human brown fat physiology.
Dv, M., & Muralidhara, K. D. (2011) · PubMed · Cited by 3
Hypothalamic mitochondria in energy homeostasis and obesity
Guo, X., Wu, L., Wang, W., Medeiros, D. M., Clarke, S. L., Lucas, E. A., Smith, B. J., Chowanadisai, W., & Lin, D. (2016) · Integrative Molecular Medicine · doi:10.15761/imm.1000209 · Cited by 3
“PR Domain Containing 16 (PRDM16) is the coactivator of PGC1α and PGC-1β, which is important for mitochondrial biogenesis and uncoupled cellular respiration [87,88].”
BackgroundHasan, A., Kochumon, S., Al‐Ozairi, E., Tuomilehto, J. O., Al‐Mulla, F., & Ahmad, R. (2020) · Diabetes Metabolic Syndrome and Obesity · doi:10.2147/dmso.s251978 · Cited by 6
Transcriptional Regulation of Brown and White Adipogenesis
Spiegelman, B. M. (2010) · Research and perspectives in endocrine interactions · doi:10.1007/978-3-642-13517-0_8 · Cited by 3
“Mechanistic studies showed that PRDM16 could work directly on the promoters of many genes, activating those selective for brown fat cells while suppressing those expressed selectively in white fat cells (Kajimura et al. 2008).”
BackgroundSelf-citationIdentification and characterization of repressive domains in Drosophila transcription factorsPreprint
Klaus, L., de Almeida, B. P., Vlasova, A. V., Nemčko, F., Schleiffer, A., Bergauer, K., Rath, M., & Stark, A. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.08.26.505062 · Cited by 3
“…indeed many known repressors: for example among the 30 highest scoring PxDLS motif matches we found 19 proteins known to repress transcription through CtBP, for example MECOM (also EVI1), ZFPM1 and PRDM16 (Izutsu et al, 2001; Katz et al, 2002; Kajimura et al, 2008; additional references in Suppl.”
PRDM16 functions as a co-repressor in the BMP pathway to suppress neural stem cell proliferationPreprint
He, L., Wen, J., & Dai, Q. (2025) · eLife · doi:10.7554/elife.104076 · Cited by 3
“The PR domain-containing (PRDM) family protein PRDM16 determines cell fate specification in various cell types ( Aguilo et al., 2011 ; Chuikov et al., 2010 ; Kajimura et al., 2008 ; Shimada et al., 2017 ; Chui et al., 2020 ; Baizabal et al., 2018 ; Inoue et al., 2017 ).”
Chen, Q.-C., Wu, C., Cai, W., Ni, Q., Lin, S., Zheng, S., Jiang, C., Yi, Y., Liu, Q., & Shen, C. (2025) · Journal of Functional Foods · doi:10.1016/j.jff.2025.106758 · Cited by 2
The Functional Interaction Between PRDM16 and the SREBP Pathway Controls Lipid Metabolism
Mahmood, H. M., Bengoechea-Alonso, M. T., Al-Ansari, D. E., Machaca, K., & Ericsson, J. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262110246 · Cited by 3
Tunbak, H., Georgiou, C., Guan, C., Richardson, W. D., & Chittka, A. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.04.128 · Cited by 2
Takahashi, T., Takase, Y., Shiraishi, A., Matsubara, S., Watanabe, T., Kirimoto, S., Yamagaki, T., & Osawa, M. (2025) · Endocrinology · doi:10.1210/endocr/bqaf064 · Cited by 1
“In contrast, the expression levels of the genes for adiponectin and resistin, which are commonly used as markers of WAT (29, 30), tended to be lower in the subcutaneous WAT of M4-KO mice at the transcript level (Fig.”
Warren, S., Farran, B. E., Kang, S., Choudhuri, A., Xiong, S., Brendel, V., & Baizabal, J. (2025) · Development · doi:10.1242/dev.204553 · Cited by 2
Schmucker, D., & Hassan, B. A. (2012) · Nature Neuroscience · doi:10.1038/nn.3029 · Cited by 2
PRDM16 in Development and Disease
Pisano, M. M. (2014) · Human Genetics & Embryology · doi:10.4172/2161-0436.1000121 · Cited by 1
“It was then subsequently demonstrated that PRDM16 was the master regulator of BAT formation by virtue of its interaction with PGC1α and PGC1β while simultaneously inhibiting the expression of WAT-specific genes through binding to CtBP 1 and 2 [27].”
BackgroundMaksimović, N., Vidović, V., Damnjanović, T., Jekić, B., Singh, N. M., Simeunović, S., Bozovic, D. S., Vidović, S., & Novaković, I. V. (2021) · Archives of Medical Science · doi:10.5114/aoms/113174 · Cited by 2
“PRDM16 and CtBP2 form complexes that bind directly to the promoters of white fat tissue specific genes such as resistin and angiotensinogen and repress their expression [11].”
