{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,30]],"date-time":"2026-07-30T13:38:49Z","timestamp":1785418729193,"version":"3.56.0"},"reference-count":175,"publisher":"MDPI AG","issue":"13","license":[{"start":{"date-parts":[[2026,6,26]],"date-time":"2026-06-26T00:00:00Z","timestamp":1782432000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100015326","name":"Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health","doi-asserted-by":"publisher","award":["ZIA HD000072"],"award-info":[{"award-number":["ZIA HD000072"]}],"id":[{"id":"10.13039\/100015326","id-type":"DOI","asserted-by":"publisher"}]},{"award":["ZIA HD000072"],"award-info":[{"award-number":["ZIA HD000072"]}],"id":[{"id":"https:\/\/ror.org\/04byxyr05","id-type":"ROR","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>The voltage-dependent anion channel (VDAC) is the primary conduit for ion and metabolite transport across the mitochondrial outer membrane. Positioned at the interface between the cytosol and the mitochondrial compartment, VDAC is uniquely accessible to proteins on both sides of the membrane, making it an interaction hub whose biophysical properties and signaling functions are shaped by protein complexation in addition to its intrinsic pore specialization. Mammals express three isoforms\u2014VDAC1, VDAC2, and VDAC3\u2014sharing a conserved \u03b2-barrel scaffold with about 70% identity. However, minor differences in the sequence lead to drastic changes in VDAC isoform affinity with other proteins. Here, we review the molecular mechanisms and physiological consequences of VDAC complexation with a set of well-characterized partners: hexokinase, dimeric tubulin, \u03b1-synuclein, mitochondria-associated membrane proteins, B-cell lymphoma 2 (BCL-2) family proteins, and the translocase of the outer membrane (TOM) protein import complex. For each complex, we evaluate the available structural, biophysical, and genetic evidence for isoform specificity, highlight where mechanistic understanding is most advanced, and identify open questions. A consistent principle emerges across all complexes: functionally nonredundant isoform contributions are primarily governed by differential partner affinity and complexation, rather than by differences in pore architecture alone. This framework has direct implications for mitochondria-associated pathologies, including cancer, cardiovascular disease, and neurodegeneration, as well as for the rational design of VDAC-targeting therapeutics.<\/jats:p>","DOI":"10.3390\/ijms27135804","type":"journal-article","created":{"date-parts":[[2026,6,30]],"date-time":"2026-06-30T00:55:11Z","timestamp":1782780911000},"page":"5804","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Mitochondrial Voltage-Dependent Anion Channel: From a Passive Pore to a Cellular Hub Through Protein Complexation"],"prefix":"10.3390","volume":"27","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-8078-4738","authenticated-orcid":false,"given":"Megha","family":"Rajendran","sequence":"first","affiliation":[{"name":"<i>Eunice Kennedy Shriver<\/i> National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sergey M.","family":"Bezrukov","sequence":"additional","affiliation":[{"name":"<i>Eunice Kennedy Shriver<\/i> National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tatiana K.","family":"Rostovtseva","sequence":"additional","affiliation":[{"name":"<i>Eunice Kennedy Shriver<\/i> National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,6,26]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1006\/jsbi.1997.3954","article-title":"Conformational changes in the mitochondrial channel protein, VDAC, and their functional implications","volume":"121","author":"Mannella","year":"1998","journal-title":"J. Struct. Biol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1466","DOI":"10.1016\/j.bbamem.2011.10.005","article-title":"VDAC isoforms in mammals","volume":"1818","author":"Messina","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1219","DOI":"10.1016\/j.bbabio.2016.02.020","article-title":"Role of cysteines in mammalian VDAC isoforms\u2019 function","volume":"1857","author":"Reina","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"15370","DOI":"10.1073\/pnas.0808115105","article-title":"Structure of the human voltage-dependent anion channel","volume":"105","author":"Bayrhuber","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"1206","DOI":"10.1126\/science.1161302","article-title":"Solution structure of the integral human membrane protein VDAC-1 in detergent micelles","volume":"321","author":"Hiller","year":"2008","journal-title":"Science"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"17742","DOI":"10.1073\/pnas.0809634105","article-title":"The crystal structure of mouse VDAC1 at 2.3 A resolution reveals mechanistic insights into metabolite gating","volume":"105","author":"Ujwal","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1126\/science.adu6445","article-title":"Structure of human PINK1 at a mitochondrial TOM-VDAC array","volume":"388","author":"Callegari","year":"2025","journal-title":"Science"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1038\/s41592-022-01488-1","article-title":"ColabFold: Making protein folding accessible to all","volume":"19","author":"Mirdita","year":"2022","journal-title":"Nat. Methods"},{"key":"ref_9","doi-asserted-by":"crossref","unstructured":"Razeto, A., Gribbon, P., and Loew, C. (wwPDB, 2019). The dynamic nature of the VDAC1 channels in bilayers: Human VDAC1 at 2.7 Angstrom resolution, wwPDB, to be published.","DOI":"10.2210\/pdb6g6u\/pdb"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1007\/BF01869662","article-title":"Reconstitution in planar lipid bilayers of a voltage-dependent anion-selective channel obtained from paramecium mitochondria","volume":"30","author":"Schein","year":"1976","journal-title":"J. Membr. Biol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1038\/279643a0","article-title":"A candidate for the permeability pathway of the outer mitochondrial membrane","volume":"279","author":"Colombini","year":"1979","journal-title":"Nature"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"2243","DOI":"10.1073\/pnas.80.8.2243","article-title":"Structural and functional evidence for multiple channel complexes in the outer membrane of Neurospora crassa mitochondria","volume":"80","author":"Mannella","year":"1983","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"28006","DOI":"10.1074\/jbc.271.45.28006","article-title":"ATP flux is controlled by a voltage-gated channel from the mitochondrial outer membrane","volume":"271","author":"Rostovtseva","year":"1996","journal-title":"J. Biol. Chem."