VDAC1 is the most abundant protein of the mitochondrial outer membrane and the major conduit between the cytosol and the intermembrane space. It folds as a 19-stranded beta barrel with an N-terminal helix inside the pore, forming a large voltage-gated channel that is open and weakly anion-selective near zero membrane potential and switches to a cation-selective, low-conductance closed state above about 30-40 mV. Through this channel VDAC1 passes ATP, ADP, phosphate, pyruvate, other small metabolites and ions, including the Ca2+ that the MCU then takes into the matrix. VDAC1 dimers additionally act as a phospholipid scramblase, translocating lipids across the outer membrane by a mechanism unrelated to channel conduction. The barrel binds cholesterol, oxysterol, phosphatidylcholine and ceramide, and its cytosolic face is a docking platform for hexokinases, BCL-2-family proteins and kinases; VDAC1 is a component of the mitochondrial permeability transition pore complex with SPG7 and PPIF, and is a Parkin substrate whose ubiquitination state sets the balance between mitophagy and apoptosis. A minor extramitochondrial pool has been reported in the plasma membrane, including neuronal lipid rafts.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005244 voltage-gated monoatomic ion channel activity | IDA PMID:8420959 Cloning and functional expression in yeast of two human isof... | MODIFY | Summary: Purified human VDAC1 forms a voltage-gated channel in planar bilayers. Reason: Correct but general: the open state is anion-selective, and the gene already carries the specific term voltage-gated monoatomic anion channel activity (GO:0008308). Proposed replacements: voltage-gated monoatomic anion channel activity Supporting Evidence: PMID:8420959 Human proteins isolated from yeast mitochondria formed channels with the characteristics expected of VDAC when incorporated into planar lipid bilayers. file:human/VDAC1/VDAC1-uniprot.txt The open state has a weak anion selectivity whereas the closed state is |
| GO:0005515 protein binding | IPI PMID:16201016 Influenza virus PB1-F2 protein induces cell death through mi... | REMOVE | Summary: Bare protein binding from an interaction assay. Reason: Generic protein binding is uninformative under the protein-binding policy; the interaction itself is not disputed, but no more specific molecular function is established by this row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19130895 Enzymatically inactive adenylate kinase 4 interacts with mit... | REMOVE | Summary: Bare protein binding from an interaction assay. Reason: Generic protein binding is uninformative under the protein-binding policy; the interaction itself is not disputed, but no more specific molecular function is established by this row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21370995 Expression of leucine-rich repeat kinase 2 (LRRK2) inhibits ... | REMOVE | Summary: Bare protein binding from an interaction assay. Reason: Generic protein binding is uninformative under the protein-binding policy; the interaction itself is not disputed, but no more specific molecular function is established by this row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21370995 Expression of leucine-rich repeat kinase 2 (LRRK2) inhibits ... | REMOVE | Summary: Bare protein binding from an interaction assay. Reason: Generic protein binding is uninformative under the protein-binding policy; the interaction itself is not disputed, but no more specific molecular function is established by this row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:22304920 PKCΞ΅ promotes oncogenic functions of ATF2 in the nucleus whi... | REMOVE | Summary: Bare protein binding from an interaction assay. Reason: Generic protein binding is uninformative under the protein-binding policy; the interaction itself is not disputed, but no more specific molecular function is established by this row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23055042 Human Bop is a novel BH3-only member of the Bcl-2 protein fa... | REMOVE | Summary: Bare protein binding from an interaction assay. Reason: Generic protein binding is uninformative under the protein-binding policy; the interaction itself is not disputed, but no more specific molecular function is established by this row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25296756 Plasminogen kringle 5 induces endothelial cell apoptosis by ... | REMOVE | Summary: Bare protein binding from an interaction assay. Reason: Generic protein binding is uninformative under the protein-binding policy; the interaction itself is not disputed, but no more specific molecular function is established by this row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25556234 New host factors important for respiratory syncytial virus (... | REMOVE | Summary: Bare protein binding from an interaction assay. Reason: Generic protein binding is uninformative under the protein-binding policy; the interaction itself is not disputed, but no more specific molecular function is established by this row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:26387735 SPG7 Is an Essential and Conserved Component of the Mitochon... | REMOVE | Summary: Bare protein binding from an interaction assay. Reason: Generic protein binding is uninformative under the protein-binding policy; the interaction itself is not disputed, but no more specific molecular function is established by this row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:26387735 SPG7 Is an Essential and Conserved Component of the Mitochon... | REMOVE | Summary: Bare protein binding from an interaction assay. Reason: Generic protein binding is uninformative under the protein-binding policy; the interaction itself is not disputed, but no more specific molecular function is established by this row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Bare protein binding from an interaction assay. Reason: Generic protein binding is uninformative under the protein-binding policy; the interaction itself is not disputed, but no more specific molecular function is established by this