Mitochondrial p32/C1qbp Is a Critical Regulator of Dendritic Cell Metabolism and Maturation
Open accessAbstract
Dendritic cell (DC) maturation induced by Toll-like receptor agonists requires activation of downstream signal transduction and metabolic changes. The endogenous metabolite citrate has recently emerged as a modulator of DC activation. However, the metabolic requirements that support citrate production remain poorly defined. Here, we demonstrate that p32/C1qbp, which functions as a multifunctional chaperone protein in mitochondria, supports mitochondrial metabolism and DC maturation. Metabolic analysis revealed that the citrate increase induced by lipopolysaccharide (LPS) is impaired in p32-deficient DCs. We also found that p32 interacts with dihydrolipoamide S-acetyltransferase (E2 component of pyruvate dehydrogenase [PDH] complex) and positively regulates PDH activity in DCs. Therefore, we suggest that DC maturation is regulated by citrate production via p32-dependent PDH activity. p32-null mice administered a PDH inhibitor show decreased DC maturation and ovalbumin-specific IgG production in vivo, suggesting that p32 may serve as a therapeutic target for DC-related autoimmune diseases.
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p32 predominantly localizes in mitochondria and is a recognized RNA-binding protein within the mitochondrial context.
“p32, a well-conserved eukaryotic protein that predominantly localizes in mitochondria (Barna et al, 2019; Gotoh et al, 2018), serves as a recognized RNA-binding protein within the mitochondrial context.”
From The mitochondrial long non-coding RNA lncMtloop regulates mitochondrial transcription and suppresses Alzheimer’s disease (2024) · cites this paper as Gotoh et al, 2018
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Everts, B., Amiel, E., Huang, S. C.-C., Smith, A. M., Chang, C.-H., Lam, W. Y., Redmann, V., Freitas, T. C., Blagih, J., van der Windt, G. J. W., et al. (2014) · Nature Immunology · doi:10.1038/ni.2833 · Cited by 1,064 · see citing works
NAD+-Dependent Activation of Sirt1 Corrects the Phenotype in a Mouse Model of Mitochondrial Disease
Cerutti, R., Pirinen, E., Lamperti, C., Marchet, S., Sauve, A. A., Li, W., Leoni, V., Schon, E. A., Dantzer, F., Auwerx, J., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.04.001 · Cited by 343 · see citing works
Yagi, M., Uchiumi, T., Takazaki, S., Okuno, B., Nomura, M., Yoshida, S.-I., Kanki, T., & Kang, D. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks774 · Cited by 169 · see citing works
Self-citationIkeda, M., Ide, T., Fujino, T., Arai, S., Saku, K., Kakino, T., Tyynismaa, H., Yamasaki, T., Yamada, K.-I., Kang, D., et al. (2015) · PLOS ONE · doi:10.1371/journal.pone.0119687 · Cited by 152 · see citing works
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Research works printed but not linked: 30
- [1]1. Alistar, A. ∙ Morris, B.B. ∙ Desnoyer, R. ... Safety and tolerability of the first-in-class agent CPI-613 in combination with modified FOLFIRINOX in patients with metastatic pancreatic cancer: a single-centre, open-label, dose-escalation, phase 1 trial Lancet Oncol. 2017; 18:770-778 Full Text Full Text (PDF) Scopus (172) PubMed Google Scholar
- [2]2. Arai, F. ∙ Hirao, A. ∙ Ohmura, M. ... Tie2/angiopoietin-1 signaling regulates hematopoietic stem cell quiescence in the bone marrow niche Cell. 2004; 118:149-161 Full Text Full Text (PDF) Scopus (1608) PubMed Google Scholar
- [3]3. Baixauli, F. ∙ Acín-Pérez, R. ∙ Villarroya-Beltrí, C. ... Mitochondrial respiration controls lysosomal function during inflammatory T cell responses Cell Metab. 2015; 22:485-498 Full Text Full Text (PDF) Scopus (241) PubMed Google Scholar
- [4]4. Banchereau, J. ∙ Briere, F. ∙ Caux, C. ... Immunobiology of dendritic cells Annu. Rev. Immunol. 2000; 18:767-811 Crossref Scopus (5789) PubMed Google Scholar
