{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nVDAC1 is a highly conserved, β‐barrel channel protein of the outer mitochondrial membrane whose three‐dimensional structure and dynamic folding properties have been elucidated by solution and solid‐state NMR, X‐ray crystallography, and molecular simulations. These studies reveal that VDAC1 spontaneously folds into lipid bilayers to form an elliptical, voltage‐gated pore with defined ion selectivity that is critical for the exchange of metabolites, ions, and nucleotides between the mitochondrion and the cytosol. The detailed structural analysis—including its β‐barrel architecture, N‐terminal mobility, and modulation by the lipid environment—provides the molecular basis for its gating behavior."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "6"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its role as a metabolite gatekeeper, VDAC1 serves as a key regulator of mitochondrial apoptosis and cellular energy homeostasis. It interacts directly with anti‐apoptotic proteins such as hexokinase, Bcl‑2, Bcl‑xL, and other Bcl‑2 family members – associations that can inhibit cytochrome c release and thus block apoptosis. Conversely, disruption of these interactions promotes apoptogenic changes. These protein–protein associations therefore integrate metabolic signals with the decision to live or die, underscoring VDAC1’s pivotal function at the crossroads of cell survival and death."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "17"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nVDAC1 also oligomerizes in response to various apoptotic stimuli, thereby forming high‑order channels that facilitate cytochrome c release and promote mitochondria-mediated cell death. Its oligomerization, in conjunction with intracellular Ca²⁺ signals, appears to be a key step in mitochondrial permeability transition. These processes are tightly regulated, as indicated by studies showing that inhibitors of VDAC1 oligomerization can prevent the cascade of events leading to apoptosis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "18", "end_ref": "24"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the context of neurodegenerative disorders, VDAC1 has emerged as an important molecular target. Aberrant ubiquitination of VDAC1 by the Parkinson’s disease–associated proteins PINK1 and Parkin links mitochondrial damage to mitophagy, while interactions with misfolded proteins such as α‑synuclein, amyloid‑β, and hyperphosphorylated tau contribute to mitochondrial dysfunction in Parkinson’s and Alzheimer’s diseases. Moreover, regulation of VDAC1 expression by microRNAs (e.g., miR‑7) highlights its role in neuroprotection."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "25", "end_ref": "31"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its established roles in mitochondrial metabolism and apoptosis, VDAC1 represents a promising therapeutic target in cancer, metabolic disorders, and other diseases. Its overexpression in many cancers contributes to the reprogramming of metabolic and survival pathways; interactions with proteins such as Mcl‑1 and components of the plasma membrane redox machinery further add to its multifaceted functions. VDAC1 also participates in steroidogenesis through interactions with proteins like StAR and functions as a receptor for certain bioactive peptides. These diverse roles underpin ongoing efforts to modulate VDAC1 function pharmacologically – for instance, by using specific peptides or small molecules (e.g., itraconazole) that target its interactions or channel activity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "32", "end_ref": "38"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Sebastian Hiller, Robert G Garces, Thomas J Malia, et al. 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