row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:29128334 A Map of Human Mitochondrial Protein Interactions Linked to ... | REMOVE | Summary: Bare protein binding from an interaction assay. Reason: Generic protein binding is uninformative under the protein-binding policy; the interaction itself is not disputed, but no more specific molecular function is established by this row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:29128334 A Map of Human Mitochondrial Protein Interactions Linked to ... | REMOVE | Summary: Bare protein binding from an interaction assay. Reason: Generic protein binding is uninformative under the protein-binding policy; the interaction itself is not disputed, but no more specific molecular function is established by this row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:29128334 A Map of Human Mitochondrial Protein Interactions Linked to ... | REMOVE | Summary: Bare protein binding from an interaction assay. Reason: Generic protein binding is uninformative under the protein-binding policy; the interaction itself is not disputed, but no more specific molecular function is established by this row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:29128334 A Map of Human Mitochondrial Protein Interactions Linked to ... | REMOVE | Summary: Bare protein binding from an interaction assay. Reason: Generic protein binding is uninformative under the protein-binding policy; the interaction itself is not disputed, but no more specific molecular function is established by this row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:29128334 A Map of Human Mitochondrial Protein Interactions Linked to ... | REMOVE | Summary: Bare protein binding from an interaction assay. Reason: Generic protein binding is uninformative under the protein-binding policy; the interaction itself is not disputed, but no more specific molecular function is established by this row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:29128334 A Map of Human Mitochondrial Protein Interactions Linked to ... | REMOVE | Summary: Bare protein binding from an interaction assay. Reason: Generic protein binding is uninformative under the protein-binding policy; the interaction itself is not disputed, but no more specific molecular function is established by this row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:30021884 Histone Interaction Landscapes Visualized by Crosslinking Ma... | REMOVE | Summary: Bare protein binding from an interaction assay. Reason: Generic protein binding is uninformative under the protein-binding policy; the interaction itself is not disputed, but no more specific molecular function is established by this row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:30352685 Stasimon/Tmem41b localizes to mitochondria-associated ER mem... | REMOVE | Summary: Bare protein binding from an interaction assay. Reason: Generic protein binding is uninformative under the protein-binding policy; the interaction itself is not disputed, but no more specific molecular function is established by this row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31046837 Parkinson's disease-associated LRRK2-G2019S mutant acts thro... | REMOVE | Summary: Bare protein binding from an interaction assay. Reason: Generic protein binding is uninformative under the protein-binding policy; the interaction itself is not disputed, but no more specific molecular function is established by this row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31206022 BAP31 regulates mitochondrial function via interaction with ... | REMOVE | Summary: Bare protein binding from an interaction assay. Reason: Generic protein binding is uninformative under the protein-binding policy; the interaction itself is not disputed, but no more specific molecular function is established by this row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Bare protein binding from an interaction assay. Reason: Generic protein binding is uninformative under the protein-binding policy; the interaction itself is not disputed, but no more specific molecular function is established by this row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Bare protein binding from an interaction assay. Reason: Generic protein binding is uninformative under the protein-binding policy; the interaction itself is not disputed, but no more specific molecular function is established by this row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Bare protein binding from an interaction assay. Reason: Generic protein binding is uninformative under the protein-binding policy; the interaction itself is not disputed, but no more specific molecular function is established by this row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Bare protein binding from an interaction assay. Reason: Generic protein binding is uninformative under the protein-binding policy; the interaction itself is not disputed, but no more specific molecular function is established by this row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:41991342 The microprotein SMIM26 connects metabolite transporters of ... | REMOVE | Summary: Bare protein binding from an interaction assay. Reason: Generic protein binding is uninformative under the protein-binding policy; the interaction itself is not disputed, but no more specific molecular function is established by this row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:9843949 Bax interacts with the permeability transition pore to induc... | REMOVE | Summary: Bare protein binding from an interaction assay. Reason: Generic protein binding is uninformative under the protein-binding policy; the interaction itself is not disputed, but no more specific molecular function is established by this row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:9843949 Bax interacts with the permeability transition pore to induc... | REMOVE | Summary: Bare protein binding from an interaction assay. Reason: Generic protein binding is uninformative under the protein-binding policy; the interaction itself is not disputed, but no more specific molecular function is established by this row. Supporting Evidence: |
