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MCUR1 Is a Scaffold Factor for the MCU Complex Function and Promotes Mitochondrial Bioenergetics
Open accessAbstract
Mitochondrial Ca(2+) Uniporter (MCU)-dependent mitochondrial Ca(2+) uptake is the primary mechanism for increasing matrix Ca(2+) in most cell types. However, a limited understanding of the MCU complex assembly impedes the comprehension of the precise mechanisms underlying MCU activity. Here, we report that mouse cardiomyocytes and endothelial cells lacking MCU regulator 1 (MCUR1) have severely impaired [Ca(2+)]m uptake and IMCU current. MCUR1 binds to MCU and EMRE and function as a scaffold factor. Our protein binding analyses identified the minimal, highly conserved regions of coiled-coil domain of both MCU and MCUR1 that are necessary for heterooligomeric complex formation. Loss of MCUR1 perturbed MCU heterooligomeric complex and functions as a scaffold factor for the assembly of MCU complex. Vascular endothelial deletion of MCU and MCUR1 impaired mitochondrial bioenergetics, cell proliferation, and migration but elicited autophagy. These studies establish the existence of a MCU complex that assembles at the mitochondrial integral membrane and regulates Ca(2+)-dependent mitochondrial metabolism.
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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
Mechanisms by which mitochondria transport calcium
Gunter, T. E., & Pfeiffer, D. R. (1990) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1990.258.5.c755 · Cited by 1,640
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
Luongo, T. S., Lambert, J. P., Yuan, A., Zhang, X., Gross, P., Song, J., Shanmughapriya, S., Gao, E., Jain, M., Houser, S. R., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.06.017 · Cited by 384
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Davidson, S. M., & Duchen, M. R. (2007) · Circulation Research · doi:10.1161/01.res.0000261970.18328.1d · Cited by 381
Echtay, K. S., Winkler, E., Frischmuth, K., & Klingenberg, M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.4.1416 · Cited by 313
Boden, G., Homko, C., Barrero, C. A., Stein, T. P., Chen, X., Cheung, P., Fecchio, C., Koller, S., & Merali, S. (2015) · Science Translational Medicine · doi:10.1126/scitranslmed.aac4765 · Cited by 214
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Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., et al. (2021) · Autophagy · doi:10.1080/15548627.2020.1797280 · Cited by 2,897
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Marchi, S., Patergnani, S., Missiroli, S., Morciano, G., Rimessi, A., Wieckowski, M. R., Giorgi, C., & Pinton, P. (2018) · Cell Calcium · doi:10.1016/j.ceca.2017.05.003 · Cited by 695
Raffaello, A., Mammucari, C., Gherardi, G., & Rizzuto, R. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.09.001 · Cited by 536
Mitochondrial calcium exchange in physiology and disease
Garbincius, J. F., & Elrod, J. W. (2022) · Physiological Reviews · doi:10.1152/physrev.00041.2020 · Cited by 412
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Hook, P. W., McClymont, S. A., Cannon, G. H., Law, W. D., Morton, A. J., Goff, L. A., & McCallion, A. S. (2018) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2018.02.001 · Cited by 136
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Walters, G. C., & Usachev, Y. M. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1094356 · Cited by 105
Gong, Y., Lin, J., Ma, Z., Yu, M., Wang, M., Lai, D., & Fu, G. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119511 · Cited by 58
Metadata
- Authors
- Tomar, D., Dong, Z., Shanmughapriya, S., Koch, D. A., Thomas, T., Hoffman, N. E., Timbalia, S. A., Goldman, S. J., Breves, S. L., Corbally, D. P., Nemani, N., Fairweather, J. P., Cutri, A. R., Zhang, X., Song, J., Jaña, F., Huang, J., Barrero, C., Rabinowitz, J. E., Luongo, T. S., Schumacher, S. M., Rockman, M. E., Dietrich, A., Merali, S., Caplan, J., Stathopulos, P., Ahima, R. S., Cheung, J. Y., Houser, S. R., Koch, W. J., Patel, V., Gohil, V. M., Elrod, J. W., Rajan, S., & Madesh, M.
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2016-05
- Volume
- 15
- Issue
- 8
- Pages
- 1673-1685
- ISSN
- 2211-1247 (ISSN-L)
- OpenAlex
- W2363363069
- Cited by
- 210
- References
- 8
- FWCI
- 11.89
- Type
- journal article
- Language
- en
- Open access
- gold
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