Journal
FRONTIERS IN PHYSIOLOGY
Volume 12, Issue -, Pages -Publisher
FRONTIERS MEDIA SA
DOI: 10.3389/fphys.2021.732742
Keywords
beta-barrels; chaperones; mitochondria; outer membrane; TOM complex; VDAC
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Funding
- Deutsche Forschungsgemeinschaft [RA1028/8-2]
- IMPRS From Molecules to Organisms
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VDAC is the most abundant protein in the mitochondrial outer membrane, composed of 19 beta-strands forming a hydrophilic pore and maintained in an import competent conformation by specific cytosolic factors. Recent studies using yeast cells have revealed the mitochondrial targeting signal for VDAC.
Voltage dependent anion-selective channel (VDAC) is the most abundant protein in the mitochondrial outer membrane. It is a membrane embedded beta-barrel protein composed of 19 mostly anti-parallel beta-strands that form a hydrophilic pore. Similar to the vast majority of mitochondrial proteins, VDAC is encoded by nuclear DNA, and synthesized on cytosolic ribosomes. The protein is then targeted to the mitochondria while being maintained in an import competent conformation by specific cytosolic factors. Recent studies, using yeast cells as a model system, have unearthed the long searched for mitochondrial targeting signal for VDAC and the role of cytosolic chaperones and mitochondrial import machineries in its proper biogenesis. In this review, we summarize our current knowledge regarding the early cytosolic stages of the biogenesis of VDAC molecules, the specific targeting of VDAC to the mitochondrial surface, and the subsequent integration of VDAC into the mitochondrial outer membrane by the TOM and TOB/SAM complexes.
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