BackgroundProtein PRDM16 and its importance for adipose tissue (literature review)
Afanaskina, L. N., Деревцова, С. Н., Николаевна, Ч. Т., & Медведева, Н. Н. (2023) · Сибирский научный медицинский журнал · doi:10.18699/ssmj20230503 · Cited by 1
Clinical value of serum PRDM16 in early diagnosis and prognosis assessment of lung adenocarcinoma
Fan, M., Li, M., Zhou, J., Li, A., Sun, Y., Shi, P., Zhang, S., Chen, M., & Ren, H. (2025) · Molecular Biology Reports · doi:10.1007/s11033-025-10315-7 · Cited by 1
“PRDM16 may also control the tran - scription of metabolic genes in adipocytes [23].”
Wang, Y., Zhang, K. X., Kan, C., Zhang, W., Sun, X., & Li, L. (2025) · Food Science & Nutrition · doi:10.1002/fsn3.70613 · Cited by 1
“…protein, directly influences UCP1 expression in BAT to regulate thermogenesis, while PRDM16, a zinc-finger protein, governs BAT determination by promoting brown adipocyte-specific gene expression and repressing white adipocyte-specific genes (Kajimura et al. 2008; Sanders and Tisdale 2004).”
Köker, Ş. C., Tsokanos, F., El‐Merahbi, R., Jha, A. K., Cicatelli, K., Weber, P., Mhamane, A., Kaltenecker, D., Morigny, P., Loft, A., et al. (2025) · The FASEB Journal · doi:10.1096/fj.202402993rrr · Cited by 1
“While only a fraction of total PRDM16 appears to associate with the TBLR1/TBL1 complex under non-stimulated conditions, this is consistent with the known biology of PRDM16 as a transcriptional scaffold that forms multiple, distinct complexes depending on the physiological context [54–56].”
Kajimura, S. (2025) · Diabetes · doi:10.2337/dbi25-0026 · Cited by 2
Self-citationGabpα‐Pparγ Complex Determines Glycolytic Capacity and Lactic Acid Homeostasis in Brown Fat
Wang, Z., Wang, H., Kang, Q., Pan, R., He, R., Yang, M., Liu, J., Peng, X., Xie, Y., Deng, H., et al. (2025) · Advanced Science · doi:10.1002/advs.202517426 · Cited by 1
Paulo, E., Wu, Y., & Wang, B. (2026) · iScience · doi:10.1016/j.isci.2026.116442 · Cited by 1
“35,36 Briefly, BAT SVF was digested in digestion buffer for 45 min: Ham’s F-10 1 × Medium (Corning, #10-070-CV), Collagenase 1.5 mg/mL (Sigma, #C6885) and Dispase II 1 mg/mL (Roche, #14549000).”
Influential
Metadata
- Authors
- Kajimura, S., Seale, P., Tomaru, T., Erdjument-Bromage, H., Cooper, M. P., Ruas, J. L., Chin, S., Tempst, P., Lazar, M. A., & Spiegelman, B. M.
- Affiliations
- Harvard University (US)
- University of Pennsylvania (US)
- Memorial Sloan Kettering Cancer Center (US)
- ORCID
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2008-05-15
- Volume
- 22
- Issue
- 10
- Pages
- 1397-1409
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- PMC
- PMC2377193
- OpenAlex
- W2163468424
- Cited by
- 468
- References
- 78
- Citations by year
- 2026: 12 · 2025: 25 · 2024: 13 · 2023: 16 · 2022: 18 · 2021: 21 · 2020: 25 · 2019: 22 · 2018: 27 · 2017: 35 · 2016: 30 · 2015: 46 · 2014: 33 · 2013: 28 · 2012: 32
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Digital Access to Scholarship at Harvard (DASH) (Harvard University) (submittedVersion, cc-by)
- HighWire Press Open Archive (submittedVersion)
- Funders
- Wenner-Gren Foundation
- University of Pittsburgh
- National Institutes of Health (CA08748)
- National Cancer Institute (P30-CA-08748, CA08748, P30CA008748)
- National Institute of Diabetes and Digestive and Kidney Diseases (R37 DK-31405, P01DK049210, DK 49210, R37DK031405)
- Topics
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Peroxisome Proliferator-Activated Receptors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- PRDM16, brown adipose tissue, white adipose tissue, transcriptional repression, PGC-1α, PGC-1β, resistin, transcriptional complex, gene expression regulation, obesity
- MeSH terms
- Alcohol Oxidoreductases, Animals, Adipose Tissue, Brown, Cell Differentiation, Chlorocebus aethiops, DNA-Binding Proteins, Gene Expression Regulation, Genes, Regulator, Models, Biological, Phosphoproteins, Protein Binding, Transcription Factors, Transcription, Genetic, 3T3 Cells, COS Cells, 3T3-L1 Cells, Multiprotein Complexes, Mice, Adipose Tissue, White, Co-Repressor Proteins
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