| GO:0005634 nucleus | HDA PMID:21630459 Proteomic characterization of the human sperm nucleus. | MARK AS OVER ANNOTATED | Summary: Detected in a high-throughput nuclear proteome. Reason: VDAC1 is a mitochondrial outer-membrane protein; nuclear detection in a subcellular proteomic survey most likely reflects mitochondrial carry-over, and no function is attributed to a nuclear pool. Supporting Evidence: file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the |
| GO:0005739 mitochondrion | HDA PMID:20833797 Phosphoproteome analysis of functional mitochondria isolated... | MODIFY | Summary: VDAC1 is detected in mitochondria. Reason: Correct but general: VDAC1 is specifically an integral protein of the mitochondrial outer membrane (GO:0005741, already carried by the gene). Proposed replacements: mitochondrial outer membrane Supporting Evidence: file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the PMID:8420959 Human proteins isolated from yeast mitochondria formed channels with the characteristics expected of VDAC when incorporated into planar lipid bilayers. |
| GO:0005739 mitochondrion | HTP PMID:34800366 Quantitative high-confidence human mitochondrial proteome an... | MODIFY | Summary: VDAC1 is detected in mitochondria. Reason: Correct but general: VDAC1 is specifically an integral protein of the mitochondrial outer membrane (GO:0005741, already carried by the gene). Proposed replacements: mitochondrial outer membrane Supporting Evidence: file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the PMID:8420959 Human proteins isolated from yeast mitochondria formed channels with the characteristics expected of VDAC when incorporated into planar lipid bilayers. |
| GO:0005739 mitochondrion | IDA PMID:30188326 Deletion of Tmtc4 activates the unfolded protein response an... | MODIFY | Summary: VDAC1 is detected in mitochondria. Reason: Correct but general: VDAC1 is specifically an integral protein of the mitochondrial outer membrane (GO:0005741, already carried by the gene). Proposed replacements: mitochondrial outer membrane Supporting Evidence: file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the PMID:8420959 Human proteins isolated from yeast mitochondria formed channels with the characteristics expected of VDAC when incorporated into planar lipid bilayers. |
| GO:0005739 mitochondrion | IDA PMID:31206022 BAP31 regulates mitochondrial function via interaction with ... | MODIFY | Summary: VDAC1 is detected in mitochondria. Reason: Correct but general: VDAC1 is specifically an integral protein of the mitochondrial outer membrane (GO:0005741, already carried by the gene). Proposed replacements: mitochondrial outer membrane Supporting Evidence: file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the PMID:8420959 Human proteins isolated from yeast mitochondria formed channels with the characteristics expected of VDAC when incorporated into planar lipid bilayers. |
| GO:0005739 mitochondrion | IEA GO_REF:0000107 | MODIFY | Summary: VDAC1 is detected in mitochondria. Reason: Correct but general: VDAC1 is specifically an integral protein of the mitochondrial outer membrane (GO:0005741, already carried by the gene). Proposed replacements: mitochondrial outer membrane Supporting Evidence: file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the PMID:8420959 Human proteins isolated from yeast mitochondria formed channels with the characteristics expected of VDAC when incorporated into planar lipid bilayers. |
| GO:0005741 mitochondrial outer membrane | EXP PMID:10661876 Mitochondria-derived and extra-mitochondrial human type-1 po... | ACCEPT | Summary: VDAC1 is the major beta-barrel channel of the mitochondrial outer membrane. Reason: Core location, established by fractionation, imaging and electrophysiology of the purified protein. Supporting Evidence: file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the PMID:8420959 Human proteins isolated from yeast mitochondria formed channels with the characteristics expected of VDAC when incorporated into planar lipid bilayers. |
| GO:0005741 mitochondrial outer membrane | EXP PMID:31015432 Ceramides bind VDAC2 to trigger mitochondrial apoptosis. | ACCEPT | Summary: VDAC1 is the major beta-barrel channel of the mitochondrial outer membrane. Reason: Core location, established by fractionation, imaging and electrophysiology of the purified protein. Supporting Evidence: file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the PMID:8420959 Human proteins isolated from yeast mitochondria formed channels with the characteristics expected of VDAC when incorporated into planar lipid bilayers. |
| GO:0005741 mitochondrial outer membrane | EXP PMID:31206022 BAP31 regulates mitochondrial function via interaction with ... | ACCEPT | Summary: VDAC1 is the major beta-barrel channel of the mitochondrial outer membrane. Reason: Core location, established by fractionation, imaging and electrophysiology of the purified protein. Supporting Evidence: file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the PMID:8420959 Human proteins isolated from yeast mitochondria formed channels with the characteristics expected of VDAC when incorporated into planar lipid bilayers. |
| GO:0005741 mitochondrial outer membrane | IBA GO_REF:0000033 | ACCEPT | Summary: VDAC1 is the major beta-barrel channel of the mitochondrial outer membrane. Reason: Core location, established by fractionation, imaging and electrophysiology of the purified protein. Supporting Evidence: file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the PMID:8420959 Human proteins isolated from yeast mitochondria formed channels with the characteristics expected of VDAC when incorporated into planar lipid bilayers. |
| GO:0005741 mitochondrial outer membrane | IDA PMID:17008324 Mitochondrial functions and estrogen receptor-dependent nucl... | ACCEPT | Summary: VDAC1 is the major beta-barrel channel of the mitochondrial outer membrane. Reason: Core location, established by fractionation, imaging and electrophysiology of the purified protein. Supporting Evidence: file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the PMID:8420959 Human proteins isolated from yeast mitochondria formed channels with the characteristics expected of VDAC when incorporated into planar lipid bilayers. |
