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TitleStructural basis of apoptosis induction by the mitochondrial voltage-dependent anion channel.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 9481, Year 2025
Publish dateOct 27, 2025
AuthorsMelina Daniilidis / Umut Günsel / Georgios Broutzakis / Kira D Leitl / Robert Janowski / Kai Fredriksson / Dierk Niessing / Christos Gatsogiannis / Franz Hagn /
PubMed AbstractThe voltage-dependent anion channel (VDAC) is the main gateway for metabolites across the mitochondrial outer membrane. VDAC oligomers are connected to apoptosis induced by various stimuli. However, ...The voltage-dependent anion channel (VDAC) is the main gateway for metabolites across the mitochondrial outer membrane. VDAC oligomers are connected to apoptosis induced by various stimuli. However, the mechanistic and structural basis of apoptosis induction by VDAC remains poorly understood. Here, using cryo-EM and NMR we show that VDAC1 oligomerization or confinement in small lipid nanodiscs triggers the exposure of its N-terminal α-helix (VDAC1-N) which becomes available for partner protein binding. NMR and X-ray crystallography data show that VDAC1-N forms a complex with the BH3 binding groove of the anti-apoptotic Bcl2 protein BclxL. Biochemical assays demonstrate that VDAC1-N exhibits a pro-apoptotic function by promoting pore formation of the executor Bcl2 protein Bak via neutralization of BclxL. This mechanism is reminiscent of BH3-only sensitizer Bcl2 proteins that are efficient inducers of Bax/Bak-mediated mitochondrial outer membrane permeabilization and ultimately apoptosis. The VDAC pathway most likely responds to mitochondrial stress or damage.
External linksNat Commun / PubMed:41145501 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.95 - 7.21 Å
Structure data

EMDB-55061: VDAC1 in cMSP1D1 nanodiscs, monomeric.
Method: EM (single particle) / Resolution: 7.21 Å

EMDB-55062: VDAC1 in cMSP1D1 nanodiscs, dimeric.
Method: EM (single particle) / Resolution: 6.99 Å

EMDB-55094: VDAC1 in cMSP1delH5 nanodiscs
Method: EM (single particle) / Resolution: 5.73 Å

PDB-9hps:
Human BclxLdeltaLT-VDAC1-N fusion protein complex structure
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsAPOPTOSIS / B-cell lymphoma-extra large / BCL-XL / anti-apoptotic / VDAC1 / voltage-dependent anion channel protein / complex / fusion

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