- [5]5. Baruah, P. ∙ Dumitriu, I.E. ∙ Malik, T.H. ... C1q enhances IFN-gamma production by antigen-specific T cells via the CD40 costimulatory pathway on dendritic cells Blood. 2009; 113:3485-3493 Crossref Scopus (54) PubMed Google Scholar
- [6]6. Berwick, D.C. ∙ Hers, I. ∙ Heesom, K.J. ... The identification of ATP-citrate lyase as a protein kinase B (Akt) substrate in primary adipocytes J. Biol. Chem. 2002; 277:33895-33900 Crossref Scopus (305) PubMed Google Scholar
- [7]7. Biswas, S.K. Metabolic reprogramming of immune cells in cancer progression Immunity. 2015; 43:435-449 Full Text Full Text (PDF) Scopus (466) PubMed Google Scholar
- [8]8. Bodur, C. ∙ Kazyken, D. ∙ Huang, K. ... The IKK-related kinase TBK1 activates mTORC1 directly in response to growth factors and innate immune agonists EMBO J. 2018; 37:19-38 Crossref Scopus (70) Google Scholar
- [9]9. Castellano, G. ∙ Woltman, A.M. ∙ Nauta, A.J. ... Maturation of dendritic cells abrogates C1q production in vivo and in vitro Blood. 2004; 103:3813-3820 Crossref Scopus (142) PubMed Google Scholar
- [11]11. Chen, R. ∙ Xiao, M. ∙ Gao, H. ... Identification of a novel mitochondrial interacting protein of C1QBP using subcellular fractionation coupled with CoIP-MS Anal. Bioanal. Chem. 2016; 408:1557-1564 Crossref Scopus (23) PubMed Google Scholar
- [12]12. Chen, Y. ∙ Qian, J. ∙ He, Q. ... mTOR complex-2 stimulates acetyl-CoA and de novo lipogenesis through ATP citrate lyase in HER2/PIK3CA-hyperactive breast cancer Oncotarget. 2016; 7:25224-25240 Crossref Scopus (44) PubMed Google Scholar
- [13]13. Chung, C.Y. ∙ Ysebaert, D. ∙ Berneman, Z.N. ... Dendritic cells: cellular mediators for immunological tolerance Clin. Dev. Immunol. 2013; 2013:972865 Crossref Scopus (63) Google Scholar
- [14]14. Del Prete, A. ∙ Zaccagnino, P. ∙ Di Paola, M. ... Role of mitochondria and reactive oxygen species in dendritic cell differentiation and functions Free Radic. Biol. Med. 2008; 44:1443-1451 Crossref Scopus (92) PubMed Google Scholar
- [15]15. Everts, B. ∙ Amiel, E. ∙ van der Windt, G.J. ... Commitment to glycolysis sustains survival of NO-producing inflammatory dendritic cells Blood. 2012; 120:1422-1431 Crossref Scopus (424) PubMed Google Scholar
- [17]17. Feichtinger, R.G. ∙ Oláhová, M. ∙ Kishita, Y. ... Biallelic C1QBP mutations cause severe neonatal-, childhood-, or later-onset cardiomyopathy associated with combined respiratory-chain deficiencies Am. J. Hum. Genet. 2017; 101:525-538 Full Text Full Text (PDF) Scopus (54) PubMed Google Scholar
- [18]18. Fogal, V. ∙ Richardson, A.D. ∙ Karmali, P.P. ... Mitochondrial p32 protein is a critical regulator of tumor metabolism via maintenance of oxidative phosphorylation Mol. Cell. Biol. 2010; 30:1303-1318 Crossref Scopus (264) PubMed Google Scholar
- [19]19. Ganguly, D. ∙ Haak, S. ∙ Sisirak, V. ... The role of dendritic cells in autoimmunity Nat. Rev. Immunol. 2013; 13:566-577 Crossref Scopus (392) PubMed Google Scholar
- [20]20. Gkikas, I. ∙ Palikaras, K. ∙ Tavernarakis, N. The role of mitophagy in innate immunity Front. Immunol. 2018; 9:1283 Crossref Scopus (179) Google Scholar
- [21]21. Gomes, A.P. ∙ Price, N.L. ∙ Ling, A.J. ... Declining NAD(+) induces a pseudohypoxic state disrupting nuclear-mitochondrial communication during aging Cell. 2013; 155:1624-1638 Full Text Full Text (PDF) Scopus (1083) PubMed Google Scholar
- [22]22. Gotoh, K. ∙ Tanaka, Y. ∙ Nishikimi, A. ... Differential requirement for DOCK2 in migration of plasmacytoid dendritic cells versus myeloid dendritic cells Blood. 2008; 111:2973-2976 Crossref Scopus (62) PubMed Google Scholar
- [23]23. Gotoh, K. ∙ Tanaka, Y. ∙ Nishikimi, A. ... Selective control of type I IFN induction by the Rac activator DOCK2 during TLR-mediated plasmacytoid dendritic cell activation J. Exp. Med. 2010; 207:721-730 Crossref Scopus (94) PubMed Google Scholar
