ArticleMolecular cell2015
SPG7 Is an Essential and Conserved Component of the Mitochondrial Permeability Transition Pore.
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Article in Molecular cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 121 papers, 3 of them syntheses that pooled it.
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121citing papers in PubMed, 3 pooled it
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121 citing papers in PubMed, 3 syntheses or guidelines pooled it, 198 citations in OpenAlex.
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- Phenotypic CRISPR screens identify NLRX1 as an essential activator of the human mitochondrial permeability transition.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The role of mitochondrial proteases in inflammation and immunity.Frontiers in immunology · 2026Review
- SPG7-Mediated Regulation of mPTP and Mitochondrial Flickering in COPD: A Bioinformatics-Based Prediction of Mechanistic Framework.International journal of chronic obstructive pulmonary disease · 2026Article
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- The Aging Substantia Nigra is Characterized by ROS Accumulation Potentially Resulting in Increased Neuroinflammation and Cytoskeletal Remodeling.Advanced biology · 2025Article
- The necroptosis-related lncRNA ENSG00000253385.1 promotes the progression of esophageal squamous cell carcinoma by targeting the miR-16-2-3p/VDAC1 axis.Scientific reports · 2025Article
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- Cross-link assisted spatial proteomics to map sub-organelle proteomes and membrane protein topologies.Nature communications · 2024Article
- Article
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Authors and funding
22 authors at 1 institution in 1 country.
Santhanam ShanmughapriyaDepartment of Biochemistry, Temple University School of Medicine, Philadelphia, PA 19140, USA; Center for Translational Medicine, Temple University School of Medicine, Philadelphia, PA 19140, USA.
Sudarsan RajanDepartment of Biochemistry, Temple University School of Medicine, Philadelphia, PA 19140, USA; Center for Translational Medicine, Temple University School of Medicine, Philadelphia, PA 19140, USA.
Nicholas E HoffmanDepartment of Biochemistry, Temple University School of Medicine, Philadelphia, PA 19140, USA; Center for Translational Medicine, Temple University School of Medicine, Philadelphia, PA 19140, USA.
Andrew M HigginsDepartment of Biochemistry, Temple University School of Medicine, Philadelphia, PA 19140, USA; Center for Translational Medicine, Temple University School of Medicine, Philadelphia, PA 19140, USA.
Dhanendra TomarDepartment of Biochemistry, Temple University School of Medicine, Philadelphia, PA 19140, USA; Center for Translational Medicine, Temple University School of Medicine, Philadelphia, PA 19140, USA.
Neeharika NemaniDepartment of Biochemistry, Temple University School of Medicine, Philadelphia, PA 19140, USA; Center for Translational Medicine, Temple University School of Medicine, Philadelphia, PA 19140, USA.
Kevin J HinesDepartment of Biochemistry, Temple University School of Medicine, Philadelphia, PA 19140, USA; Center for Translational Medicine, Temple University School of Medicine, Philadelphia, PA 19140, USA.
Dylan J SmithDepartment of Biochemistry, Temple University School of Medicine, Philadelphia, PA 19140, USA; Center for Translational Medicine, Temple University School of Medicine, Philadelphia, PA 19140, USA.
Akito EguchiDepartment of Biochemistry, Temple University School of Medicine, Philadelphia, PA 19140, USA; Center for Translational Medicine, Temple University School of Medicine, Philadelphia, PA 19140, USA.
Sandhya VallemDepartment of Biochemistry, Temple University School of Medicine, Philadelphia, PA 19140, USA; Center for Translational Medicine, Temple University School of Medicine, Philadelphia, PA 19140, USA.
Farah ShaikhDepartment of Biochemistry, Temple University School of Medicine, Philadelphia, PA 19140, USA; Center for Translational Medicine, Temple University School of Medicine, Philadelphia, PA 19140, USA.
Maggie CheungDepartment of Biochemistry, Temple University School of Medicine, Philadelphia, PA 19140, USA; Center for Translational Medicine, Temple University School of Medicine, Philadelphia, PA 19140, USA.
Nicole J LeonardDepartment of Biochemistry, Temple University School of Medicine, Philadelphia, PA 19140, USA; Center for Translational Medicine, Temple University School of Medicine, Philadelphia, PA 19140, USA.
Ryan S StolakisDepartment of Biochemistry, Temple University School of Medicine, Philadelphia, PA 19140, USA; Center for Translational Medicine, Temple University School of Medicine, Philadelphia, PA 19140, USA.