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1023\/B:MCBI.0000009862.17396.8d","article-title":"VDAC: The channel at the interface between mitochondria and the cytosol","volume":"256\u2013257","author":"Colombini","year":"2004","journal-title":"Mol. Cell. Biochem."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/j.bbadis.2005.10.006","article-title":"Voltage-dependent anion channel (VDAC) as mitochondrial governator\u2014Thinking outside the box","volume":"1762","author":"Lemasters","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_16","doi-asserted-by":"crossref","unstructured":"Mannella, C.A. (2021). VDAC\u2014A Primal Perspective. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22041685"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1667","DOI":"10.1074\/mcp.T600009-MCP200","article-title":"Hunting interactomes of a membrane protein: Obtaining the largest set of voltage-dependent anion channel-interacting protein epitopes","volume":"5","author":"Roman","year":"2006","journal-title":"Mol. Cell. Proteom."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"19414","DOI":"10.1074\/jbc.M101590200","article-title":"Bcl-xL promotes the open configuration of the voltage-dependent anion channel and metabolite passage through the outer mitochondrial membrane","volume":"276","author":"Li","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1126\/science.1083995","article-title":"VDAC2 inhibits BAK activation and mitochondrial apoptosis","volume":"301","author":"Cheng","year":"2003","journal-title":"Science"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"13575","DOI":"10.1074\/jbc.M310593200","article-title":"Bid, but not Bax, regulates VDAC channels","volume":"279","author":"Rostovtseva","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"E5590","DOI":"10.1073\/pnas.1510574112","article-title":"Motifs of VDAC2 required for mitochondrial Bak import and tBid-induced apoptosis","volume":"112","author":"Naghdi","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"4976","DOI":"10.1038\/s41467-018-07309-4","article-title":"VDAC2 enables BAX to mediate apoptosis and limit tumor development","volume":"9","author":"Chin","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"10545","DOI":"10.1158\/0008-5472.CAN-05-1925","article-title":"Activation of glycogen synthase kinase 3beta disrupts the binding of hexokinase II to mitochondria by phosphorylating voltage-dependent anion channel and potentiates chemotherapy-induced cytotoxicity","volume":"65","author":"Pastorino","year":"2005","journal-title":"Cancer Res."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"3946","DOI":"10.1074\/jbc.M803614200","article-title":"Voltage-dependent anion channel 1-based peptides interact with hexokinase to prevent its anti-apoptotic activity","volume":"284","author":"Arzoine","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_25","doi-asserted-by":"crossref","unstructured":"Sheldon, K.L., Maldonado, E.N., Lemasters, J.J., Rostovtseva, T.K., and Bezrukov, S.M. (2011). Phosphorylation of voltage-dependent anion channel by serine\/threonine kinases governs its interaction with tubulin. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0025539"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"4946","DOI":"10.1016\/S0021-9258(18)50541-X","article-title":"Purification of a hexokinase-binding protein from the outer mitochondrial membrane","volume":"254","author":"Felgner","year":"1979","journal-title":"J. Biol. Chem."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"e2110996118","DOI":"10.1073\/pnas.2110996118","article-title":"In-cell structures of conserved supramolecular protein arrays at the mitochondria-cytoskeleton interface in mammalian sperm","volume":"118","author":"Leung","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"113728","DOI":"10.1016\/j.bcp.2019.113728","article-title":"JNK activation and translocation to mitochondria mediates mitochondrial dysfunction and cell death induced by VDAC opening and sorafenib in hepatocarcinoma cells","volume":"171","author":"Heslop","year":"2020","journal-title":"Biochem. Pharmacol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1007\/s002320010060","article-title":"Actin modulates the gating of Neurospora crassa VDAC","volume":"180","author":"Xu","year":"2001","journal-title":"J. Membr. Biol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"18746","DOI":"10.1073\/pnas.0806303105","article-title":"Tubulin binding blocks mitochondrial voltage-dependent anion channel and regulates respiration","volume":"105","author":"Rostovtseva","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"E2905","DOI":"10.1073\/pnas.1402544111","article-title":"Impaired functional communication between the L-type calcium channel and mitochondria contributes to metabolic inhibition in the mdx heart","volume":"111","author":"Viola","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"18467","DOI":"10.1074\/jbc.M115.641746","article-title":"alpha-Synuclein Shows High Affinity Interaction with Voltage-dependent Anion Channel, Suggesting Mechanisms of Mitochondrial Regulation and Toxicity in Parkinson Disease","volume":"290","author":"Rostovtseva","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"34802","DOI":"10.1038\/srep34802","article-title":"Hexokinase I N-terminal based peptide prevents the VDAC1-SOD1 G93A interaction and re-establishes ALS cell viability","volume":"6","author":"Magri","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"5131","DOI":"10.1093\/hmg\/dds360","article-title":"Abnormal interaction of VDAC1 with amyloid beta and phosphorylated tau causes mitochondrial dysfunction in Alzheimer\u2019s disease","volume":"21","author":"Manczak","year":"2012","journal-title":"Hum. Mol. Genet."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"3170","DOI":"10.1073\/pnas.89.8.3170","article-title":"Isolation of the mitochondrial benzodiazepine receptor: Association with the voltage-dependent anion channel and the adenine nucleotide carrier","volume":"89","author":"McEnery","year":"1992","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"2466","DOI":"10.1039\/C7MB00434F","article-title":"Protein-protein interaction networks as a new perspective to evaluate distinct functional roles of voltage-dependent anion channel isoforms","volume":"13","author":"Caterino","year":"2017","journal-title":"Mol. Biosyst."