Please note this is a comparison between Version 2 by Conner Chen and Version 1 by Ashley Pitt.
Mitochondria rely on the translocase of the outer membrane (TOM) complex for the bulk of mitochondrial protein import. In addition to its role as the major entry point for mitochondrial proteins, the TOM complex serves as an entry pathway for viral proteins. TOM complex subunits also participate in a host of interactions that have been studied extensively for their function in neurodegenerative diseases, cardiovascular diseases, innate immunity, cancer, metabolism, mitophagy and autophagy.
mitochondrial quality control
mitochondrial cell signaling
TOM subunits
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References
Chacinska, A.; Koehler, C.M.; Milenkovic, D.; Lithgow, T.; Pfanner, N. Importing Mitochondrial Proteins: Machineries and Mechanisms. Cell 2009, 138, 628–644.
Lotz, C.; Lin, A.J.; Black, C.M.; Zhang, J.; Lau, E.; Deng, N.; Wang, Y.; Zong, N.C.; Choi, J.H.; Xu, T.; et al. Characterization, Design, and Function of the Mitochondrial Proteome: From Organs to Organisms. J. Proteome Res. 2014, 13, 433–446.
Gottschalk, W.K.; Lutz, M.W.; He, Y.T.; Saunders, A.M.; Burns, D.K.; Roses, A.D.; Chiba-Falek, O. The Broad Impact of TOM40 on Neurodegenerative Diseases in Aging. J. Parkinsons Dis. Alzheimers Dis. 2014, 1, 1.
Cotter, D. MitoProteome: Mitochondrial protein sequence database and annotation system. Nucleic Acids Res. 2004, 32, 463D–467D.
Pérez-Treviño, P.; Velásquez, M.; García, N. Mechanisms of mitochondrial DNA escape and its relationship with different metabolic diseases. Biochim. Biophys. Acta (BBA) Mol. Basis Dis. 2020, 1866, 165761.
Martincová, E.; Voleman, L.; Pyrih, J.; Zarsky, V.; Vondráčková, P.; Kolisko, M.; Tachezy, J.; Doležal, P. Probing the Biology of Giardia intestinalis Mitosomes UsingIn VivoEnzymatic Tagging. Mol. Cell. Biol. 2015, 35, 2864–2874.
Taylor, R.D.; McHale, B.J.; Nargang, F.E. Characterization of Neurospora crassa Tom40-deficient Mutants and Effect of Specific Mutations on Tom40 Assembly. J. Biol. Chem. 2003, 278, 765–775.
Kinoshita, J.-Y.; Mihara, K.; Oka, T. Identification and Characterization of a New Tom40 Isoform, a Central Component of Mitochondrial Outer Membrane Translocase. J. Biochem. 2007, 141, 897–906.
Mager, F.; Gessmann, D.; Nussberger, S.; Zeth, K. Functional Refolding and Characterization of Two Tom40 Isoforms from Human Mitochondria. J. Membr. Biol. 2011, 242, 11–21.
Wiedemann, N.; Pfanner, N.; Ryan, M.T. The three modules of ADP/ATP carrier cooperate in receptor recruitment and translocation into mitochondria. EMBO J. 2001, 20, 951–960.
Yoshizumi, T.; Ichinohe, T.; Sasaki, O.; Otera, H.; Kawabata, S.-I.; Mihara, K.; Koshiba, T. Influenza A virus protein PB1-F2 translocates into mitochondria via Tom40 channels and impairs innate immunity. Nat. Commun. 2014, 5, 4713.
Loo, Y.-M.; Gale, M. Immune Signaling by RIG-I-like Receptors. Immunity 2011, 34, 680–692.
Zara, V.; Ferramosca, A.; Günnewig, K.; Kreimendahl, S.; Schwichtenberg, J.; Sträter, D.; Çakar, M.; Emmrich, K.; Guidato, P.; Palmieri, F.; et al. Mimivirus-Encoded Nucleotide Translocator VMC1 Targets the Mitochondrial Inner Membrane. J. Mol. Biol. 2018, 430, 5233–5245.
Valverde, D.P.; Yu, S.; Boggavarapu, V.; Kumar, N.; Lees, J.A.; Walz, T.; Reinisch, K.M.; Melia, T.J. ATG2 transports lipids to promote autophagosome biogenesis. J. Cell Biol. 2019, 218, 1787–1798.