| GO:0005741 mitochondrial outer membrane | IDA PMID:25244949 Hepatitis C virus core protein suppresses mitophagy by inter... | ACCEPT | Summary: VDAC1 is the major beta-barrel channel of the mitochondrial outer membrane. Reason: Core location, established by fractionation, imaging and electrophysiology of the purified protein. Supporting Evidence: file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the PMID:8420959 Human proteins isolated from yeast mitochondria formed channels with the characteristics expected of VDAC when incorporated into planar lipid bilayers. |
| GO:0005741 mitochondrial outer membrane | IDA PMID:7539795 Subcellular localization of human voltage-dependent anion ch... | ACCEPT | Summary: VDAC1 is the major beta-barrel channel of the mitochondrial outer membrane. Reason: Core location, established by fractionation, imaging and electrophysiology of the purified protein. Supporting Evidence: file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the PMID:8420959 Human proteins isolated from yeast mitochondria formed channels with the characteristics expected of VDAC when incorporated into planar lipid bilayers. |
| GO:0005741 mitochondrial outer membrane | IEA GO_REF:0000120 | ACCEPT | Summary: VDAC1 is the major beta-barrel channel of the mitochondrial outer membrane. Reason: Core location, established by fractionation, imaging and electrophysiology of the purified protein. Supporting Evidence: file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the PMID:8420959 Human proteins isolated from yeast mitochondria formed channels with the characteristics expected of VDAC when incorporated into planar lipid bilayers. |
| GO:0005741 mitochondrial outer membrane | TAS Reactome:R-HSA-5205649 | ACCEPT | Summary: VDAC1 is the major beta-barrel channel of the mitochondrial outer membrane. Reason: Core location, established by fractionation, imaging and electrophysiology of the purified protein. Supporting Evidence: Reactome:R-HSA-5205649 file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the |
| GO:0005741 mitochondrial outer membrane | TAS Reactome:R-HSA-5205663 | ACCEPT | Summary: VDAC1 is the major beta-barrel channel of the mitochondrial outer membrane. Reason: Core location, established by fractionation, imaging and electrophysiology of the purified protein. Supporting Evidence: Reactome:R-HSA-5205663 file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the |
| GO:0005741 mitochondrial outer membrane | TAS Reactome:R-HSA-5205673 | ACCEPT | Summary: VDAC1 is the major beta-barrel channel of the mitochondrial outer membrane. Reason: Core location, established by fractionation, imaging and electrophysiology of the purified protein. Supporting Evidence: Reactome:R-HSA-5205673 file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the |
| GO:0005741 mitochondrial outer membrane | TAS Reactome:R-HSA-9012374 | ACCEPT | Summary: VDAC1 is the major beta-barrel channel of the mitochondrial outer membrane. Reason: Core location, established by fractionation, imaging and electrophysiology of the purified protein. Supporting Evidence: Reactome:R-HSA-9012374 file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the |
| GO:0005741 mitochondrial outer membrane | TAS Reactome:R-HSA-9824888 | ACCEPT | Summary: VDAC1 is the major beta-barrel channel of the mitochondrial outer membrane. Reason: Core location, established by fractionation, imaging and electrophysiology of the purified protein. Supporting Evidence: Reactome:R-HSA-9824888 file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the |
| GO:0005741 mitochondrial outer membrane | TAS Reactome:R-HSA-9824892 | ACCEPT | Summary: VDAC1 is the major beta-barrel channel of the mitochondrial outer membrane. Reason: Core location, established by fractionation, imaging and electrophysiology of the purified protein. Supporting Evidence: Reactome:R-HSA-9824892 file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the |
| GO:0005741 mitochondrial outer membrane | TAS Reactome:R-HSA-9824894 | ACCEPT | Summary: VDAC1 is the major beta-barrel channel of the mitochondrial outer membrane. Reason: Core location, established by fractionation, imaging and electrophysiology of the purified protein. Supporting Evidence: Reactome:R-HSA-9824894 file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the |
| GO:0005741 mitochondrial outer membrane | TAS Reactome:R-HSA-9824897 | ACCEPT | Summary: VDAC1 is the major beta-barrel channel of the mitochondrial outer membrane. Reason: Core location, established by fractionation, imaging and electrophysiology of the purified protein. Supporting Evidence: Reactome:R-HSA-9824897 file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the |
| GO:0005741 mitochondrial outer membrane | TAS Reactome:R-HSA-9834070 | ACCEPT | Summary: VDAC1 is the major beta-barrel channel of the mitochondrial outer membrane. Reason: Core location, established by fractionation, imaging and electrophysiology of the purified protein. Supporting Evidence: Reactome:R-HSA-9834070 file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the |
| GO:0005741 mitochondrial outer membrane | TAS Reactome:R-HSA-9840807 | ACCEPT | Summary: VDAC1 is the major beta-barrel channel of the mitochondrial outer membrane. Reason: Core location, established by fractionation, imaging and electrophysiology of the purified protein. Supporting Evidence: Reactome:R-HSA-9840807 file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the |
| GO:0005757 mitochondrial permeability transition pore complex | IDA PMID:26387735 SPG7 Is an Essential and Conserved Component of the Mitochon... | ACCEPT | Summary: VDAC1 is a component of the mitochondrial permeability transition pore complex together with SPG7 and PPIF. Reason: Direct co-purification evidence in human cells; consistent with the long-standing role of VDAC1 in permeability transition and apoptosis. Supporting Evidence: PMID:26387735 SPG7 Is an Essential and Conserved Component of the Mitochondrial Permeability file:human/VDAC1/VDAC1-uniprot.txt Component of the mitochondrial |