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"2049","DOI":"10.1242\/jeb.00241","article-title":"Isozymes of mammalian hexokinase: Structure, subcellular localization and metabolic function","volume":"206","author":"Wilson","year":"2003","journal-title":"J. Exp. Biol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1016\/S0021-9258(19)52639-4","article-title":"The Association of Hexokinase with Particulate Fractions of Brain and Other Tissue Homogenates","volume":"203","author":"Crane","year":"1953","journal-title":"J. Biol. Chem."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1635","DOI":"10.1016\/S0021-9258(18)96139-9","article-title":"Mitochondrial hexokinase: Release, rebinding, and location.","volume":"242","author":"Rose","year":"1967","journal-title":"J. Biol. Chem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1016\/0005-2736(82)90354-6","article-title":"Evidence for identity between the hexokinase-binding protein and the mitochondrial porin in the outer membrane of rat liver mitochondria","volume":"688","author":"Fiek","year":"1982","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"1015","DOI":"10.1021\/bi00353a010","article-title":"Hexokinase receptor complex in hepatoma mitochondria: Evidence from N,N\u2019-dicyclohexylcarbodiimide-labeling studies for the involvement of the pore-forming protein VDAC","volume":"25","author":"Nakashima","year":"1986","journal-title":"Biochemistry"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1016\/0003-9861(85)90633-2","article-title":"An intact hydrophobic N-terminal sequence is critical for binding of rat brain hexokinase to mitochondria","volume":"236","author":"Polakis","year":"1985","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"e00205","DOI":"10.1042\/BSR20150047","article-title":"Identification of a mitochondrial-binding site on the N-terminal end of hexokinase II","volume":"35","author":"Bryan","year":"2015","journal-title":"Biosci. Rep."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1006\/abbi.1997.0241","article-title":"Structural determinants for the intracellular localization of the isozymes of mammalian hexokinase: Intracellular localization of fusion constructs incorporating structural elements from the hexokinase isozymes and the green fluorescent protein","volume":"345","author":"Sui","year":"1997","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_45","doi-asserted-by":"crossref","unstructured":"Golestani, A., Ramshini, H., and Nemat-Gorgani, M. (2007). A study on the two binding sites of hexokinase on brain mitochondria. BMC Biochem., 8.","DOI":"10.1186\/1471-2091-8-20"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1006\/abbi.1993.1089","article-title":"Mitochondrial hexokinase in brain of various species: Differences in sensitivity to solubilization by glucose 6-phosphate","volume":"300","author":"Kabir","year":"1993","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1016\/j.bbabio.2006.11.013","article-title":"VDAC1 serves as a mitochondrial binding site for hexokinase in oxidative muscles","volume":"1767","author":"Cai","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"853","DOI":"10.33594\/000000274","article-title":"Knockout of VDAC1 in H9c2 Cells Promotes Oxidative Stress-Induced Cell Apoptosis through Decreased Mitochondrial Hexokinase II Binding and Enhanced Glycolytic Stress","volume":"54","author":"Yang","year":"2020","journal-title":"Cell Physiol. Biochem."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"111009","DOI":"10.1016\/j.jbc.2025.111009","article-title":"Three mammalian VDAC isoforms distinctly regulate mitochondrial function and proteome to maintain cell metabolism","volume":"302","author":"Rajendran","year":"2026","journal-title":"J. Biol. Chem."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1038\/s42003-021-02205-y","article-title":"Structural basis of complex formation between mitochondrial anion channel VDAC1 and Hexokinase-II","volume":"4","author":"Haloi","year":"2021","journal-title":"Commun. Biol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1038\/s42003-025-07551-9","article-title":"Hexokinase-I directly binds to a charged membrane-buried glutamate of mitochondrial VDAC1 and VDAC2","volume":"8","author":"Bieker","year":"2025","journal-title":"Commun. Biol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1186\/1757-5036-3-4","article-title":"Two-color STED microscopy reveals different degrees of colocalization between hexokinase-I and the three human VDAC isoforms","volume":"3","author":"Neumann","year":"2010","journal-title":"PMC Biophys."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"17422","DOI":"10.1016\/S0021-9258(19)77853-3","article-title":"Functional significance of mitochondrial bound hexokinase in tumor cell metabolism. Evidence for preferential phosphorylation of glucose by intramitochondrially generated ATP","volume":"263","author":"Arora","year":"1988","journal-title":"J. Biol. Chem."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1038\/s42255-025-01428-1","article-title":"Hexokinase detachment from mitochondria drives the Warburg effect to support compartmentalized ATP production","volume":"8","author":"Huggler","year":"2026","journal-title":"Nat. Metab."},{"key":"ref_55","doi-asserted-by":"crossref","unstructured":"Lemeshko, V.V. (2017). The Mitochondrial Outer Membrane Potential as an Electrical Feedback Control of Cell Energy Metabolism. Molecular Basis for Mitochondrial Signaling; Biological and Medical Physics, Biomedical Engineering, Springer.","DOI":"10.1007\/978-3-319-55539-3_9"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"eade7652","DOI":"10.1126\/sciimmunol.ade7652","article-title":"Hexokinase dissociation from mitochondria promotes oligomerization of VDAC that facilitates NLRP3 inflammasome assembly and activation","volume":"8","author":"Baik","year":"2023","journal-title":"Sci. Immunol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"2732","DOI":"10.1016\/j.molcel.2024.06.009","article-title":"Hexokinase 1 forms rings that regulate mitochondrial fission during energy stress","volume":"84","author":"Pilic","year":"2024","journal-title":"Mol. Cell"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1083\/jcb.97.1.209","article-title":"Evidence for tubulin-binding sites on cellular membranes: Plasma membranes, mitochondrial membranes, and secretory granule membranes","volume":"97","author":"Aunis","year":"1983","journal-title":"J. Cell Biol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/BF00737221","article-title":"Associations between beta-tubulin and mitochondria in adult isolated heart myocytes as shown by immunofluorescence and immunoelectron