Bender, A.; Desplats, P.; Spencer, B.; Rockenstein, E.; Adame, A.; Elstner, M.; Laub, C.; Mueller, S.; Koob, A.O.; Mante, M.; et al. TOM40 Mediates Mitochondrial Dysfunction Induced by α-Synuclein Accumulation in Parkinson’s Disease. PLoS ONE 2013, 8, e62277.
Wang, Y.; Zhang, S.; Li, F.; Zhou, Y.; Zhang, Y.; Wang, Z.; Zhang, R.; Zhu, J.; Ren, Y.; Tan, Y.; et al. Therapeutic target database 2020: Enriched resource for facilitating research and early development of targeted therapeutics. Nucleic Acids Res. 2019, 48, D1031–D1041.
Yang, W.; Shin, H.-Y.; Cho, H.; Chung, J.-Y.; Lee, E.-J.; Kim, J.-H.; Kang, E.-S. TOM40 Inhibits Ovarian Cancer Cell Growth by Modulating Mitochondrial Function Including Intracellular ATP and ROS Levels. Cancers 2020, 12, 1329.
Bellot, G.; Cartron, P.-F.; Er, E.; Oliver, L.; Juin, P.; Armstrong, L.C.; Bornstein, P.; Mihara, K.; Manon, S.; Vallette, F.M. TOM22, a core component of the mitochondria outer membrane protein translocation pore, is a mitochondrial receptor for the proapoptotic protein Bax. Cell Death Differ. 2006, 14, 785–794.
Curado, S.; Ober, E.A.; Walsh, S.; Cortes-Hernandez, P.; Verkade, H.; Koehler, C.M.; Stainier, D.Y.R. The mitochondrial import gene tomm22 is specifically required for hepatocyte survival and provides a liver regeneration model. Dis. Model. Mech. 2010, 3, 486–495.
Rajapaksha, M.; Kaur, J.; Prasad, M.; Pawlak, K.J.; Marshall, B.; Perry, E.W.; Whittal, R.M.; Bose, H.S. An Outer Mitochondrial Translocase, Tom22, Is Crucial for Inner Mitochondrial Steroidogenic Regulation in Adrenal and Gonadal Tissues. Mol. Cell. Biol. 2016, 36, 1032–1047.
Fukasawa, Y.; Tsuji, J.; Fu, S.-C.; Tomii, K.; Horton, P.; Imai, K. MitoFates: Improved Prediction of Mitochondrial Targeting Sequences and Their Cleavage Sites*. Mol. Cell. Proteom. 2015, 14, 1113–1126.
Liu, Z.; Ding, Y.; Ye, N.; Wild, C.; Chen, H.; Zhou, J. Direct Activation of Bax Protein for Cancer Therapy. Med. Res. Rev. 2016, 36, 313–341.
Cartron, P.-F.; Bellot, G.; Oliver, L.; Grandier-Vazeille, X.; Manon, S.; Vallette, F.M. Bax inserts into the mitochondrial outer membrane by different mechanisms. FEBS Lett. 2008, 582, 3045–3051.
Grosse, L.; Wurm, A.C.; Bruser, C.; Neumann, D.C.J.; Jakobs, S. Bax assembles into large ring-like structures remodeling the mitochondrial outer membrane in apoptosis. EMBO J. 2016, 35, 402–413.
Renault, T.T.; Grandier-Vazeille, X.; Arokium, H.; Velours, G.; Camougrand, N.; Priault, M.; Teijido, O.; Dejean, L.M.; Manon, S. The cytosolic domain of human Tom22 modulates human Bax mitochondrial translocation and conformation in yeast. FEBS Lett. 2012, 586, 116–121.
Rumlová, M.; Křížová, I.; Keprová, A.; Hadravová, R.; Doležal, M.; Strohalmová, K.; Pichová, I.; Hájek, M.; Ruml, T. HIV-1 protease-induced apoptosis. Retrovirology 2014, 11, 37.
Veresov, V.G.; Davidovskii, A.I. Structural insights into proapoptotic signaling mediated by MTCH2, VDAC2, TOM40 and TOM22. Cell. Signal. 2014, 26, 370–382.
Feng, L.; Zhang, D.; Fan, C.; Ma, C.; Yang, W.; Meng, Y.; Wu, W.; Guan, S.; Jiang, B.; Yang, M.; et al. ER stress-mediated apoptosis induced by celastrol in cancer cells and important role of glycogen synthase kinase-3beta in the signal network. Cell Death Dis. 2013, 4, e715.