- [24]24. Guilliams, M. ∙ van de Laar, L. A hitchhiker’s guide to myeloid cell subsets: practical implementation of a novel mononuclear phagocyte classification system Front. Immunol. 2015; 6:406 Crossref Scopus (103) PubMed Google Scholar
- [25]25. Herwald, H. ∙ Dedio, J. ∙ Kellner, R. ... Isolation and characterization of the kininogen-binding protein p33 from endothelial cells. Identity with the gC1q receptor J. Biol. Chem. 1996; 271:13040-13047 Crossref Scopus (206) PubMed Google Scholar
- [26]26. Hosszu, K.K. ∙ Valentino, A. ∙ Vinayagasundaram, U. ... DC-SIGN, C1q, and gC1qR form a trimolecular receptor complex on the surface of monocyte-derived immature dendritic cells Blood. 2012; 120:1228-1236 Crossref Scopus (52) Google Scholar
- [28]28. Infantino, V. ∙ Convertini, P. ∙ Cucci, L. ... The mitochondrial citrate carrier: a new player in inflammation Biochem. J. 2011; 438:433-436 Crossref Scopus (295) PubMed Google Scholar
- [29]29. Jiang, J. ∙ Zhang, Y. ∙ Krainer, A.R. ... Crystal structure of human p32, a doughnut-shaped acidic mitochondrial matrix protein Proc. Natl. Acad. Sci. U S A. 1999; 96:3572-3577 Crossref Scopus (232) PubMed Google Scholar
- [30]30. Kamal, A. ∙ Datta, K. Upregulation of hyaluronan binding protein 1 (HABP1/p32/gC1qR) is associated with Cisplatin induced apoptosis Apoptosis. 2006; 11:861-874 Crossref Scopus (42) PubMed Google Scholar
- [31]31. Kawai, T. ∙ Akira, S. Toll-like receptors and their crosstalk with other innate receptors in infection and immunity Immunity. 2011; 34:637-650 Full Text Full Text (PDF) Scopus (2913) PubMed Google Scholar
- [32]32. Koni, P.A. ∙ Joshi, S.K. ∙ Temann, U.A. ... Conditional vascular cell adhesion molecule 1 deletion in mice: impaired lymphocyte migration to bone marrow J. Exp. Med. 2001; 193:741-754 Crossref Scopus (421) PubMed Google Scholar
- [33]33. Krainer, A.R. ∙ Mayeda, A. ∙ Kozak, D. ... Functional expression of cloned human splicing factor SF2: homology to RNA-binding proteins, U1 70K, and Drosophila splicing regulators Cell. 1991; 66:383-394
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Dendritic cell immunotherapy has its antitumor action improved by the LPS in the maturation process
Lopes, A. M. M., Vieira, J. F., da Silva, S. F. M., Murta, E., & Michelin, M. (2025) · Clinical and Translational Oncology · doi:10.1007/s12094-025-03858-5 · Cited by 4 · see citing works
“Although the stimulation for dendritic cell maturation is mainly derived from pathogens or in vivo tissue injury, the in vitro maturation process can be achieved by culturing these cells with various stimuli [13, 15].”
Carlosama, C., Arévalo, C., Jiménez, M. C., Lasso, P., Urueña, C., Fiorentino, S., & Barreto, A. (2024) · Scientific Reports · doi:10.1038/s41598-024-70550-z · Cited by 4 · see citing works
Davoli, R., Vegni, J., Cesarani, A., Dimauro, C., Zappaterra, M., & Zambonelli, P. (2022) · Meat Science · doi:10.1016/j.meatsci.2022.108754 · Cited by 4 · see citing works
Ahl, P. J., Hopkins, R. A., Xiang, W.-W., Au, B., Kaliaperumal, N., Fairhurst, A., & Connolly, J. (2020) · bioRxiv · doi:10.1101/2020.01.21.914663 · Cited by 4
Guo, L., Govindaraj, P., Kievit, M. T., de Coo, I. D., Gerards, M., Hellebrekers, D., Stassen, A. P., Gayathri, N., Taly, A., Sankaran, B. P., et al. (2021) · Neuromuscular Disorders · doi:10.1016/j.nmd.2021.06.014 · Cited by 3 · see citing works
Spatial multiomics profiling reveals ZFP36-mediated immunometabolic reprogramming in bladder cancer
Ye, F.-D., Han, X., Li, W., Huang, L., Chen, Z., Lu, Y., Huang, H., Jiang, H.-W., & Zheng, L.-F. (2026) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.2505125123 · Cited by 2 · see citing works
“This aligns with prior findings that link C1QBP - mediated mitochondrial ROS production to inflammatory processes, including psoriasis (42) and dendritic cell (DC) activation (29).”
Mitochondria power immunity against cancer.
