{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nVoltage‐dependent anion channel 2 (VDAC2) is a key pore‐forming protein of the mitochondrial outer membrane that orchestrates multiple cell death pathways. In several studies, VDAC2 has been implicated in both pro‐ and anti‐apoptotic processes. For example, its identification in the flagellar outer dense fibers of spermatozoa highlights non‐canonical roles beyond metabolite exchange (PMID 14739283 ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "]). Functional analyses further reveal that VDAC2 directly regulates the integration and retrotranslocation of pro‐apoptotic mediators such as Bak and Bax, and its interaction with death‐inducing peptides (via its binding to elements of truncated Bid and Noxa domains) contributes to the control of mitochondrial permeability and cell fate (PMID 15757910 ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": "], PMID 22114330 ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": "], PMID 26417093 ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": "], PMID 27620692 ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": "], PMID 31285435 ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "6"}]}, {"type": "t", "text": "], PMID 31974380 ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "7"}]}, {"type": "t", "text": "], PMID 31981967 ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "8"}]}, {"type": "t", "text": "]). These interactions not only underlie its involvement in intrinsic apoptotic signaling but also influence the cellular response to ferroptosis activators like erastin, which trigger VDAC2 ubiquitination and degradation as part of negative feedback loops to modulate cell death.\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its central role in apoptotic control, VDAC2 is pivotal in maintaining mitochondrial homeostasis and regulating cellular metabolism. For instance, studies in cardiomyocytes have demonstrated that VDAC2 contributes to the fine‐tuning of local Ca²⁺ signaling and spark dynamics, which are critical for proper mitochondrial and cardiac function (PMID 21241999 ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "9"}]}, {"type": "t", "text": "]). Moreover, VDAC2 expression is modulated in response to metabolic stress such as iron deprivation (PMID 18278581 ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "10"}]}, {"type": "t", "text": "]) and in germ cell compartments where it plays a role in cellular differentiation (PMID 21347391 ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "11"}]}, {"type": "t", "text": "]). Reconstitution studies employing lipid bilayer nanodiscs have underscored the importance of VDAC2’s membrane milieu for its stability and channel function (PMID 22119777 ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "12"}]}, {"type": "t", "text": "], PMID 30503532 ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "13"}]}, {"type": "t", "text": "], PMID 32098132 ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "14"}]}, {"type": "t", "text": "]). In cancer cells, altered VDAC2 expression and post‐translational oxidation of cysteine residues contribute to metabolic reprogramming and chemoresistance—for example, in glioma stem cells and pancreatic or endometrial tumors—while its interaction with innate immune regulators such as STING further modulates reactive oxygen species and Ca²⁺ homeostasis (PMID 30250190 ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "15"}]}, {"type": "t", "text": "], PMID 32641986 ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "16"}]}, {"type": "t", "text": "], PMID 32829673 ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "17"}]}, {"type": "t", "text": "], PMID 33067418 ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "18"}]}, {"type": "t", "text": "]).\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nVDAC2 also exerts key functions in reproductive biology and exhibits unique structural features that underpin its regulation. Epigenetic studies have linked VDAC2 promoter methylation to sperm motility and acrosomal function, implying an important role in male fertility (PMID 22842492 ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "19"}]}, {"type": "t", "text": "], PMID 27892527 ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "20"}]}, {"type": "t", "text": "], PMID 27806320 ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "21"}]}, {"type": "t", "text": "]). Detailed structural and biophysical analyses have revealed that a distinct set of cysteine residues in VDAC2 governs its protein–lipid interactions and channel gating properties, thereby influencing its overall conformational stability (PMID 23873934 ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "22"}]}, {"type": "t", "text": "], PMID 24642864 ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "23"}]}, {"type": "t", "text": "], PMID 25341036 ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "24"}]}, {"type": "t", "text": "], PMID 25583988 ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "25"}]}, {"type": "t", "text": "], PMID 26947058 ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "26"}]}, {"type": "t", "text": "]). Additionally, although interactions with anti‐apoptotic proteins such as Mcl-1 appear comparatively weaker, they still contribute to the tightly regulated network of protein–protein interactions modulating mitochondrial permeability (PMID 25341036 ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "24"}]}, {"type": "t", "text": "], PMID 25583988 ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "25"}]}, {"type": "t", "text": "]). Finally, the ability of VDAC2 to participate in necrotic cell death pathways induced by small molecules such as bisindolylpyrrole further underscores its multifaceted role in cellular fate determination (PMID 33046783 ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "27"}]}, {"type": "t", "text": ">]).\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Klaus-Dieter Hinsch, Vito De Pinto, Viviana A Aires, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Voltage-dependent anion-selective channels VDAC2 and VDAC3 are abundant proteins in bovine outer dense fibers, a cytoskeletal component of the sperm flagellum."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M313433200"}], "href": "https://doi.org/10.1074/jbc.M313433200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "14739283"}], "href": "https://pubmed.ncbi.nlm.nih.gov/14739283"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Dhyan Chandra, Grace Choy, Peter T Daniel, et al. 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