| GO:0005886 plasma membrane | EXP PMID:25168729 AΞ² promotes VDAC1 channel dephosphorylation in neuronal lipi... | KEEP AS NON CORE | Summary: A plasma-membrane ("plasmalemmal porin") pool of VDAC1 is reported, notably in neuronal lipid rafts and as a receptor for plasminogen kringle 5. Reason: Retained: several groups report surface VDAC1 with roles in volume regulation and apoptosis, and UniProt records a cell-membrane location. It is nonetheless a minor pool relative to the mitochondrial outer membrane, which is where the channel does its established work. Supporting Evidence: PMID:25168729 The present study demonstrates that VDAC1 associates with APP and AΞ² in lipid rafts of neurons. file:human/VDAC1/VDAC1-uniprot.txt in the plasma membrane it is involved in cell volume |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: A plasma-membrane ("plasmalemmal porin") pool of VDAC1 is reported, notably in neuronal lipid rafts and as a receptor for plasminogen kringle 5. Reason: Retained: several groups report surface VDAC1 with roles in volume regulation and apoptosis, and UniProt records a cell-membrane location. It is nonetheless a minor pool relative to the mitochondrial outer membrane, which is where the channel does its established work. Supporting Evidence: file:human/VDAC1/VDAC1-uniprot.txt in the plasma membrane it is involved in cell volume PMID:25168729 The present study demonstrates that VDAC1 associates with APP and AΞ² in lipid rafts of neurons. |
| GO:0005886 plasma membrane | IDA PMID:25296756 Plasminogen kringle 5 induces endothelial cell apoptosis by ... | KEEP AS NON CORE | Summary: A plasma-membrane ("plasmalemmal porin") pool of VDAC1 is reported, notably in neuronal lipid rafts and as a receptor for plasminogen kringle 5. Reason: Retained: several groups report surface VDAC1 with roles in volume regulation and apoptosis, and UniProt records a cell-membrane location. It is nonetheless a minor pool relative to the mitochondrial outer membrane, which is where the channel does its established work. Supporting Evidence: PMID:25296756 the voltage-dependent anion channel 1 (VDAC1) has been identified as a receptor of K5 file:human/VDAC1/VDAC1-uniprot.txt in the plasma membrane it is involved in cell volume |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: A plasma-membrane ("plasmalemmal porin") pool of VDAC1 is reported, notably in neuronal lipid rafts and as a receptor for plasminogen kringle 5. Reason: Retained: several groups report surface VDAC1 with roles in volume regulation and apoptosis, and UniProt records a cell-membrane location. It is nonetheless a minor pool relative to the mitochondrial outer membrane, which is where the channel does its established work. Supporting Evidence: file:human/VDAC1/VDAC1-uniprot.txt in the plasma membrane it is involved in cell volume PMID:25168729 The present study demonstrates that VDAC1 associates with APP and AΞ² in lipid rafts of neurons. |
| GO:0006820 monoatomic anion transport | IDA PMID:8420959 Cloning and functional expression in yeast of two human isof... | ACCEPT | Summary: VDAC1 mediates anion flux through the membrane. Reason: Core transport role of the open, anion-selective channel. Supporting Evidence: PMID:8420959 Human proteins isolated from yeast mitochondria formed channels with the characteristics expected of VDAC when incorporated into planar lipid bilayers. file:human/VDAC1/VDAC1-uniprot.txt The open state has a weak anion selectivity whereas the closed state is |
| GO:0006915 apoptotic process | IDA PMID:25296756 Plasminogen kringle 5 induces endothelial cell apoptosis by ... | KEEP AS NON CORE | Summary: VDAC1 participates in apoptosis (kringle-5-induced endothelial apoptosis). Reason: Well-supported role in apoptotic signaling via permeability transition and BCL2-family interactions, but downstream of and regulatory to the channel function. Supporting Evidence: PMID:25296756 the voltage-dependent anion channel 1 (VDAC1) has been identified as a receptor of K5 PMID:26387735 SPG7 Is an Essential and Conserved Component of the Mitochondrial Permeability |
| GO:0006915 apoptotic process | TAS PMID:10365962 Bcl-2 family proteins regulate the release of apoptogenic cy... | KEEP AS NON CORE | Summary: VDAC1 implicated in apoptosis (Bax/permeability transition). Reason: Retained as a non-core, regulatory role linked to the permeability transition pore. Supporting Evidence: PMID:26387735 SPG7 Is an Essential and Conserved Component of the Mitochondrial Permeability |
| GO:0008142 oxysterol binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Oxysterol binding transferred from ortholog data. Reason: Consistent with curated lipid-binding properties of VDAC1 (cholesterol, oxysterol, phosphatidylcholine, ceramide), but ancillary to channel and scramblase function. Supporting Evidence: file:human/VDAC1/VDAC1-uniprot.txt Binds various |
| GO:0008142 oxysterol binding | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Oxysterol binding by sequence similarity. Reason: As above: consistent with curated lipid binding, non-core. Supporting Evidence: file:human/VDAC1/VDAC1-uniprot.txt Binds various |
| GO:0008308 voltage-gated monoatomic anion channel activity | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference of voltage-gated anion channel activity for the VDAC family. Reason: Matches direct electrophysiology of human VDAC1; the family-level node is well placed. Supporting Evidence: PMID:8420959 Human proteins isolated from yeast mitochondria formed channels with the characteristics expected of VDAC when incorporated into planar lipid bilayers. file:human/VDAC1/VDAC1-uniprot.txt The open state has a weak anion selectivity whereas the closed state is |
