VDAC1 transports PYR from cytosol to mitochondrial intermembrane space

Stable Identifier
Reaction [transition]
Homo sapiens
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Like other ions and metabolites, pyruvate (PYR) probably crosses the outer mitochondrial membrane through the relatively non-specific, voltage-dependent anion-selective channel protein 1 (VDAC1). The channel is in a high-conductance, moderately anion-selective state at low membrane potentials (McCommis & Finck, 2015; Najbauer et al., 2022). VDAC1 is inhibited by NO (Cheng et al., 2011). It is unknown if VDAC1 needs to be in the open state to pass PYR. However, humans with defective VDAC1 show impaired PYR oxidation and ATP production (Huizing et al. 1996). The role of VDAC1 in mitochondrial dysfunction and disease was reviewed in Varughese et al., 2021.
Literature References
PubMed ID Title Journal Year
8726225 Deficiency of the voltage-dependent anion channel: a novel cause of mitochondriopathy

Thinnes, FP, ter Laak, HJ, van den Heuvel, LP, Trijbels, FJ, Smit, LM, Wendel, U, Huizing, M, DePinto, V, Ruitenbeek, W

Pediatr. Res. 1996
25748677 Mitochondrial pyruvate transport: a historical perspective and future research directions

Finck, BN, McCommis, KS

Biochem. J. 2015
21156174 Biphasic effect of nitric oxide on the cardiac voltage-dependent anion channel

Pravdic, D, Kwok, WM, Cheng, Q, Sedlic, F, Bosnjak, ZJ

FEBS Lett 2011
34359907 The Role of Voltage-Dependent Anion Channel in Mitochondrial Dysfunction and Human Disease

Pitt, AS, Varughese, JT, Buchanan, SK

Cells 2021
35164499 Structure and Gating Behavior of the Human Integral Membrane Protein VDAC1 in a Lipid Bilayer

Andreas, LB, Najbauer, EE, Griesinger, C, Giller, K, Benz, R, Becker, S, Tekwani Movellan, K

J Am Chem Soc 2022
Catalyst Activity

voltage-gated anion channel activity of VDAC1 [mitochondrial outer membrane]

This event is regulated
Negatively by
Orthologous Events
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