microscopy","volume":"95","author":"Saetersdal","year":"1990","journal-title":"Histochemistry"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"33664","DOI":"10.1074\/jbc.M203834200","article-title":"Tubulin is an inherent component of mitochondrial membranes that interacts with the voltage-dependent anion channel","volume":"277","author":"Carre","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1038\/34465","article-title":"Structure of the alpha beta tubulin dimer by electron crystallography","volume":"391","author":"Nogales","year":"1998","journal-title":"Nature"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"938","DOI":"10.1038\/nrm1260","article-title":"Post-translational modifications regulate microtubule function","volume":"4","author":"Westermann","year":"2003","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_63","doi-asserted-by":"crossref","unstructured":"Gasic, I. (2022). Regulation of Tubulin Gene Expression: From Isotype Identity to Functional Specialization. Front. Cell Dev. Biol., 10.","DOI":"10.3389\/fcell.2022.898076"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/S0091-679X(10)95006-1","article-title":"Mass spectrometry analysis of C-terminal posttranslational modifications of tubulins","volume":"95","author":"Redeker","year":"2010","journal-title":"Methods Cell Biol."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1007\/s10863-008-9145-y","article-title":"VDAC regulation: Role of cytosolic proteins and mitochondrial lipids","volume":"40","author":"Rostovtseva","year":"2008","journal-title":"J. Bioenerg. Biomembr."},{"key":"ref_66","doi-asserted-by":"crossref","unstructured":"Rostovtseva, T.K., Bezrukov, S.M., and Hoogerheide, D.P. (2021). Regulation of Mitochondrial Respiration by VDAC Is Enhanced by Membrane-Bound Inhibitors with Disordered Polyanionic C-Terminal Domains. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22147358"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"2363","DOI":"10.1016\/j.febslet.2011.06.008","article-title":"Tubulin-blocked state of VDAC studied by polymer and ATP partitioning","volume":"585","author":"Gurnev","year":"2011","journal-title":"FEBS Lett."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"9246","DOI":"10.1021\/bi4011495","article-title":"ATP transport through VDAC and the VDAC-tubulin complex probed by equilibrium and nonequilibrium MD simulations","volume":"52","author":"Noskov","year":"2013","journal-title":"Biochemistry"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"E3622","DOI":"10.1073\/pnas.1619806114","article-title":"Structural features and lipid binding domain of tubulin on biomimetic mitochondrial membranes","volume":"114","author":"Hoogerheide","year":"2017","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"772","DOI":"10.1016\/j.bpj.2017.12.019","article-title":"Real-Time Nanopore-Based Recognition of Protein Translocation Success","volume":"114","author":"Hoogerheide","year":"2018","journal-title":"Biophys. J."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"10949","DOI":"10.1074\/jbc.RA117.001569","article-title":"Sequence diversity of tubulin isotypes in regulation of the mitochondrial voltage-dependent anion channel","volume":"293","author":"Rostovtseva","year":"2018","journal-title":"J. Biol. Chem."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1007\/s11010-008-9865-7","article-title":"Regulation of respiration in brain mitochondria and synaptosomes: Restrictions of ADP diffusion in situ, roles of tubulin, and mitochondrial creatine kinase","volume":"318","author":"Monge","year":"2008","journal-title":"Mol. Cell Biochem."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"10192","DOI":"10.1158\/0008-5472.CAN-10-2429","article-title":"Free Tubulin Modulates Mitochondrial Membrane Potential in Cancer Cells","volume":"70","author":"Maldonado","year":"2011","journal-title":"Cancer Res."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"11920","DOI":"10.1074\/jbc.M112.433847","article-title":"Voltage-dependent anion channels modulate mitochondrial metabolism in cancer cells: Regulation by free tubulin and erastin","volume":"288","author":"Maldonado","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_75","doi-asserted-by":"crossref","unstructured":"Parker, A.L., Teo, W.S., Brayford, S., Moorthi, U.K., Arumugam, S., Ferguson, C., Parton, R.G., McCarroll, J.A., and Kavallaris, M. (2022). \u03b2III-Tubulin Structural Domains Regulate Mitochondrial Network Architecture in an Isotype-Specific Manner. Cells, 11.","DOI":"10.3390\/cells11050776"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"787","DOI":"10.1093\/carcin\/bgw058","article-title":"\u03b2III-Tubulin alters glucose metabolism and stress response signaling to promote cell survival and proliferation in glucose-starved non-small cell lung cancer cells","volume":"37","author":"Parker","year":"2016","journal-title":"Carcinogenesis"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1007\/s007020050002","article-title":"Involvement of alpha-synuclein in Parkinson\u2019s disease and other neurodegenerative disorders","volume":"107","author":"Kruger","year":"2000","journal-title":"J. Neural Transm."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1038\/42166","article-title":"Alpha-synuclein in Lewy bodies","volume":"388","author":"Spillantini","year":"1997","journal-title":"Nature"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"a024109","DOI":"10.1101\/cshperspect.a024109","article-title":"Genetics of Synucleinopathies","volume":"8","author":"Nussbaum","year":"2018","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"1543","DOI":"10.1097\/WNR.0b013e3282f03db4","article-title":"Localization of alpha-synuclein to mitochondria within midbrain of mice","volume":"18","author":"Li","year":"2007","journal-title":"Neuroreport"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"2499","DOI":"10.1002\/cbic.201402281","article-title":"Alpha-synuclein binds to the inner membrane of mitochondria in an alpha-helical conformation","volume":"15","author":"Robotta","year":"2014","journal-title":"Chembiochem"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"9089","DOI":"10.1074\/jbc.M710012200","article-title":"Mitochondrial import and accumulation of alpha-synuclein impair complex I in human dopaminergic neuronal cultures and Parkinson disease brain","volume":"283","author":"Devi","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1016\/j.neulet.2010.09.061","article-title":"Mitochondrial alpha-synuclein accumulation impairs complex I function in dopaminergic neurons and results in increased mitophagy in vivo","volume":"486","author":"Chinta","year":"2010","journal-title":"Neurosci. Lett."