Binding of FUN14 domain containing 1 with inositol 1,4,5-trisphosphate receptor in mitochondria-associated endoplasmic reticulum membranes maintains mitochondrial dynamics and function in hearts in vivo
Open accessAbstract
Background: FUN14 domain containing 1 (FUNDC1) is a highly conserved outer mitochondrial membrane protein. The aim of this study is to examine whether FUNDC1 modulates the mitochondria-associated endoplasmic reticulum (ER) membranes (MAMs), mitochondrial morphology, and function in cardiomyocytes and intact hearts. Methods: The impacts of FUNDC1 on MAMs formation and cardiac functions were studied in mouse neonatal cardiomyocytes, in mice with cardiomyocyte-specific Fundc1 gene knockout ( Fundc1 f/Y /Cre αMyHC+/− ), and in the cardiac tissues of the patients with heart failure. Results: In mouse neonatal cardiomyocytes and intact hearts, FUNDC1 was localized in MAMs by binding to ER-resided inositol 1,4,5-trisphosphate type 2 receptor (IP 3 R2). Fundc1 ablation disrupted MAMs and reduced the levels of IP 3 R2 and Ca 2+ in both mitochondria and cytosol, whereas overexpression of Fundc1 increased the levels of IP 3 R2 and Ca 2+ in both mitochondria and cytosol. Consistently, Fundc1 ablation increased Ca 2+ levels in ER, whereas Fundc1 overexpression lowered ER Ca 2+ levels. Further, Fundc1 ablation in cardiomyocytes elongated mitochondria and compromised mitochondrial functions. Mechanistically, we found that Fundc1 ablation-induced reduction of intracellular Ca 2+ levels suppressed mitochondrial fission 1 protein ( Fis1 ) expression and mitochondrial fission by reducing the binding of the cAMP response element binding protein (CREB) in the Fis1 promoter. Fundc1 f/Y /Cre αMyHC+/− mice but not their littermate control mice ( Fundc1 wt/Y /Cre αMyHC+/− ) exhibited cardiac dysfunction. The ligation of the left ventricle artery of Fundc1 f/Y /Cre αMyHC+/− mice caused more severe cardiac dysfunction than those in sham-treated Fundc1 f/Y /Cre αMyHC+/− mice. Finally, we found that the FUNDC1/MAMs/CREB/Fis1 signaling axis was significantly suppressed in patients with heart failure. Conclusions: We conclude that FUNDC1 binds to IP 3 R2 to modulate ER Ca 2+ release into mitochondria and cytosol. Further, a disruption of the FUNDC1 and IP 3 R2 interaction lowers the levels of Ca 2+ in mitochondria and cytosol, both of which instigate aberrant mitochondrial fission, mitochondrial dysfunction, cardiac dysfunction, and heart failure.
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FUNDC1 is essential for maintaining the MAM structure and ensuring appropriate Ca2+ transfer from the sarcoplasmic reticulum to mitochondria in healthy hearts.
“Study showed that mitochondrial outer membrane protein FUN14 domain containing 1 (FUNDC1) is essential for maintaining the MAM structure and ensuring appropriate Ca2+ transfer from the sarcoplasmic reticulum (i.e., ER in myocytes) to mitochondria in healthy hearts [241].”