| GO:0008308 voltage-gated monoatomic anion channel activity | IDA PMID:38065946 Phospholipids are imported into mitochondria by VDAC, a dime... | MODIFY | Summary: PMID:38065946 is a scramblase study; by IDA it demonstrates phospholipid scrambling, not channel activity. Reason: This UniProt IDA row maps GO:0008308 voltage-gated anion channel activity to PMID:38065946, but that paper assays phospholipid scramblase activity and explicitly states the mechanism is unrelated to channel conduction; its full text contains no conductance measurement. The activity the paper demonstrates is GO:0017128 phospholipid scramblase activity. VDAC1 channel activity is real and retained by the IBA, IEA, ISS, Reactome and PMID:8420959 rows and the channel core function, so re-pointing this row loses nothing. Proposed replacements: phospholipid scramblase activity Supporting Evidence: PMID:38065946 dimers of human VDAC1 and VDAC2 catalyze rapid transbilayer translocation of phospholipids by a mechanism that is unrelated to their channel activity |
| GO:0008308 voltage-gated monoatomic anion channel activity | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic mapping of voltage-gated anion channel activity. Reason: Consistent with direct evidence. Supporting Evidence: PMID:8420959 Human proteins isolated from yeast mitochondria formed channels with the characteristics expected of VDAC when incorporated into planar lipid bilayers. |
| GO:0008308 voltage-gated monoatomic anion channel activity | ISS GO_REF:0000024 | ACCEPT | Summary: ISS voltage-gated anion channel activity. Reason: Consistent with direct human evidence. Supporting Evidence: PMID:8420959 Human proteins isolated from yeast mitochondria formed channels with the characteristics expected of VDAC when incorporated into planar lipid bilayers. |
| GO:0008308 voltage-gated monoatomic anion channel activity | TAS Reactome:R-HSA-9012374 | ACCEPT | Summary: Reactome voltage-gated anion channel activity. Reason: Consistent with direct evidence. Supporting Evidence: Reactome:R-HSA-9012374 PMID:8420959 Human proteins isolated from yeast mitochondria formed channels with the characteristics expected of VDAC when incorporated into planar lipid bilayers. |
| GO:0015485 cholesterol binding | IDA PMID:31015432 Ceramides bind VDAC2 to trigger mitochondrial apoptosis. | KEEP AS NON CORE | Summary: VDAC1 binds cholesterol. Reason: Supported lipid binding of the barrel; ancillary to the channel and scramblase activities. Supporting Evidence: PMID:31015432 indicating that VDAC1 and VDAC2 are genuine mitochondrial CBPs file:human/VDAC1/VDAC1-uniprot.txt Binds various |
| GO:0016020 membrane | IDA PMID:27641616 TSPO ligands stimulate ZnPPIX transport and ROS accumulation... | MODIFY | Summary: VDAC1 detected in membranes. Reason: Too general: VDAC1 is a multi-pass (beta-barrel) protein of the mitochondrial outer membrane. Proposed replacements: mitochondrial outer membrane Supporting Evidence: file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the |
| GO:0016020 membrane | IEA GO_REF:0000107 | MODIFY | Summary: Electronic membrane localization. Reason: Too general; mitochondrial outer membrane is the supported specific location. Proposed replacements: mitochondrial outer membrane Supporting Evidence: file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the |
| GO:0016020 membrane | ISS GO_REF:0000024 | MODIFY | Summary: ISS membrane localization. Reason: Too general; mitochondrial outer membrane is the supported specific location. Proposed replacements: mitochondrial outer membrane Supporting Evidence: file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the |
| GO:0019901 protein kinase binding | IPI PMID:21370995 Expression of leucine-rich repeat kinase 2 (LRRK2) inhibits ... | KEEP AS NON CORE | Summary: VDAC1 binds protein kinases at the outer membrane. Reason: More informative than bare protein binding and consistent with VDAC1 serving as a docking platform (hexokinases, kinases) on the outer membrane, but not its core activity. Supporting Evidence: PMID:8420959 mitochondria expressing HVDAC1 are capable of specifically binding hexokinase |
| GO:0030855 epithelial cell differentiation | IEP PMID:21492153 Analysis of proteomic changes induced upon cellular differen... | MARK AS OVER ANNOTATED | Summary: IEP correlation of VDAC1 abundance with Caco-2 differentiation. Reason: Expression change during differentiation does not show that VDAC1 executes a step of epithelial differentiation; mitochondrial content changes with differentiation generally. Supporting Evidence: |
| GO:0031210 phosphatidylcholine binding | IDA PMID:31015432 Ceramides bind VDAC2 to trigger mitochondrial apoptosis. | KEEP AS NON CORE | Summary: VDAC1 binds phosphatidylcholine. Reason: Supported lipid binding; related to the scramblase activity but ancillary as a standalone function. Supporting Evidence: PMID:31015432 indicating that VDAC1 and VDAC2 are genuine mitochondrial CBPs file:human/VDAC1/VDAC1-uniprot.txt Binds various |
| GO:0031966 mitochondrial membrane | IDA PMID:31015432 Ceramides bind VDAC2 to trigger mitochondrial apoptosis. | MODIFY | Summary: VDAC1 localizes to mitochondrial membranes. Reason: Correct but general; the specific supported term is mitochondrial outer membrane. Proposed replacements: mitochondrial outer membrane Supporting Evidence: file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the PMID:31015432 indicating that VDAC1 and VDAC2 are genuine mitochondrial CBPs |
| GO:0036444 calcium import into the mitochondrion | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: ISS role in calcium import into mitochondria. Reason: VDAC1 provides the outer-membrane conduit for Ca2+ en route to the MCU, and VDAC1 ubiquitination state modulates mitochondrial Ca2+ uptake; a regulatory/conduit role rather than the core channel description. Supporting Evidence: PMID:32047033 VDAC1 deficient with polyubiquitination (VDAC1 Poly-KR) hampers mitophagy, but VDAC1 deficient with monoubiquitination (VDAC1 K274R) promotes apoptosis by augmenting the mitochondrial calcium uptake through the mitochondrial calcium uniporter (MCU) channel. file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the |