Zeng, Y.; Pan, Q.; Wang, X.; Li, N.; Lin, Y.; Man, F.; Xiao, F.; Guo, L. Impaired Mitochondrial Fusion and Oxidative Phosphorylation Triggered by High Glucose Is Mediated by Tom22 in Endothelial Cells. Oxidative Med. Cell. Longev. 2019, 2019, 4508762.
Siemen, D.; Loupatatzisa, C.; Boreckyb, J.; Gulbinsa, E.; Langa, F. Ca2+-Activated K Channel of the BK-Type in the Inner Mitochondrial Membrane of a Human Glioma Cell Line. Biochem. Biophys. Res. Commun. 1999, 257, 549–554.
Zhang, J.; Li, M.; Zhang, Z.; Zhu, R.; Olcese, R.; Stefani, E.; Toro, L. The mitochondrial BKCa channel cardiac interactome reveals BKCa association with the mitochondrial import receptor subunit Tom22, and the adenine nucleotide translocator. Mitochondrion 2017, 33, 84–101.
Sokol, A.M.; Sztolsztener, M.E.; Wasilewski, M.; Heinz, E.; Chacinska, A. Mitochondrial protein translocases for survival and wellbeing. FEBS Lett. 2014, 588, 2484–2495.
Bajaj, R.; Jaremko, Ł.; Jaremko, M.; Becker, S.; Zweckstetter, M. Molecular Basis of the Dynamic Structure of the TIM23 Complex in the Mitochondrial Intermembrane Space. Structure 2014, 22, 1501–1511.
Waegemann, K.; Popov-Čeleketić, D.; Neupert, W.; Azem, A.; Mokranjac, D. Cooperation of TOM and TIM23 Complexes during Translocation of Proteins into Mitochondria. J. Mol. Biol. 2015, 427, 1075–1084.
Qian, X.; Gebert, M.; Höpker, J.; Yan, M.; Li, J.; Wiedemann, N.; Van Der Laan, M.; Pfanner, N.; Sha, B. Structural Basis for the Function of Tim50 in the Mitochondrial Presequence Translocase. J. Mol. Biol. 2011, 411, 513–519.
Bose, H.S.; Whittal, R.M.; Marshall, B.; Rajapaksha, M.; Wang, N.P.; Bose, M.; Perry, E.W.; Zhao, Z.-O.; Miller, W.L. A novel mitochondrial complex of P450c11AS, StAR and Tom22 synthesizes aldosterone in the rat heart. J. Pharmacol. Exp. Ther. 2021.
Lazarou, M.; Jin, S.M.; Kane, L.A.; Youle, R.J. Role of PINK1 Binding to the TOM Complex and Alternate Intracellular Membranes in Recruitment and Activation of the E3 Ligase Parkin. Dev. Cell 2012, 22, 320–333.
Fiesel, F.C.; Caulfield, T.R.; Moussaud-Lamodière, E.L.; Ogaki, K.; Dourado, D.F.; Flores, S.C.; Ross, O.A.; Springer, W. Structural and Functional Impact of Parkinson Disease-Associated Mutations in the E3 Ubiquitin Ligase Parkin. Hum. Mutat. 2015, 36, 774–786.
Geisler, S.; Holmström, K.M.; Treis, A.; Skujat, D.; Weber, S.S.; Fiesel, F.C.; Kahle, P.J.; Springer, W. The PINK1/Parkin-mediated mitophagy is compromised by PD-associated mutations. Autophagy 2010, 6, 871–878.
Jacoupy, M.; Hamon-Keromen, E.; Ordureau, A.; Erpapazoglou, Z.; Coge, F.; Corvol, J.-C.; Nosjean, O.; La Cour, C.M.; Millan, M.J.; Boutin, J.A.; et al. The PINK1 kinase-driven ubiquitin ligase Parkin promotes mitochondrial protein import through the presequence pathway in living cells. Sci. Rep. 2019, 9, 1–15.
Wu, X.; Li, L.; Jiang, H. Mitochondrial inner-membrane protease Yme1 degrades outer-membrane proteins Tom22 and Om45. J. Cell Biol. 2017, 217, 139–149.
Schmidt, O.; Harbauer, A.B.; Rao, S.; Eyrich, B.; Zahedi, R.P.; Stojanovski, D.; Schönfisch, B.; Guiard, B.; Sickmann, A.; Pfanner, N.; et al. Regulation of Mitochondrial Protein Import by Cytosolic Kinases. Cell 2011, 144, 227–239.