From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [241]
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Cites
Mitofusin 2 tethers endoplasmic reticulum to mitochondria
de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442 · see citing works
The Failing Heart — An Engine Out of Fuel
Neubauer, S. (2007) · New England Journal of Medicine · doi:10.1056/nejmra063052 · Cited by 2,410 · see citing works
Rizzuto, R., Pinton, P., Carrington, W., Fay, F. S., Fogarty, K. E., Lifshitz, L. M., Tuft, R. A., & Pozzan, T. (1998) · Science · doi:10.1126/science.280.5370.1763 · Cited by 2,257 · see citing works
ER Tubules Mark Sites of Mitochondrial Division
Friedman, J. R., Lackner, L. L., West, M., DiBenedetto, J. R., Nunnari, J., & Voeltz, G. K. (2011) · Science · doi:10.1126/science.1207385 · Cited by 2,072 · see citing works
Mitochondria as sensors and regulators of calcium signalling
Rizzuto, R., De Stefani, D., Raffaello, A., & Mammucari, C. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3412 · Cited by 1,781 · see citing works
Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia-induced mitophagy in mammalian cells
Liu, L., Feng, D., Chen, G., Chen, M., Zheng, Q., Song, P., Ma, Q., Zhu, C., Wang, R., Qi, W., et al. (2012) · Nature Cell Biology · doi:10.1038/ncb2422 · Cited by 1,689 · see citing works
Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels
Szabadkai, G., Bianchi, K., Várnai, P., De Stefani, D., Wieckowski, M. R., Cavagna, D., Nagy, A. I., Balla, T., & Rizzuto, R. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200608073 · Cited by 1,413 · see citing works
Csordás, G., Renken, C. W., Várnai, P., Walter, L., Weaver, D., BUTTLE, K. F., Balla, T., Mannella, C. A., & Hajnóczky, G. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200604016 · Cited by 1,377 · see citing works
Mitochondrial Dynamics — Mitochondrial Fission and Fusion in Human Diseases
Archer, S. L. (2013) · New England Journal of Medicine · doi:10.1056/nejmra1215233 · Cited by 1,103 · see citing works
Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis
Lee, Y.-J., Jeong, S.-Y., Karbowski, M., Smith, C. L., & Youle, R. J. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-04-0294 · Cited by 1,042 · see citing works
Cárdenas, C., Miller, R. A., Smith, I., Bui, T., Molgó, J., Müller, M., Vais, H., Cheung, K.-H., Yang, J., Parker, I., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.007 · Cited by 1,026 · see citing works
Endoplasmic reticulum-mitochondria contacts: Function of the junction
Rowland, A. A., & Voeltz, G. K. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3440 · Cited by 1,018 · see citing works
Inhibiting Mitochondrial Fission Protects the Heart Against Ischemia/Reperfusion Injury
Ong, S.-B., Subrayan, S., Lim, S. Y., Yellon, D. M., Davidson, S. M., & Hausenloy, D. J. (2010) · Circulation · doi:10.1161/circulationaha.109.906610 · Cited by 986 · see citing works
Mitochondrial dynamics and mitochondrial quality control
Ni, H.-M., Williams, J. A., & Ding, W.-X. (2015) · Redox Biology · doi:10.1016/j.redox.2014.11.006 · Cited by 931 · see citing works
Yoon, Y., Krueger, E. W., Oswald, B. J., & McNiven, M. A. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.15.5409-5420.2003 · Cited by 820 · see citing works
Regulation of mitochondrial dynamics in acute kidney injury in cell culture and rodent models
Brooks, C., Wei, Q., Cho, S.-G., & Dong, Z. (2009) · Journal of Clinical Investigation · doi:10.1172/jci37829 · Cited by 735 · see citing works