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1385\/JMN:18:3:229","article-title":"Mutant and wild-type alpha-synuclein interact with mitochondrial cytochrome C oxidase","volume":"18","author":"Elkon","year":"2002","journal-title":"J. Mol. Neurosci."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"2293","DOI":"10.1038\/s41467-018-04422-2","article-title":"\u03b1-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson\u2019s disease","volume":"9","author":"Ludtmann","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"1272","DOI":"10.1007\/s00018-008-7589-1","article-title":"Mitochondrial association of alpha-synuclein causes oxidative stress","volume":"65","author":"Parihar","year":"2008","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"2015","DOI":"10.1016\/j.biocel.2009.05.008","article-title":"Alpha-synuclein overexpression and aggregation exacerbates impairment of mitochondrial functions by augmenting oxidative stress in human neuroblastoma cells","volume":"41","author":"Parihar","year":"2009","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"20710","DOI":"10.1074\/jbc.M110.213538","article-title":"Direct membrane association drives mitochondrial fission by the Parkinson disease-associated protein alpha-synuclein","volume":"286","author":"Nakamura","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_89","doi-asserted-by":"crossref","unstructured":"Vicario, M., Cieri, D., Brini, M., and Cali, T. (2018). The Close Encounter Between Alpha-Synuclein and Mitochondria. Front. Neurosci., 12.","DOI":"10.3389\/fnins.2018.00388"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"167992","DOI":"10.1016\/j.jmb.2023.167992","article-title":"Common Mechanisms Underlying alpha-Synuclein-Induced Mitochondrial Dysfunction in Parkinson\u2019s Disease","volume":"435","author":"Sohrabi","year":"2023","journal-title":"J. Mol. Biol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"3611","DOI":"10.1007\/s00018-019-03386-w","article-title":"Molecular mechanism of olesoxime-mediated neuroprotection through targeting alpha-synuclein interaction with mitochondrial VDAC","volume":"77","author":"Rovini","year":"2020","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"3827","DOI":"10.1038\/ncomms4827","article-title":"Direct observation of the three regions in alpha-synuclein that determine its membrane-bound behaviour","volume":"5","author":"Fusco","year":"2014","journal-title":"Nat. Commun."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"9595","DOI":"10.1074\/jbc.M411805200","article-title":"Structure and dynamics of micelle-bound human alpha-synuclein","volume":"280","author":"Ulmer","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1039\/C6NR08145B","article-title":"Mechanism of alpha-synuclein translocation through a VDAC nanopore revealed by energy landscape modeling of escape time distributions","volume":"9","author":"Hoogerheide","year":"2017","journal-title":"Nanoscale"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"102355","DOI":"10.1016\/j.ceca.2021.102355","article-title":"\u03b1-Synuclein emerges as a potent regulator of VDAC-facilitated calcium transport","volume":"95","author":"Rosencrans","year":"2021","journal-title":"Cell Calcium"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"e201912501","DOI":"10.1085\/jgp.201912501","article-title":"A lower affinity to cytosolic proteins reveals VDAC3 isoform-specific role in mitochondrial biology","volume":"152","author":"Bergdoll","year":"2020","journal-title":"J. Gen. Physiol."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"eadv4410","DOI":"10.1126\/sciadv.adv4410","article-title":"Conformational plasticity of mitochondrial VDAC2 controls the kinetics of its interaction with cytosolic proteins","volume":"11","author":"Rosencrans","year":"2025","journal-title":"Sci. Adv."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"22634","DOI":"10.1073\/pnas.2015886117","article-title":"How the mitochondrial calcium uniporter complex (MCUcx) works","volume":"117","author":"Boyman","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"e55008","DOI":"10.7554\/eLife.55008","article-title":"IP3 mediated global Ca2+ signals arise through two temporally and spatially distinct modes of Ca2+ release","volume":"9","author":"Lock","year":"2020","journal-title":"Elife"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"2380","DOI":"10.1073\/pnas.032423699","article-title":"Ca2+ marks: Miniature calcium signals in single mitochondria driven by ryanodine receptors","volume":"99","author":"Pacher","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"19266","DOI":"10.1073\/pnas.2003236117","article-title":"Mitochondria-lysosome contacts regulate mitochondrial Ca2+ dynamics via lysosomal TRPML1","volume":"117","author":"Peng","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1083\/jcb.200205091","article-title":"Recombinant expression of the voltage-dependent anion channel enhances the transfer of Ca2+ microdomains to mitochondria","volume":"159","author":"Rapizzi","year":"2002","journal-title":"J. Cell Biol."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"901","DOI":"10.1083\/jcb.200608073","article-title":"Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels","volume":"175","author":"Szabadkai","year":"2006","journal-title":"J. Cell Biol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"25152564231181020","DOI":"10.1177\/25152564231181020","article-title":"IP3R at ER-Mitochondrial Contact Sites: Beyond the IP3R-GRP75-VDAC1 Ca2+ Funnel","volume":"6","author":"Ivanova","year":"2023","journal-title":"Contact"},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1038\/cdd.2011.92","article-title":"VDAC1 selectively transfers apoptotic Ca2+ signals to mitochondria","volume":"19","author":"Bononi","year":"2012","journal-title":"Cell Death Differ."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"jcs249045","DOI":"10.1242\/jcs.249045","article-title":"Palmitoylated CKAP4 regulates mitochondrial functions through an interaction with VDAC2 at ER-mitochondria contact sites","volume":"133","author":"Harada","year":"2020","journal-title":"J. Cell Sci."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"114794","DOI":"10.1016\/j.celrep.2024.114794","article-title":"Mitotic ER-mitochondria contact enhances mitochondrial Ca2+ influx to promote cell division","volume":"43","author":"Zhao","year":"2024","journal-title":"Cell Rep."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1042\/BJ20120705","article-title":"Coupling of ryanodine receptor 2 and voltage-dependent anion channel 2 is essential for Ca2+ transfer from the sarcoplasmic reticulum to the mitochondria in the heart","volume":"447","author":"Min","year":"2012","journal-title":"Biochem. J."