Kravic, B.; Harbauer, A.B.; Romanello, V.; Simeone, L.; Vögtle, F.-N.; Kaiser, T.; Straubinger, M.; Huraskin, D.; Böttcher, M.; Cerqua, C.; et al. In mammalian skeletal muscle, phosphorylation of TOMM22 by protein kinase CSNK2/CK2 controls mitophagy. Autophagy 2018, 14, 311–335.
Horie, C.; Suzuki, H.; Sakaguchi, M.; Mihara, K. Targeting and Assembly of Mitochondrial Tail-anchored Protein Tom5 to the TOM Complex Depend on a Signal Distinct from That of Tail-anchored Proteins Dispersed in the Membrane. J. Biol. Chem. 2003, 278, 41462–41471.
Brandner, K.; Mick, D.U.; Frazier, A.E.; Taylor, R.D.; Meisinger, C.; Rehling, P. Taz1, an Outer Mitochondrial Membrane Protein, Affects Stability and Assembly of Inner Membrane Protein Complexes: Implications for Barth Syndrome. Mol. Biol. Cell 2005, 16, 5202–5214.
Becker, T.; Guiard, B.; Thornton, N.; Zufall, N.; Stroud, D.A.; Wiedemann, N.; Pfanner, N. Assembly of the mitochondrial protein import channel: Role of Tom5 in two-stage interaction of Tom40 with the SAM complex. Mol. Biol. Cell. 2010, 21, 3106–3113.
Kato, H.; Mihara, K. Identification of Tom5 and Tom6 in the preprotein translocase complex of human mitochondrial outer membrane. Biochem. Biophys. Res. Commun. 2008, 369, 958–963.
Dietmeier, K.; Hönlinger, A.; Bömer, U.; Dekker, P.J.T.; Eckerskorn, C.; Lottspeich, F.; Kübrich, M.; Pfanner, N. Tom5 functionally links mitochondrial preprotein receptors to the general import pore. Nat. Cell Biol. 1997, 388, 195–200.
Umemoto, T.; Asai, T.; Hirashima, K.; Shimizu, K.; Mihara, M.; Yamamoto, K.; Kubota, K.; Miyagawa, S.-I.; Oku, N. Proapoptotic Action of p53-Tom5 in p53-Resistant A549 Human Non-small Cell Lung Cancer Cells through Direct Mitochondrial Dysfunction. Biol. Pharm. Bull. 2011, 34, 551–554.
Dukanovic, J.; Dimmer, K.S.; Bonnefoy, N.; Krumpe, K.; Rapaport, D. Genetic and Functional Interactions between the Mitochondrial Outer Membrane Proteins Tom6 and Sam37. Mol. Cell. Biol. 2009, 29, 5975–5988.
Turcu, A.L.; Versini, A.; Khene, N.; Gaillet, C.; Cañeque, T.; Müller, S.; Rodriguez, R. DMT1 Inhibitors Kill Cancer Stem Cells by Blocking Lysosomal Iron Translocation. Chem. A Eur. J. 2020, 26, 7369–7373.
Wolff, N.A.; Ghio, A.J.; Garrick, L.M.; Garrick, M.D.; Zhao, L.A.; Fenton, R.; Thévenod, F. Evidence for mitochondrial localization of divalent metal transporter 1 (DMT1). FASEB J. 2014, 28, 2134–2145.
Johnston, A.J.; Hoogenraad, J.; Dougan, D.A.; Truscott, K.N.; Yano, M.; Mori, M.; Hoogenraad, N.J.; Ryan, M.T. Insertion and Assembly of Human Tom7 into the Preprotein Translocase Complex of the Outer Mitochondrial Membrane. J. Biol. Chem. 2002, 277, 42197–42204.
Sekine, S.; Wang, C.; Sideris, D.P.; Bunker, E.; Zhang, Z.; Youle, R.J. Reciprocal Roles of Tom7 and OMA1 during Mitochondrial Import and Activation of PINK1. Mol. Cell 2019, 73, 1028–1043.e5.
Okatsu, K.; Uno, M.; Koyano, F.; Go, E.; Kimura, M.; Oka, T.; Tanaka, K.; Matsuda, N. A Dimeric PINK1-containing Complex on Depolarized Mitochondria Stimulates Parkin Recruitment. J. Biol. Chem. 2013, 288, 36372–36384.