Sebastián, D., Hernández-Alvarez, M. I., Segalés, J., Sorianello, E., Muñoz, J. P., Sala, D., Waget, A., Liesa, M., Paz, J. C., Gopalacharyulu, P., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1108220109 · Cited by 673 · see citing works
A Sensitive and Quantitative Technique for Detecting Autophagic Events Based on Lysosomal Delivery
Katayama, H., Kogure, T., Mizushima, N., Yoshimori, T., & Miyawaki, A. (2011) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.05.013 · Cited by 650 · see citing works
Mitophagy receptor FUNDC1 regulates mitochondrial dynamics and mitophagy
Chen, M., Chen, Z., Wang, Y., Tan, Z. L., Zhu, C., Li, Y., Han, Z., Chen, L., Gao, R., Liu, L., et al. (2016) · Autophagy · doi:10.1080/15548627.2016.1151580 · Cited by 600 · see citing works
Mitofusin 2 ablation increases endoplasmic reticulum–mitochondria coupling
Filadi, R., Greotti, E., Turacchio, G., Luini, A., Pozzan, T., & Pizzo, P. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1504880112 · Cited by 578 · see citing works
Mitochondrial energy metabolism in heart failure: a question of balance
Huss, J. M., & Kelly, D. P. (2005) · Journal of Clinical Investigation · doi:10.1172/jci24405 · Cited by 533 · see citing works
Multiple dynamin family members collaborate to drive mitochondrial division
Lee, J. E., Westrate, L. M., Wu, H., Page, C., & Voeltz, G. K. (2016) · Nature · doi:10.1038/nature20555 · Cited by 512 · see citing works
Mitochondrial Fusion is Essential for Organelle Function and Cardiac Homeostasis
Chen, Y., Liu, Y., & Dorn, G. W. (2011) · Circulation Research · doi:10.1161/circresaha.111.258723 · Cited by 506 · see citing works
MCUR1 is an essential component of mitochondrial Ca2+ uptake that regulates cellular metabolism
Mallilankaraman, K. B., Cárdenas, C., Doonan, P. J., Chandramoorthy, H. C. K., Irrinki, K. M., Golenár, T., Csordás, G., Madireddi, P., Yang, J., Müller, M., et al. (2012) · Nature Cell Biology · doi:10.1038/ncb2622 · Cited by 487 · see citing works
Parkin-mediated mitophagy directs perinatal cardiac metabolic maturation in mice
Gong, G., Song, M., Csordás, G., Kelly, D. P., Matkovich, S. J., & Dorn, G. W. (2015) · Science · doi:10.1126/science.aad2459 · Cited by 441 · see citing works
CaM kinase Iα–induced phosphorylation of Drp1 regulates mitochondrial morphology
Han, X.-J., Lü, Y.-F., Li, S.-A., Kaitsuka, T., Sato, Y., Tomizawa, K., Nairn, A. C., Takei, K., Matsui, H., & Matsushita, M. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200802164 · Cited by 423 · see citing works
Mallilankaraman, K. B., Cárdenas, C., Doonan, P. J., Chandramoorthy, H. C. K., Irrinki, K. M., Golenár, T., Csordás, G., Madireddi, P., Yang, J., Müller, M., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3202 · Cited by 418 · see citing works
Wu, W., Lin, C., Wu, K., Jiang, L., Wang, X., Li, W., Zhuang, H., Zhang, X., Chen, H. H., Li, S., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201593102 · Cited by 362 · see citing works
Papanicolaou, K. N., Khairallah, R. J., Ngoh, G. A., Chikando, A. C., Luptak, I., O’Shea, K. M., Riley, D. D., Lugus, J. J., Colucci, W. S., Lederer, W. J., et al. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.00911-10 · Cited by 358 · see citing works
Giorgi, C., Missiroli, S., Patergnani, S., Duszyński, J., Wieckowski, M. R., & Pinton, P. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6223 · Cited by 332 · see citing works
Levels of human Fis1 at the mitochondrial outer membrane regulate mitochondrial morphology
Stojanovski, D., Koutsopoulos, O. S., Okamoto, K., & Ryan, M. T. (2004) · Journal of Cell Science · doi:10.1242/jcs.01058 · Cited by 332 · see citing works