| GO:0042645 mitochondrial nucleoid | IDA PMID:18063578 The layered structure of human mitochondrial DNA nucleoids. | KEEP AS NON CORE | Summary: VDAC1 detected in mitochondrial nucleoid preparations. Reason: Nucleoid fractions retain outer-membrane components; plausible as a peripheral association of the abundant outer-membrane channel rather than a nucleoid function. Supporting Evidence: file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the |
| GO:0042802 identical protein binding | IPI PMID:18832158 Structure of the human voltage-dependent anion channel. | ACCEPT | Summary: VDAC1 self-associates into dimers and higher oligomers. Reason: Oligomerization is directly documented and is required for scramblase activity. Supporting Evidence: PMID:38065946 dimers of human VDAC1 and VDAC2 catalyze rapid transbilayer translocation of phospholipids by a mechanism that is unrelated to their channel activity file:human/VDAC1/VDAC1-uniprot.txt oligomerization is required for scramblase activity |
| GO:0042866 pyruvate biosynthetic process | TAS Reactome:R-HSA-70268 | KEEP AS NON CORE | Summary: Reactome places VDAC1 in pyruvate metabolism (metabolite flux across the outer membrane). Reason: VDAC1 permits diffusion of small metabolites across the outer membrane, so it supports such pathways without catalysing any of their steps. Supporting Evidence: Reactome:R-HSA-70268 file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the |
| GO:0043066 negative regulation of apoptotic process | IMP PMID:32047033 Decision between mitophagy and apoptosis by Parkin via VDAC1... | KEEP AS NON CORE | Summary: VDAC1 ubiquitination state controls the balance between apoptosis and mitophagy. Reason: Supported regulatory role (monoubiquitination-deficient VDAC1 promotes apoptosis), but downstream of the channel function. Supporting Evidence: PMID:32047033 VDAC1 deficient with polyubiquitination (VDAC1 Poly-KR) hampers mitophagy, but VDAC1 deficient with monoubiquitination (VDAC1 K274R) promotes apoptosis by augmenting the mitochondrial calcium uptake through the mitochondrial calcium uniporter (MCU) channel. |
| GO:0044325 transmembrane transporter binding | IPI PMID:25296756 Plasminogen kringle 5 induces endothelial cell apoptosis by ... | KEEP AS NON CORE | Summary: VDAC1 binds a transmembrane transporter (BCL2L1/BAK1-type partners at the outer membrane). Reason: More informative than bare protein binding and consistent with VDAC1 as an outer-membrane interaction hub; non-core. Supporting Evidence: PMID:25296756 the voltage-dependent anion channel 1 (VDAC1) has been identified as a receptor of K5 file:human/VDAC1/VDAC1-uniprot.txt Interacts with BCL2L1 |
| GO:0045121 membrane raft | EXP PMID:25168729 AΞ² promotes VDAC1 channel dephosphorylation in neuronal lipi... | KEEP AS NON CORE | Summary: VDAC1 is present in neuronal lipid rafts at the plasma membrane. Reason: Supported by direct raft fractionation and APP/Abeta association; a minor extramitochondrial pool, non-core relative to the outer-membrane channel. Supporting Evidence: PMID:25168729 The present study demonstrates that VDAC1 associates with APP and AΞ² in lipid rafts of neurons. |
| GO:0045121 membrane raft | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: UniProt mapping to membrane raft. Reason: Consistent with the reported plasmalemmal raft pool; non-core. Supporting Evidence: PMID:25168729 The present study demonstrates that VDAC1 associates with APP and AΞ² in lipid rafts of neurons. file:human/VDAC1/VDAC1-uniprot.txt in the plasma membrane it is involved in cell volume |
| GO:0046930 pore complex | TAS PMID:9843949 Bax interacts with the permeability transition pore to induc... | ACCEPT | Summary: VDAC1 is part of a pore complex of the outer membrane. Reason: Consistent with the beta-barrel channel and its participation in the permeability transition pore complex. Supporting Evidence: PMID:26387735 SPG7 Is an Essential and Conserved Component of the Mitochondrial Permeability |
| GO:0055085 transmembrane transport | IEA GO_REF:0000002 | MODIFY | Summary: InterPro mapping to transmembrane transport. Reason: Correct but general; VDAC1 mediates anion transport across the outer membrane. Proposed replacements: monoatomic anion transmembrane transport Supporting Evidence: PMID:8420959 Human proteins isolated from yeast mitochondria formed channels with the characteristics expected of VDAC when incorporated into planar lipid bilayers. file:human/VDAC1/VDAC1-uniprot.txt The open state has a weak anion selectivity whereas the closed state is |
| GO:0070062 extracellular exosome | HDA PMID:19056867 Large-scale proteomics and phosphoproteomics of urinary exos... | MARK AS OVER ANNOTATED | Summary: Detected in high-throughput exosome proteomes. Reason: VDAC1 is an abundant mitochondrial outer-membrane protein and a common contaminant of vesicle preparations; no targeted evidence supports a functional exosomal pool. Supporting Evidence: file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the |
| GO:0070062 extracellular exosome | HDA PMID:20458337 MHC class II-associated proteins in B-cell exosomes and pote... | MARK AS OVER ANNOTATED | Summary: Detected in high-throughput exosome proteomes. Reason: VDAC1 is an abundant mitochondrial outer-membrane protein and a common contaminant of vesicle preparations; no targeted evidence supports a functional exosomal pool. Supporting Evidence: file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the |
| GO:0070062 extracellular exosome | HDA PMID:23533145 In-depth proteomic analyses of exosomes isolated from expres... | MARK AS OVER ANNOTATED | Summary: Detected in high-throughput exosome proteomes. Reason: VDAC1 is an abundant mitochondrial outer-membrane protein and a common contaminant of vesicle preparations; no targeted evidence supports a functional exosomal pool. Supporting Evidence: file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the |
| GO:0097001 ceramide binding | IDA PMID:31015432 Ceramides bind VDAC2 to trigger mitochondrial apoptosis. | ACCEPT | Summary: VDAC1 binds ceramide (photoaffinity labelling, siRNA validation, MD simulations). Reason: Direct evidence that VDAC1 is a genuine mitochondrial ceramide-binding protein. Supporting Evidence: PMID:31015432 indicating that VDAC1 and VDAC2 are genuine mitochondrial CBPs |