Zhang, C.; Wang, R.; Liu, Z.; Bunker, E.; Lee, S.; Giuntini, M.; Chapnick, D.; Liu, X. The plant triterpenoid celastrol blocks PINK1-dependent mitophagy by disrupting PINK1’s association with the mitochondrial protein TOM20. J. Biol. Chem. 2019, 294, 7472–7487.
Bertolin, G.; Ferrando-Miguel, R.; Jacoupy, M.; Traver, S.; Grenier, K.; Greene, A.W.; Dauphin, A.; Waharte, F.; Bayot, A.; Salamero, J.; et al. The TOMM machinery is a molecular switch in PINK1 and PARK2/PARKIN-dependent mitochondrial clearance. Autophagy 2013, 9, 1801–1817.
Kato, H.; Lu, Q.; Rapaport, D.; Kozjak-Pavlovic, V. Tom70 Is Essential for PINK1 Import into Mitochondria. PLoS ONE 2013, 8, e58435.
Freeman, B.C.; Morimoto, R.I. The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding. EMBO J. 1996, 15, 2969–2979.
Sarraf, S.A.; Raman, M.; Guarani-Pereira, V.; Sowa, M.E.; Huttlin, E.L.; Gygi, S.P.; Harper, J.W. Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization. Nat. Cell Biol. 2013, 496, 372–376.
Kotrasová, V.; Keresztesová, B.; Ondrovičová, G.; Bauer, J.; Havalová, H.; Pevala, V.; Kutejová, E.; Kunová, N. Mitochondrial Kinases and the Role of Mitochondrial Protein Phosphorylation in Health and Disease. Life 2021, 11, 82.
Zhang, M.; Yu, Q.; Liu, Z.; Liang, C.; Zhang, B.; Li, M. UBX domain-containing proteins are involved in lipid homeostasis and stress responses in Pichia pastoris. Int. J. Biochem. Cell Biol. 2017, 90, 136–144.
Frank, D.O.; Dengjel, J.; Wilfling, F.; Kozjak-Pavlovic, V.; Häcker, G.; Weber, A. The Pro-Apoptotic BH3-Only Protein Bim Interacts with Components of the Translocase of the Outer Mitochondrial Membrane (TOM). PLoS ONE 2015, 10, e0123341.
Takano, T.; Kohara, M.; Kasama, Y.; Nishimura, T.; Tsukiyama-Kohara, K.; Saito, M.; Kai, C. Translocase of outer mitochondrial membrane 70 expression is induced by hepatitis C virus and is related to the apoptotic response. J. Med. Virol. 2011, 83, 801–809.
Chou, C.-H.; Lee, R.-S.; Yang-Yen, H.-F. An Internal EELD Domain Facilitates Mitochondrial Targeting of Mcl-1 via a Tom70-dependent Pathway. Mol. Biol. Cell 2006, 17, 3952–3963.
Liu, X.-Y.; Wei, B.; Shi, H.-X.; Shan, Y.-F.; Wang, C. Tom70 mediates activation of interferon regulatory factor 3 on mitochondria. Cell Res. 2010, 20, 994–1011.
Wei, B.; Cui, Y.; Huang, Y.; Liu, H.; Li, L.; Li, M.; Ruan, K.-C.; Zhou, Q.; Wang, C. Tom70 Mediates Sendai Virus-Induced Apoptosis on Mitochondria. J. Virol. 2015, 89, 3804–3818.
Gordon, D.E.; Jang, G.M.; Bouhaddou, M.; Xu, J.; Obernier, K.; O’Meara, M.J.; Guo, J.Z.; Swaney, D.L.; Tummino, T.A.; Huettenhain, R.; et al. A SARS-CoV-2-Human Protein-Protein Interaction Map Reveals Drug Targets and Potential Drug-Repurposing. BioRxiv 2020.
Jiang, H.W.; Zhang, H.-N.; Meg, Q.-F.; Xie, J.; Li, Y.; Chen, H.; Zheng, Y.-X.; Wang, X.-N.; Qi, H.; Zhang, J.; et al. SARS-CoV-2 Orf9b suppresses type I interferon responses by targeting TOM70. Cell. Mol. Immunol. 2020, 17, 998–1000.
Hira, S.; Packialakshmi, B.; Tang, E.; Zhou, X. Dexamethasone upregulates mitochondrial Tom20, Tom70, and MnSOD through SGK1 in the kidney cells. J. Physiol. Biochem. 2021, 77, 1–11.
