Cited by 209Mitochondrial Function and PathologyCell death mechanisms and regulationATP Synthase and ATPases Research

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SPG7 Is an Essential and Conserved Component of the Mitochondrial Permeability Transition Pore

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Shanmughapriya, Santhanam, Rajan, Sudarsan, Hoffman, Nicholas E., Higgins, Andrew M., Tomar, Dhanendra, Nemani, Neeharika, Hines, Kevin J., Smith, Dylan J., Eguchi, Akito, Vallem, Sandhya, Shaikh, Farah, Cheung, Maggie, Leonard, Nicole J., Stolakis, Ryan S., Wolfers, Matthew P., Ibetti, Jessica, Chuprun, J. Kurt, Jog, Neelakshi R., Houser, Steven R., Koch, Walter J., Elrod, John W., Madesh, Muniswamy·2015·Molecular Cell

DOI 10.1016/j.molcel.2015.08.009PMC PMC4592475

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Abstract

Mitochondrial permeability transition is a phenomenon in which the mitochondrial permeability transition pore (PTP) abruptly opens, resulting in mitochondrial membrane potential (ΔΨm) dissipation, loss of ATP production, and cell death. Several genetic candidates have been proposed to form the PTP complex, however, the core component is unknown. We identified a necessary and conserved role for spastic paraplegia 7 (SPG7) in Ca(2+)- and ROS-induced PTP opening using RNAi-based screening. Loss of SPG7 resulted in higher mitochondrial Ca(2+) retention, similar to cyclophilin D (CypD, PPIF) knockdown with sustained ΔΨm during both Ca(2+) and ROS stress. Biochemical analyses revealed that the PTP is a heterooligomeric complex composed of VDAC, SPG7, and CypD. Silencing or disruption of SPG7-CypD binding prevented Ca(2+)- and ROS-induced ΔΨm depolarization and cell death. This study identifies an ubiquitously expressed IMM integral protein, SPG7, as a core component of the PTP at the OMM and IMM contact site.

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Bootman, M. D., Missiaen, L., Parys, J. B., SMEDT, H. D., & Casteels, R. (1995) · Biochemical Journal · doi:10.1042/bj3060445 · Cited by 5,131
Mitochondrial membrane permeabilization in cell death
Kroemer, G., Galluzzi, L., & Brenner, C. (2007) · Physiological Reviews · doi:10.1152/physrev.00013.2006 · Cited by 3,598
Mitochondria and cell death: outer membrane permeabilization and beyond
Tait, S. W. G., & Green, D. R. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2952 · Cited by 2,593
The mitochondrial permeability transition pore and its role in cell death
CROMPTON, M. (1999) · Biochemical Journal · doi:10.1042/bj3410233 · Cited by 2,432
Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death
Baines, C. P., Kaiser, R. A., Purcell, N. H., Blair, N. S., Osinska, H., Hambleton, M. A., Brunskill, E. W., Sayen, M. R., Gottlieb, R. A., Dorn, G. W., et al. (2005) · Nature · doi:10.1038/nature03434 · Cited by 2,280
A Mitochondrial Protein Compendium Elucidates Complex I Disease Biology
Pagliarini, D. J., Calvo, S. E., Chang, B., Sheth, S. A., Vafai, S. B., Ong, S.-E., Walford, G. A., Sugiana, C., Boneh, A., Chen, W. K., et al. (2008) · Cell · doi:10.1016/j.cell.2008.06.016 · Cited by 1,994
Dynamin-related Protein Drp1 Is Required for Mitochondrial Division in Mammalian Cells
Smirnova, E., Griparić, L., Shurland, D., & van der Bliek, A. M. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.8.2245 · Cited by 1,938
The Role of Dynamin-Related Protein 1, a Mediator of Mitochondrial Fission, in Apoptosis
Frank, S., Gaume, B., Bergmann-Leitner, E. S., Leitner, W. W., Robert, E. G., Catez, F., Smith, C. L., & Youle, R. J. (2001) · Developmental Cell · doi:10.1016/s1534-5807(01)00055-7 · Cited by 1,755
Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death
Nakagawa, T., Shimizu, S., Watanabe, T., Yamaguchi, O., Otsu, K., Yamagata, H., Inohara, H., Kubo, T., & Tsujimoto, Y. (2005) · Nature · doi:10.1038/nature03317 · Cited by 1,635
Mitochondrial Transport of Cations: Channels, Exchangers, and Permeability Transition
Bernardi, P. (1999) · Physiological Reviews · doi:10.1152/physrev.1999.79.4.1127 · Cited by 1,546

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Zhang, W., Li, G., Luo, R., Lei, J., Song, Y., Wang, B., Ma, L., Liao, Z., Ke, W., Liu, H., et al. (2022) · Experimental & Molecular Medicine · doi:10.1038/s12276-022-00729-9 · Cited by 338
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Authors: Shanmughapriya, S., Rajan, S., Hoffman, N. E., Higgins, A. M., Tomar, D., Nemani, N., Hines, K. J., Smith, D. J., Eguchi, A., Vallem, S., Shaikh, F., Cheung, M., Leonard, N. J., Stolakis, R. S., Wolfers, M. P., Ibetti, J., Chuprun, J. K., Jog, N. R., Houser, S. R., Koch, W. J., Elrod, J. W., & Madesh, M.
Affiliations: Temple University (US)
Corresponding author: Madesh, Muniswamy
ORCID: Shanmughapriya, Santhanam
Rajan, Sudarsan
Higgins, Andrew M.
Tomar, Dhanendra
Nemani, Neeharika
Eguchi, Akito
Leonard, Nicole J.
Ibetti, Jessica
Chuprun, J. Kurt
Jog, Neelakshi R.
Houser, Steven R.
Koch, Walter J.
Elrod, John W.
Madesh, Muniswamy
Venue: Molecular Cell
Publisher: Elsevier BV
Published: 2015-10
Volume: 60
Issue: 1
Pages: 47-62
ISSN: 1097-2765 (ISSN-L)
DOI: 10.1016/j.molcel.2015.08.009
PMC: PMC4592475
OpenAlex: W1895235630
Cited by: 209
References: 49
Citations by year: 2026: 12 · 2025: 15 · 2024: 10 · 2023: 17 · 2022: 20 · 2021: 13 · 2020: 25 · 2019: 23 · 2018: 26 · 2017: 22 · 2016: 24 · 2015: 1
FWCI: 10.56
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 366 d)
Locations: Molecular Cell (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health (1S10RR027327, R01GM109882, R01HL086699, R01HL119306)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
Keywords: SPG7, mitochondrial permeability transition pore, mitochondrial permeability transition, cyclophilin D, voltage-dependent anion channel, mitochondrial membrane potential, reactive oxygen species, mitochondrial depolarization, cell death, inner membrane, outer membrane, RNAi screening
MeSH terms: ATPases Associated with Diverse Cellular Activities, Peptidyl-Prolyl Isomerase D, Binding Sites, Calcium, HeLa Cells, Humans, Metalloendopeptidases, Mitochondria, Cell Death, Reactive Oxygen Species, Cyclophilins, RNA Interference, Voltage-Dependent Anion Channel 1, Mitochondrial Membranes, Membrane Potential, Mitochondrial, HEK293 Cells

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SPG7 Is an Essential and Conserved Component of the Mitochondrial Permeability Transition Pore

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