Determinants and Functions of Mitochondrial Behavior
Labbè, K., Murley, A., & Nunnari, J. M. (2014) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-101011-155756 · Cited by 315 · see citing works
Calí, T., Ottolini, D., Negro, A., & Brini, M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.302794 · Cited by 311 · see citing works
The ER in 3D: a multifunctional dynamic membrane network
Friedman, J. R., & Voeltz, G. K. (2011) · Trends in Cell Biology · doi:10.1016/j.tcb.2011.07.004 · Cited by 301 · see citing works
MCUR1は細胞代謝を制御するミトコンドリアCa 2MCUR1+ 取込の必須成分である
Mallilankaraman, K. B., Cesar, C., Patrick, J., Harish, C. C., Krishna, M. I., Golenár, T., Gyoergy, C., Madireddi, P., Jun, Y., Müller, M., et al. (2012) · Nature Cell Biology · Cited by 270 · see citing works
Mao, K., Wang, K., Liu, X., & Klionsky, D. J. (2013) · Developmental Cell · doi:10.1016/j.devcel.2013.05.024 · Cited by 247 · see citing works
Fentzke, R. C., Korcarz, C. E., Lang, R. M., Lin, H., & Leiden, J. M. (1998) · Journal of Clinical Investigation · doi:10.1172/jci2950 · Cited by 246 · see citing works
miR-484 regulates mitochondrial network through targeting Fis1
Wang, K., Long, B., Jiao, J.-Q., Wang, J., Liu, J., Li, Q., & Li, P. (2012) · Nature Communications · doi:10.1038/ncomms1770 · Cited by 227 · see citing works
Mitofusins 1 and 2 Are Essential for Postnatal Metabolic Remodeling in Heart
Papanicolaou, K. N., Kikuchi, R., Ngoh, G. A., Coughlan, K. A., Dominguez, I. M., Stanley, W. C., & Walsh, K. X. (2012) · Circulation Research · doi:10.1161/circresaha.112.274142 · Cited by 217 · see citing works
Role 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
Mitochondrial Dynamics in Cardiovascular Health and Disease
Ong, S., Hall, A. R., & Hausenloy, D. J. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4777 · Cited by 204 · see citing works
The cell-type specificity of mitochondrial dynamics
Kuznetsov, A. V., Hermann, M., Saks, V. A., Hengster, P., & Margreiter, R. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.03.007 · Cited by 168 · see citing works
Mitochondrial dynamics in heart disease
Dorn, G. W. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.03.008 · Cited by 159 · see citing works
Onoue, K., Jofuku, A., Ban-Ishihara, R., Ishihara, T., Maeda, M., Koshiba, T., Itoh, T., Fukuda, M., Otera, H., Oka, T., et al. (2012) · Journal of Cell Science · doi:10.1242/jcs.111211 · Cited by 158 · see citing works
Pennanen, C., Parra, V., López‐Crisosto, C., Morales, P. E., del Campo, A., Gutiérrez, T., Rivera-Mejías, P., Kuzmicic, J., Chiong, M., Zorzano, A., et al. (2014) · Journal of Cell Science · doi:10.1242/jcs.139394 · Cited by 157 · see citing works
Shaping the dynamic mitochondrial network
Lackner, L. L. (2014) · BMC Biology · doi:10.1186/1741-7007-12-35 · Cited by 148 · see citing works
Shanmughapriya, S., Rajan, S., Hoffman, N. E., Zhang, X., Guo, S., Kolesar, J. E., Hines, K. J., Ragheb, J. G., Jog, N. R., Caricchio, R., et al. (2015) · Science Signaling · doi:10.1126/scisignal.2005673 · Cited by 123 · see citing works
Drp1 phosphorylation and mitochondrial regulation
Chang, C., & Blackstone, C. D. (2007) · EMBO Reports · doi:10.1038/sj.embor.7401118 · Cited by 102 · see citing works
Mitochondria in the human heart
Lemieux, H., & Hoppel, C. L. (2009) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-009-9211-0 · Cited by 93 · see citing works
The complex interplay between mitochondrial dynamics and cardiac metabolism
Parra, V., Verdejo, H., del Campo, A., Pennanen, C., Kuzmicic, J., Iglewski, M., Hill, J. A., Rothermel, B. A., & Lavandero, S. (2011) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-011-9332-0 · Cited by 75 · see citing works