Recovery Collaborative Group; Horby, P.; Lim, W.S.; Emberson, J.R.; Mafham, M.; Bell, J.L.; Linsell, L.; Staplin, N.; Brightling, C.; Ustianowski, A.; et al. Dexamethasone in Hospitalized Patients with Covid-19. N. Engl. J. Med. 2021, 384, 693–704.
Filadi, R.; Leal, N.S.; Schreiner, B.; Rossi, A.; Dentoni, G.; Pinho, C.M.; Wiehager, B.; Cieri, D.; Calì, T.; Pizzo, P.; et al. TOM70 Sustains Cell Bioenergetics by Promoting IP3R3-Mediated ER to Mitochondria Ca2+ Transfer. Curr. Biol. 2018, 28, 369–382.
Bartok, A.; Weaver, D.; Golenár, T.; Nichtova, Z.; Katona, M.; Bánsághi, S.; Alzayady, K.J.; Thomas, V.K.; Ando, H.; Mikoshiba, K.; et al. IP3 receptor isoforms differently regulate ER-mitochondrial contacts and local calcium transfer. Nat. Commun. 2019, 10, 1–14.
Li, J.; Qi, M.; Li, C.; Shi, D.; Zhang, D.; Xie, D.; Yuan, T.; Feng, J.; Liu, Y.; Liang, D.; et al. Tom70 serves as a molecular switch to determine pathological cardiac hypertrophy. Cell Res. 2014, 24, 977–993.
Herkenne, S.; Ek, O.; Zamberlan, M.; Pellattiero, A.; Chergova, M.; Chivite, I.; Novotná, E.; Rigoni, G.; Fonseca, T.B.; Samardzic, D.; et al. Developmental and Tumor Angiogenesis Requires the Mitochondria-Shaping Protein Opa1. Cell Metab. 2020, 31, 987–1003.e8.
Wang, P.; Wang, D.; Yang, Y.; Hou, J.; Wan, J.; Ran, F.; Dai, X.; Zhou, P.; Yang, Y. Tom70 protects against diabetic cardiomyopathy through its antioxidant and antiapoptotic properties. Hypertens. Res. 2020, 43, 1047–1056.
Pei, H.; Yang, Y.; Zhao, H.; Li, X.; Yang, D.; Li, D.; Yang, Y. The Role of Mitochondrial Functional Proteins in ROS Production in Ischemic Heart Diseases. Oxidative Med. Cell. Longev. 2016, 2016, 1–8.
Xue, Q.; Pei, H.; Liu, Q.; Zhao, M.; Sun, J.; Gao, E.; Ma, X.; Tao, L. MICU1 protects against myocardial ischemia/reperfusion injury and its control by the importer receptor Tom70. Cell Death Dis. 2017, 8, e2923.
Boengler, K.; Gres, P.; Cabestrero, A.; Ruiz-Meana, M.; García-Dorado, D.; Heusch, G.; Schulz, R. Prevention of the ischemia-induced decrease in mitochondrial Tom20 content by ischemic preconditioning. J. Mol. Cell. Cardiol. 2006, 41, 426–430.
Di Maio, R.; Barrett, P.J.; Hoffman, E.K.; Barrett, C.W.; Zharikov, A.; Borah, A.; Hu, X.; McCoy, J.; Chu, C.T.; Burton, E.A.; et al. α-Synuclein binds to TOM20 and inhibits mitochondrial protein import in Parkinson’s disease. Sci. Transl. Med. 2016, 8, 342ra78.
De Miranda, B.R.; Rocha, E.M.; Castro, S.L.; Greenamyre, J.T. Protection from α-Synuclein induced dopaminergic neurodegeneration by overexpression of the mitochondrial import receptor TOM20. NPJ Park. Dis. 2020, 6, 1–10.
Domańska, G.; Motz, C.; Meinecke, M.; Harsman, A.; Papatheodorou, P.; Reljic, B.; Dian-Lothrop, E.A.; Galmiche, A.; Kepp, O.; Becker, L.; et al. Helicobacter pylori VacA Toxin/Subunit p34: Targeting of an Anion Channel to the Inner Mitochondrial Membrane. PLoS Pathog. 2010, 6, e1000878.
Kang, B.H.; Xia, F.; Pop, R.; Dohi, T.; Socolovsky, M.; Altieri, D.C. Developmental Control of Apoptosis by the Immunophilin Aryl Hydrocarbon Receptor-interacting Protein (AIP) Involves Mitochondrial Import of the Survivin Protein. J. Biol. Chem. 2011, 286, 16758–16767.