Journal
ANNUAL REVIEW OF BIOCHEMISTRY
Volume 91, Issue -, Pages 679-703Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev-biochem-032620-104527
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Funding
- JSPS KAKENHI [15H05705, 2222703, 20H02583, 18K11543, 21H03551]
- AMED CREST grant [21gm1410002h0002]
- Takeda Science Foundation
- Platform Project for Supporting Drug Discovery and Life Science Research [Basis for Supporting Innovative Drug Discovery and Life Science Research (BINDS)] from AMED [JP21am0101114]
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Mitochondria play a crucial role in energy production, metabolism, signaling, and apoptosis. The cell relies on translocators in the mitochondrial membranes to import mitochondrial proteins from the cytosol. Recent high-resolution structures have provided insights into the pathways and exits for the translocation of mitochondrial precursor proteins.
Mitochondria are central to energy production, metabolism and signaling, and apoptosis. To make new mitochondria from preexisting mitochondria, the cell needs to import mitochondrial proteins from the cytosol into the mitochondria with the aid of translocators in the mitochondrial membranes. The translocase of the outer membrane (TOM) complex, an outer membrane translocator, functions as an entry gate for most mitochondrial proteins. Although high-resolution structures of the receptor subunits of the TOM complex were deposited in the early 2000s, those of entire TOM complexes became available only in 2019. The structural details of these TOM complexes, consisting of the dimer of the beta-barrel import channel Tom40 and four a-helical membrane proteins, revealed the presence of several distinct paths and exits for the translocation of over 1,000 different mitochondrial precursor proteins. High-resolution structures of TOM complexes now open up a new era of studies on the structures, functions, and dynamics of the mitochondrial import system.
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