Marriott, K.-S. C., Prasad, M., Thapliyal, V., & Bose, H. S. (2012) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.112.198168 · Cited by 75 · see citing works
Amyloid-Beta Disrupts Calcium and Redox Homeostasis in Brain Endothelial Cells
Fonseca, A. C., Moreira, P., Oliveira, C., Cardoso, S., Pinton, P., & Pereira, C. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8740-7 · Cited by 56 · see citing works
cAMP Response Element Binding Protein Is Expressed and Phosphorylated in the Human Heart
Müller, F. U., Boknı́k, P., Horst, A., Knapp, J., Linck, B., Schmitz, W. L., Vahlensieck, U., Böhm, M., Deng, M. C.-H. K., & Scheld, H. H. (1995) · Circulation · doi:10.1161/01.cir.92.8.2041 · Cited by 49 · see citing works
DJ-1 promotes the proteasomal degradation of Fis1: implications of DJ-1 in neuronal protection
Zhang, Q., Wu, J., Wu, R., Ma, J., Du, G., Jiao, R., Tian, Y., Zheng, Z., & Yuan, Z. (2012) · Biochemical Journal · doi:10.1042/bj20120598 · Cited by 44 · see citing works
Transcriptional regulation by cAMP in the heart
Müller, F. U., Neumann, J., & Schmitz, W. L. (2000) · Springer eBooks · doi:10.1007/978-1-4615-4351-0_2 · Cited by 37 · see citing works
Transcriptional regulation by cAMP in the heart
Müller, F. U., Neumann, J., & Schmitz, W. L. (2000) · Molecular and Cellular Biochemistry · doi:10.1023/a:1007176030884 · Cited by 35 · see citing works
Müller, F. U., Boknı́k, P., Knapp, J., et al. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6971 · Cited by 10 · see citing works
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- Authors
- Wu, S., Lu, Q., Wang, Q., Ding, Y., Ma, Z., Mao, X., Huang, K., Xie, Z., & Zou, M.-H.
- Affiliations
- Georgia State University (US)
- Corresponding author
- Wu, Shengnan
- Lu, Qiulun
- Venue
- Circulation
- Published
- 2017-12-05
- Volume
- 136
- Issue
- 23
- Pages
- 2248-2266
- ISSN
- 0009-7322 (ISSN-L)
- 1524-4539
- PMC
- PMC5716911
- OpenAlex
- W2760395470
- Cited by
- 320
- References
- 57
- Citations by year
- 2026: 32 · 2025: 48 · 2024: 48 · 2023: 34 · 2022: 51 · 2021: 39 · 2020: 37 · 2019: 15 · 2018: 13 · 2017: 2
- FWCI
- 7.49
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Circulation (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute on Aging (R01AG047776)
- National Heart, Lung, and Blood Institute (R01HL079584, R01HL142287, R01HL137371, R01HL132500, R01HL074399, R01HL080499, R01HL110488, R01HL128014, R01HL089920)
- National Cancer Institute (R01CA213022)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiac electrophysiology and arrhythmias
- Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
- Keywords
- FUNDC1, mitochondria-associated endoplasmic reticulum membranes, mitochondrial dynamics, mitochondrial fission, Fis1, CREB, cardiomyocytes, calcium signaling, heart failure, cardiac dysfunction, cardiomyocyte-specific knockout, myocardial ischemia, mitochondrial outer membrane proteins, ER-mitochondria crosstalk
- MeSH terms
- Animals, Binding Sites, Calcium, Cells, Cultured, Endoplasmic Reticulum, Heart Failure, Humans, Intracellular Membranes, Membrane Proteins, Mitochondria, Heart, Phenotype, Promoter Regions, Genetic, Protein Binding, Time Factors, Signal Transduction, Case-Control Studies, Cyclic AMP Response Element-Binding Protein, Mice, Knockout, Genetic Predisposition to Disease, Mitochondrial Proteins, Myocytes, Cardiac, Mitochondrial Membranes, Inositol 1,4,5-Trisphosphate Receptors, Mitochondrial Dynamics, Mitophagy
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