Matthew P WolfersDepartment of Biochemistry, Temple University School of Medicine, Philadelphia, PA 19140, USA; Center for Translational Medicine, Temple University School of Medicine, Philadelphia, PA 19140, USA.
Jessica IbettiCenter for Translational Medicine, Temple University School of Medicine, Philadelphia, PA 19140, USA; Department of Pharmacology, Temple University School of Medicine, Philadelphia, PA 19140, USA.
J Kurt ChuprunCenter for Translational Medicine, Temple University School of Medicine, Philadelphia, PA 19140, USA; Department of Pharmacology, Temple University School of Medicine, Philadelphia, PA 19140, USA.
Neelakshi R JogDepartment of Biochemistry, Temple University School of Medicine, Philadelphia, PA 19140, USA; Center for Translational Medicine, Temple University School of Medicine, Philadelphia, PA 19140, USA.
Steven R HouserCardiovascular Research Center, Temple University School of Medicine, Philadelphia, PA 19140, USA.
Walter J KochCenter for Translational Medicine, Temple University School of Medicine, Philadelphia, PA 19140, USA; Department of Pharmacology, Temple University School of Medicine, Philadelphia, PA 19140, USA.
John W ElrodCenter for Translational Medicine, Temple University School of Medicine, Philadelphia, PA 19140, USA; Department of Pharmacology, Temple University School of Medicine, Philadelphia, PA 19140, USA.
Muniswamy MadeshDepartment of Biochemistry, Temple University School of Medicine, Philadelphia, PA 19140, USA; Center for Translational Medicine, Temple University School of Medicine, Philadelphia, PA 19140, USA; Cardiovascular Research Center, Temple University School of Medicine, Philadelphia, PA 19140, USA. Electronic address: madeshm@temple.edu.
Temple University · US
Funding
Targeted Cancer Therapeutics and Heart Failure: Mechanisms and Post-injury RepairP01HL091799 · NHLBI · THOMAS JEFFERSON UNIVERSITY · PI KOCH, WALTER J. · 2008 to 2018
$23.1MProject 3 Dysregulation of metabolic communication of oligodendrocytes and neurons by cocaine and TatP01DA037830 · NIDA · TEMPLE UNIV OF THE COMMONWEALTH · PI KHALILI, KAMEL · 2015 to 2019
$7.4MCoordination of Pathophysiologic Endothelial Cell Signaling by ROSR01HL086699 · NHLBI · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI MUNISWAMY, MADESH · 2008 to 2018
$4.3MSpectral revelations of mitochondrial Ca2+ flux interactomeR01GM109882 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI MUNISWAMY, MADESH · 2014 to 2022
$3.3MMechanisms of mitochondrial calcium exchange in heart failureR01HL123966 · NHLBI · TEMPLE UNIV OF THE COMMONWEALTH · PI ELROD, JOHN WILLIAM · 2014 to 2018
$2.3MInhibition of MCUR1-MCU mediated mitochondrial Ca2+ uptake prevents I/R injuryR01HL119306 · NHLBI · TEMPLE UNIV OF THE COMMONWEALTH · PI MUNISWAMY, MADESH · 2014 to 2017
$1.6MMultiphoton Confocal Microscopy for Biomedical ResearchS10RR027327 · NCRR · TEMPLE UNIV OF THE COMMONWEALTH · PI MUNISWAMY, MADESH · 2010 to 2010
$500kNCRR NIH HHS 1S10RR027327NCRR NIH HHS S10 RR027327NHLBI NIH HHS P01 HL091799NHLBI NIH HHS R01 HL086699NHLBI NIH HHS R01HL086699NHLBI NIH HHS R01 HL119306NHLBI NIH HHS R01HL119306NHLBI NIH HHS R01 HL123966NIDA NIH HHS P01 DA037830NIGMS NIH HHS R01 GM109882NIGMS NIH HHS R01GM109882
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.
Indexed as
ATPases Associated with Diverse Cellular ActivitiesBinding SitesCalciumCell DeathCyclophilinsHEK293 CellsHeLa CellsHumansMembrane Potential, MitochondrialMetalloendopeptidasesMitochondriaMitochondrial MembranesPeptidyl-Prolyl Isomerase DReactive Oxygen SpeciesRNA InterferenceVoltage-Dependent Anion Channel 1ATPases Associated with Diverse Cellular ActivitiesCalciumCyclophilinsMetalloendopeptidasesPeptidyl-Prolyl Isomerase DPPID protein, humanReactive Oxygen SpeciesSPG7 protein, humanVDAC1 protein, humanVoltage-Dependent Anion Channel 1
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