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"4583","DOI":"10.1038\/s41467-021-24869-0","article-title":"Cardiac-specific deletion of voltage dependent anion channel 2 leads to dilated cardiomyopathy by altering calcium homeostasis","volume":"12","author":"Shankar","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_110","doi-asserted-by":"crossref","unstructured":"Shimizu, H., Huber, S., Langenbacher, A.D., Crisman, L., Huang, J., Wang, K., Wilting, F., Gudermann, T., Schredelseker, J., and Chen, J.N. (2021). Glutamate 73 Promotes Anti-arrhythmic Effects of Voltage-Dependent Anion Channel Through Regulation of Mitochondrial Ca2+ Uptake. Front. Physiol., 12.","DOI":"10.3389\/fphys.2021.724828"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.freeradbiomed.2023.05.021","article-title":"\u03b2-carotene targets IP3R\/GRP75\/VDAC1-MCU axis to renovate LPS-induced mitochondrial oxidative damage by regulating STIM1","volume":"205","author":"Meng","year":"2023","journal-title":"Free Radic. Biol. Med."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"1058","DOI":"10.1038\/s41467-025-67816-z","article-title":"A small molecule VDAC ligand inhibits ERAD and induces selective cancer cell death via disruption of calcium homeostasis","volume":"17","author":"Yan","year":"2026","journal-title":"Nat. Commun."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"1760","DOI":"10.1038\/s44318-026-00700-8","article-title":"STIM1-containing contact sites promote direct calcium flux from the endoplasmic reticulum to mitochondria","volume":"45","author":"Montesinos","year":"2026","journal-title":"EMBO J."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"731","DOI":"10.7150\/ijbs.121759","article-title":"Parkin Deficiency Impairs ER-Mitochondria Associations and calcium homeostasis via IP3R-Grp75-VDAC1 Complex","volume":"22","author":"Xue","year":"2026","journal-title":"Int. J. Biol. Sci."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"25322","DOI":"10.1073\/pnas.1906565116","article-title":"DJ-1 regulates the integrity and function of ER-mitochondria association through interaction with IP3R3-Grp75-VDAC1","volume":"116","author":"Liu","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"536","DOI":"10.1242\/jcs.019281","article-title":"LUMA interacts with emerin and influences its distribution at the inner nuclear membrane","volume":"121","author":"Bengtsson","year":"2008","journal-title":"J. Cell Sci."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"11943","DOI":"10.1073\/pnas.211201898","article-title":"Nuclear envelope proteomics: Novel integral membrane proteins of the inner nuclear membrane","volume":"98","author":"Dreger","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"e57306","DOI":"10.7554\/eLife.57306","article-title":"Interaction mapping of endoplasmic reticulum ubiquitin ligases identifies modulators of innate immune signalling","volume":"9","author":"Fenech","year":"2020","journal-title":"Elife"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"E5","DOI":"10.1002\/mus.26355","article-title":"Emery-Dreifuss muscular dystrophy-related myopathy with TMEM43 mutations","volume":"59","author":"Mukai","year":"2019","journal-title":"Muscle Nerve"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"809","DOI":"10.1016\/j.ajhg.2008.01.010","article-title":"Arrhythmogenic right ventricular cardiomyopathy type 5 is a fully penetrant, lethal arrhythmic disorder caused by a missense mutation in the TMEM43 gene","volume":"82","author":"Merner","year":"2008","journal-title":"Am. J. Hum. Genet."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"e00100","DOI":"10.14309\/ctg.0000000000000100","article-title":"Identification of a Novel Candidate Gene for Serrated Polyposis Syndrome Germline Predisposition by Performing Linkage Analysis Combined With Whole-Exome Sequencing","volume":"10","author":"Toma","year":"2019","journal-title":"Clin. Transl. Gastroenterol."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1152\/physiolgenomics.00066.2021","article-title":"Systems genetics analysis defines importance of TMEM43\/LUMA for cardiac- and metabolic-related pathways","volume":"54","author":"Gu","year":"2022","journal-title":"Physiol. Genom."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"400","DOI":"10.1007\/s00018-025-05942-z","article-title":"The ARVC-5-associated protein TMEM43 controls mitochondrial energy metabolism by stabilising ER-mitochondrial contact sites","volume":"82","author":"Jurgens","year":"2025","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_124","doi-asserted-by":"crossref","unstructured":"Zhu, Q., Zheng, G., Lu, Y., Jiang, Y., Li, Y., Chen, H., Huang, L., Tang, N., Li, B., and Lu, Y. (2025). Proteomic screening of TMEM43 binding partners identifies VDAC leading to mitochondrial dysfunction. PLoS ONE, 20.","DOI":"10.1371\/journal.pone.0339129"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"9","DOI":"10.21037\/tgh-23-108","article-title":"TMEM43 promotes the development of hepatocellular carcinoma by activating VDAC1 through USP7 deubiquitination","volume":"9","author":"Zhang","year":"2024","journal-title":"Transl. Gastroenterol. Hepatol."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1038\/s41580-023-00629-4","article-title":"Mechanisms of BCL-2 family proteins in mitochondrial apoptosis","volume":"24","author":"Czabotar","year":"2023","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1038\/20959","article-title":"Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC","volume":"399","author":"Shimizu","year":"1999","journal-title":"Nature"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"1174","DOI":"10.1038\/sj.cdd.4400780","article-title":"VDAC regulation by the Bcl-2 family of proteins","volume":"7","author":"Tsujimoto","year":"2000","journal-title":"Cell Death Differ."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1007\/s10863-005-6566-8","article-title":"On the role of VDAC in apoptosis: Fact and fiction","volume":"37","author":"Rostovtseva","year":"2005","journal-title":"J. Bioenerg. Biomembr."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"550","DOI":"10.1038\/ncb1575","article-title":"Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death","volume":"9","author":"Baines","year":"2007","journal-title":"Nat. Cell Biol."