| GO:0098656 monoatomic anion transmembrane transport | IEA GO_REF:0000002 | ACCEPT | Summary: Electronic mapping to anion transmembrane transport. Reason: Consistent with the anion-selective open state of the channel. Supporting Evidence: PMID:8420959 Human proteins isolated from yeast mitochondria formed channels with the characteristics expected of VDAC when incorporated into planar lipid bilayers. file:human/VDAC1/VDAC1-uniprot.txt The open state has a weak anion selectivity whereas the closed state is |
| GO:0110099 negative regulation of calcium import into the mitochondrion | IMP PMID:32047033 Decision between mitophagy and apoptosis by Parkin via VDAC1... | KEEP AS NON CORE | Summary: VDAC1 monoubiquitination limits mitochondrial calcium uptake through MCU. Reason: Supported regulatory role; peripheral to the core channel/scramblase functions. Supporting Evidence: PMID:32047033 VDAC1 deficient with polyubiquitination (VDAC1 Poly-KR) hampers mitophagy, but VDAC1 deficient with monoubiquitination (VDAC1 K274R) promotes apoptosis by augmenting the mitochondrial calcium uptake through the mitochondrial calcium uniporter (MCU) channel. |
| GO:1901524 regulation of mitophagy | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Electronic mapping to regulation of mitophagy. Reason: Consistent with VDAC1 serving as a Parkin substrate whose ubiquitination recruits the autophagy machinery; a regulated substrate role rather than catalysis of mitophagy. Supporting Evidence: PMID:20098416 we identified VDAC1 (voltage-dependent anion channel 1) as a target for Parkin-mediated Lys 27 poly-ubiquitylation and mitophagy PMID:32047033 VDAC1 deficient with polyubiquitination (VDAC1 Poly-KR) hampers mitophagy, but VDAC1 deficient with monoubiquitination (VDAC1 K274R) promotes apoptosis by augmenting the mitochondrial calcium uptake through the mitochondrial calcium uniporter (MCU) channel. |
| GO:1901526 positive regulation of mitophagy | IDA PMID:20098416 PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p6... | KEEP AS NON CORE | Summary: VDAC1 is a target of Parkin Lys27 polyubiquitination required for mitophagy. Reason: Well supported, but the work of mitophagy is performed by Parkin, p62 and the autophagy machinery; VDAC1 is the ubiquitinated platform. Kept as non-core. Supporting Evidence: PMID:20098416 we identified VDAC1 (voltage-dependent anion channel 1) as a target for Parkin-mediated Lys 27 poly-ubiquitylation and mitophagy |
| GO:1903146 regulation of autophagy of mitochondrion | NAS PMID:20098416 PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p6... | KEEP AS NON CORE | Summary: NAS statement on regulation of mitochondrial autophagy. Reason: Same evidence as the Parkin/mitophagy rows; retained as non-core. Supporting Evidence: PMID:20098416 we identified VDAC1 (voltage-dependent anion channel 1) as a target for Parkin-mediated Lys 27 poly-ubiquitylation and mitophagy |
| GO:1905091 positive regulation of type 2 mitophagy | IMP PMID:32047033 Decision between mitophagy and apoptosis by Parkin via VDAC1... | KEEP AS NON CORE | Summary: VDAC1 polyubiquitination promotes type 2 mitophagy. Reason: Supported by the ubiquitination-mutant analysis; non-core for the same reason as the other mitophagy rows. Supporting Evidence: PMID:32047033 VDAC1 deficient with polyubiquitination (VDAC1 Poly-KR) hampers mitophagy, but VDAC1 deficient with monoubiquitination (VDAC1 K274R) promotes apoptosis by augmenting the mitochondrial calcium uptake through the mitochondrial calcium uniporter (MCU) channel. |
| GO:1990542 mitochondrial transmembrane transport | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference of mitochondrial transmembrane transport. Reason: Correct family-level process: VDAC proteins conduct metabolites and ions across the outer membrane. Supporting Evidence: PMID:8420959 Human proteins isolated from yeast mitochondria formed channels with the characteristics expected of VDAC when incorporated into planar lipid bilayers. file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the |
| GO:1990542 mitochondrial transmembrane transport | IDA PMID:38065946 Phospholipids are imported into mitochondria by VDAC, a dime... | ACCEPT | Summary: VDAC dimers translocate phospholipids across the outer membrane. Reason: Direct reconstitution evidence for lipid import across the outer membrane, a second transport function distinct from the channel. Supporting Evidence: PMID:38065946 dimers of human VDAC1 and VDAC2 catalyze rapid transbilayer translocation of phospholipids by a mechanism that is unrelated to their channel activity PMID:38065946 We identify the Voltage Dependent Anion Channel (VDAC), an abundant outer membrane protein, as a scramblase-type lipid transporter that catalyzes lipid entry. |
| GO:2000378 negative regulation of reactive oxygen species metabolic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Electronic mapping to negative regulation of reactive oxygen species metabolism. Reason: Plausible consequence of VDAC1 control over metabolite and calcium flux, but indirect. Supporting Evidence: file:human/VDAC1/VDAC1-uniprot.txt Non-selective voltage-gated ion channel that mediates the |
Loading supporting contentβ¦
Download this section (compressed HTML)Q: How much of cellular VDAC1 is genuinely in the plasma membrane, and by what route does a beta-barrel protein normally targeted to the outer mitochondrial membrane reach the cell surface?
Q: Does the scramblase activity require the same dimer interface in intact mitochondria, and is it regulated separately from channel gating?
Experiment: Quantify surface VDAC1 in neurons and endothelial cells by surface biotinylation and antibody labelling of non-permeabilized cells, with VDAC1 knockout controls, to settle the size and reality of the plasmalemmal pool.
Experiment: Test dimer-interface mutants (scramblase-dead but conduction-competent) in VDAC1/2-null cells for mitochondrial phospholipid import versus metabolite flux.
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