Molina, I. S., & Haldar, M. (2026) · Science · doi:10.1126/science.aeg4325 · Cited by 1
Wen, X., Li, W., Li, S.-F., Chen, D., Zheng, J.-J., Wang, X., Zhang, C., Liu, Y.-T., Ning, Y., Jia, R.-P., et al. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.139307 · Cited by 1 · see citing works
Okuzono, S., Fujii, F., Setoyama, D., Taira, R., Shinmyo, Y., Kato, H., Masuda, K., Yonemoto, K., Akamine, S., Matsushita, Y., et al. (2024) · Genes to Cells · doi:10.1111/gtc.13142 · Cited by 1 · see citing works
“No selection medium (neomycin) was used for stable cell lines or mock-transfected cells in this study (Gotoh et al., 2018; Sasaki et al., 2017).”
Self-citationMetabolic Profile of Innate Immune Cells
Codo, A. C., Penteado, L. D. A., de Medeiros, A. I., & Moraes‐Vieira, P. M. (2021) · Springer eBooks · doi:10.1007/978-3-030-86684-6_5
DeBlasio, S., Wilson, J. R., Tamborindeguy, C., Johnson, R. S., Pinheiro, P., MacCoss, M., Gray, S., & Heck, M. (2020) · bioRxiv · doi:10.1101/2020.12.04.412668 · Cited by 1
“having roles in innate and adaptive immunity, inflammation, infection, apoptosis, pre634 mRNA splicing, macrophage cell adhesion and cancer cell metastasis (73-78).”
BackgroundUnveiling the mysteries of C1QBP in gynecological tumors (Review)
Zhang, H.-R., Feng, J., Zhu, X.-D., Fu, F., Li, B.-L., Guo, T., Liu, J.-B., & Zhan, P. (2026) · Molecular and clinical oncology · doi:10.3892/mco.2026.2944
“Gotoh et al (17) reported that C1QBP supports the maturation of dendritic cells, which induces primary immune responses.”
Cyclophilin D reduces Ca2+ sequestration by complement 1q binding protein
Adegbite, O. S., Adegbite, Y. I., Pickering, C., Criddle, D. N., & Lian, L. (2025) · Biochemical Journal · doi:10.1042/bcj20253361
Liu, Y., Chen, T., & Fan, C. (2025) · Genetics Research · doi:10.1155/genr/6637484
“In addition to its localization in the mitochondrial matrix, the C1QBP protein is distributed across the cell surface, cytoplasm, and nucleus [21, 22].”
Lee, W., Kingstad-Bakke, B. A., Paulson, B. R., Larsen, A., Overmyer, K. A., Marinaik, C. B., Dulli, K., Toy, R., Vogel, G., Mueller, K. P., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.08.083790 · Cited by 1 · see citing works
“…glycolytic reprogramming of DCs via the Akt-mTORC1-KLF2-HIF-1α axis Typically, catabolic metabolism in resting DCs is characterized by oxidative phosphorylation (OXPHOS) fueled by fatty acid oxidation (FAO) and limited glycolysis (Krawczyk et al., 2010, Gotoh et al., 2018, Zuo and Wan, 2019).”
Background
- Authors
- Gotoh, K., Morisaki, T., Setoyama, D., Sasaki, K., Yagi, M., Igami, K., Mizuguchi, S., Uchiumi, T., Fukui, Y., & Kang, D.
- Affiliations
- Kyushu University (JP)
- Corresponding author
- Gotoh, Kazuhito
- Kang, Dongchon
- ORCID
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2018-11
- Volume
- 25
- Issue
- 7
- Pages
- 1800-1815.e4
- ISSN
- 2211-1247 (ISSN-L)
- OpenAlex
- W2901693839
- Cited by
- 80
- References
- 64
- Citations by year
- 2026: 2 · 2025: 11 · 2024: 5 · 2023: 21 · 2022: 9 · 2021: 18 · 2020: 12 · 2019: 2
- FWCI
- 3.56
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Cell Reports (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Bard Graduate Center, Bard College
- Kyushu University
- Japan Society for the Promotion of Science (25893162, 18H07417, 24590387, 16K19196, 15H04764, 18K11077, 26860512)
- Japan Agency for Medical Research and Development (JP18gm0010001)
- Foundation for Promotion of Cancer Research
- Takeda Science Foundation
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Immunotherapy and Immune Responses
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Biochemical Acid Research Studies
- Keywords
- dendritic cell maturation, dendritic cell metabolism, mitochondrial metabolism, citric acid production, lipopolysaccharide, Toll-like receptor signaling, pyruvate dehydrogenase complex, molecular chaperones, IgG production, autoimmune disease therapy
- MeSH terms
- Animals, Cell Differentiation, Dendritic Cells, Electron Transport, Endoplasmic Reticulum, Fatty Acids, Gene Expression Regulation, Glycolysis, Lipopolysaccharides, Mice, Inbred C57BL, Mitochondria, Oxidative Phosphorylation, Protein Binding, Pyruvate Dehydrogenase Complex, Gene Deletion, Mitochondrial Proteins, Toll-Like Receptors
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