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"1531","DOI":"10.1126\/science.aav4011","article-title":"VDAC oligomers form mitochondrial pores to release mtDNA fragments and promote lupus-like disease","volume":"366","author":"Kim","year":"2019","journal-title":"Science"},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"151598","DOI":"10.1016\/j.ijbiomac.2026.151598","article-title":"Inhibition of voltage-dependent anion channel 1 aggregation protects pancreatic beta-cell mitochondria from glucose toxicity","volume":"356","author":"Yao","year":"2026","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_133","doi-asserted-by":"crossref","unstructured":"Belosludtsev, K.N., Serov, D.A., Ilzorkina, A.I., Starinets, V.S., Dubinin, M.V., Talanov, E.Y., Karagyaur, M.N., Primak, A.L., and Belosludtseva, N.V. (2023). Pharmacological and Genetic Suppression of VDAC1 Alleviates the Development of Mitochondrial Dysfunction in Endothelial and Fibroblast Cell Cultures upon Hyperglycemic Conditions. Antioxidants, 12.","DOI":"10.3390\/antiox12071459"},{"key":"ref_134","doi-asserted-by":"crossref","unstructured":"Shteinfer-Kuzmine, A., Argueti-Ostrovsky, S., Leyton-Jaimes, M.F., Anand, U., Abu-Hamad, S., Zalk, R., Shoshan-Barmatz, V., and Israelson, A. (2022). Targeting the Mitochondrial Protein VDAC1 as a Potential Therapeutic Strategy in ALS. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23179946"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1186\/s40035-022-00329-7","article-title":"Targeting the overexpressed mitochondrial protein VDAC1 in a mouse model of Alzheimer\u2019s disease protects against mitochondrial dysfunction and mitigates brain pathology","volume":"11","author":"Verma","year":"2022","journal-title":"Transl. Neurodegener."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1016\/0005-2736(84)90293-1","article-title":"Evidence that the crystalline arrays in the outer membrane of Neurospora mitochondria are composed of the voltage-dependent channel protein","volume":"774","author":"Mannella","year":"1984","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/0304-3991(84)90060-3","article-title":"Negative staining characteristics of arrays of mitochondrial pore protein: Use of correspondence analysis to classify different staining patterns","volume":"13","author":"Mannella","year":"1984","journal-title":"Ultramicroscopy"},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1016\/j.jmb.2007.03.063","article-title":"Supramolecular assembly of VDAC in native mitochondrial outer membranes","volume":"369","author":"Goncalves","year":"2007","journal-title":"J. Mol. Biol."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1016\/j.jmb.2007.04.073","article-title":"The supramolecular assemblies of voltage-dependent anion channels in the native membrane","volume":"370","author":"Hoogenboom","year":"2007","journal-title":"J. Mol. Biol."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"6854","DOI":"10.1038\/s41467-025-62021-4","article-title":"Oligomer-based functions of mitochondrial porin","volume":"16","author":"Takeda","year":"2025","journal-title":"Nat. Commun."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1016\/j.bpj.2011.12.049","article-title":"The role of lipids in VDAC oligomerization","volume":"102","author":"Betaneli","year":"2012","journal-title":"Biophys. J."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"936","DOI":"10.1038\/s42003-025-08311-5","article-title":"Membrane lipid composition modulates the organization of VDAC1, a mitochondrial gatekeeper","volume":"8","author":"Lafargue","year":"2025","journal-title":"Commun. Biol."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1042\/BST20250480","article-title":"A pore is a pore is a pore (or a hub?): VDAC oligomerization in mitochondrial connectivity and modulation","volume":"54","author":"Battiato","year":"2026","journal-title":"Biochem. Soc. Trans."},{"key":"ref_144","doi-asserted-by":"crossref","unstructured":"Ravishankar, V., Borges-Araujo, L., Lafargue, E., Byrne, D., Buzhinsky, N., Wolfe, M.S., Bautista, N.A., Beyene, B.G., Larimi, M.G., and Duneau, J.P. (2025). A Membrane-Disruptive Action of VBIT-4 Challenges Its Role as a Widely Used VDAC Oligomerization Inhibitor. bioRxiv.","DOI":"10.1101\/2025.06.30.661942"},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"184329","DOI":"10.1016\/j.bbamem.2024.184329","article-title":"Effect of VBIT-4 on the functional activity of isolated mitochondria and cell viability","volume":"1866","author":"Belosludtsev","year":"2024","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"389","DOI":"10.15252\/embj.201593384","article-title":"Bax assembly into rings and arcs in apoptotic mitochondria is linked to membrane pores","volume":"35","author":"Mund","year":"2016","journal-title":"EMBO J."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1016\/j.tcb.2016.11.004","article-title":"Bax and Bak Pores: Are We Closing the Circle?","volume":"27","author":"Cosentino","year":"2017","journal-title":"Trends Cell Biol."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"933","DOI":"10.1016\/j.molcel.2022.01.008","article-title":"The interplay between BAX and BAK tunes apoptotic pore growth to control mitochondrial-DNA-mediated inflammation","volume":"82","author":"Cosentino","year":"2022","journal-title":"Mol. Cell"},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"514","DOI":"10.1021\/bi061577h","article-title":"NMR structural investigation of the mitochondrial outer membrane protein VDAC and its interaction with antiapoptotic Bcl-xL","volume":"46","author":"Malia","year":"2007","journal-title":"Biochemistry"},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"36876","DOI":"10.1074\/jbc.M110.159301","article-title":"Inhibition of Bak activation by VDAC2 is dependent on the Bak transmembrane anchor","volume":"285","author":"Lazarou","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"1341","DOI":"10.1038\/embor.2009.219","article-title":"VDAC2 is required for truncated BID-induced mitochondrial apoptosis by recruiting BAK to the mitochondria","volume":"10","author":"Roy","year":"2009","journal-title":"EMBO Rep."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"1057","DOI":"10.1038\/s41589-019-0365-8","article-title":"A small molecule interacts with VDAC2 to block mouse BAK-driven apoptosis","volume":"15","author":"Chappaz","year":"2019","journal-title":"Nat. Chem. Biol."},{"key":"ref_153","doi-asserted-by":"crossref","unstructured":"Yuan, Z., van Delft, M.F., Li, M.X., Sumardy, F., Smith, B.J., Huang, D.C.S., Lessene, G., Khakam, Y., Jin, R., and He, S. (2024). Key residues in the VDAC2-BAK complex can be targeted to modulate apoptosis. PLoS Biol., 22.","DOI":"10.1371\/journal.pbio.3002617"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"1062","DOI":"10.1038\/s41586-025-08732-6","article-title":"VDAC2 loss elicits tumour destruction and inflammation for cancer therapy","volume":"640","author":"Yuan","year":"2025","journal-title":"Nature"},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"808","DOI":"10.1038\/s41590-025-02171-1","article-title":"VDAC2 enforces a mitochondrial checkpoint to cancer immunity","volume":"26","author":"Cosentino","year":"2025","journal-title":"Nat. Immunol."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1016\/j.tips.2025.07.001","article-title":"VDAC2 brake release: Unleashing inflammation via IFN\u03b3","volume":"46","author":"Patel","year":"2025","journal-title":"Trends Pharmacol. Sci."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"2416","DOI":"10.1038\/s41467-025-56898-4","article-title":"VDAC2 and Bak scarcity in liver mitochondria enables targeting hepatocarcinoma while sparing hepatocytes","volume":"16","author":"Naghdi","year":"2025","journal-title":"Nat. Commun."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"995","DOI":"10.1038\/s41375-025-02523-8","article-title":"VDAC2 primes myeloma cells for BAK-dependent apoptosis and represents a novel therapeutic target","volume":"39","author":"Champion","year":"2025","journal-title":"Leukemia"},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"2330","DOI":"10.1093\/emboj\/18.9.2330","article-title":"Conformation of the Bax C-terminus regulates subcellular location and cell death","volume":"18","author":"Nechushtan","year":"1999","journal-title":"EMBO J."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"32994","DOI":"10.1038\/srep32994","article-title":"The porin VDAC2 is the mitochondrial platform for Bax retrotranslocation","volume":"6","author":"Lauterwasser","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"1925","DOI":"10.1038\/cdd.2014.119","article-title":"Bax targets mitochondria by distinct mechanisms before or during apoptotic cell death: A requirement for VDAC2 or Bak for efficient Bax apoptotic function","volume":"21","author":"Ma","year":"2014","journal-title":"Cell Death Differ."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1016\/j.cell.2011.02.034","article-title":"Bcl-xL retrotranslocates Bax from the mitochondria into the cytosol","volume":"145","author":"Edlich","year":"2011","journal-title":"Cell"},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"1044","DOI":"10.1016\/j.molcel.2019.01.003","article-title":"Porin Associates with Tom22 to Regulate the Mitochondrial Protein Gate Assembly","volume":"73","author":"Sakaue","year":"2019","journal-title":"Mol. Cell"},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"1056","DOI":"10.1016\/j.molcel.2018.12.014","article-title":"Dual Role of Mitochondrial Porin in Metabolite Transport across the Outer Membrane and Protein Transfer to the Inner Membrane","volume":"73","author":"Ellenrieder","year":"2019","journal-title":"Mol. Cell"},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"48027","DOI":"10.1074\/jbc.M106524200","article-title":"Mitochondrial creatine kinase and mitochondrial outer membrane porin show a direct interaction that is modulated by calcium","volume":"276","author":"Schlattner","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"38879","DOI":"10.1074\/jbc.M608820200","article-title":"Protein-protein interactions mediate mitochondrial cholesterol transport and steroid biosynthesis","volume":"281","author":"Liu","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"2279","DOI":"10.4161\/15548627.2014.991665","article-title":"TSPO interacts with VDAC1 and triggers a ROS-mediated inhibition of mitochondrial quality control","volume":"10","author":"Gatliff","year":"2014","journal-title":"Autophagy"},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"8837","DOI":"10.1074\/jbc.M709221200","article-title":"Steroidogenic activity of StAR requires contact with mitochondrial VDAC1 and phosphate carrier protein","volume":"283","author":"Bose","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"112229","DOI":"10.1016\/j.celrep.2023.112229","article-title":"Interaction between PI3K and the VDAC2 channel tethers Ras-PI3K-positive endosomes to mitochondria and promotes endosome maturation","volume":"42","author":"Satoh","year":"2023","journal-title":"Cell Rep."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"19870","DOI":"10.1074\/jbc.M112.448290","article-title":"An interaction between Bcl-xL and the voltage-dependent anion channel (VDAC) promotes mitochondrial Ca2+ uptake","volume":"288","author":"Huang","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"e1482","DOI":"10.1038\/cddis.2014.419","article-title":"Mcl-1 promotes lung cancer cell migration by directly interacting with VDAC to increase mitochondrial Ca2+ uptake and reactive oxygen species generation","volume":"5","author":"Huang","year":"2014","journal-title":"Cell Death Dis."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"3705","DOI":"10.1242\/jcs.192203","article-title":"Desmin and alphaB-crystallin interplay in the maintenance of mitochondrial homeostasis and cardiomyocyte survival","volume":"129","author":"Diokmetzidou","year":"2016","journal-title":"J. Cell Sci."},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"40652","DOI":"10.1074\/jbc.M112.419721","article-title":"Voltage-dependent anion channels (VDACs) recruit Parkin to defective mitochondria to promote mitochondrial autophagy","volume":"287","author":"Sun","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"e56297","DOI":"10.15252\/embr.202256297","article-title":"MIRO-1 interacts with VDAC-1 to regulate mitochondrial membrane potential in Caenorhabditis elegans","volume":"24","author":"Ren","year":"2023","journal-title":"EMBO Rep."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"2134","DOI":"10.1039\/C4MB00237G","article-title":"Live cell interactome of the human voltage dependent anion channel 3 (VDAC3) revealed in HeLa cells by affinity purification tag technique","volume":"10","author":"Messina","year":"2014","journal-title":"Mol. Biosyst."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/27\/13\/5804\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,7,7]],"date-time":"2026-07-07T10:12:04Z","timestamp":1783419124000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/27\/13\/5804"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,6,26]]},"references-count":175,"journal-issue":{"issue":"13","published-online":{"date-parts":[[2026,7]]}},"alternative-id":["ijms27135804"],"URL":"https:\/\/doi.org\/10.3390\/ijms27135804","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,6,26]]}}}