期刊
JOURNAL OF CELL BIOLOGY
卷 211, 期 2, 页码 373-389出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201504062
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资金
- Jane and Aatos Erkko Foundation
- Academy of Finland
- University of Helsinki
- Ella and Georg Ehrnrooth Foundation
Mitochondrial ribosomes synthesize a subset of hydrophobic proteins required for assembly of the oxidative phosphorylation complexes. This process requires temporal and spatial coordination and regulation, so quality control of mitochondrial protein synthesis is paramount to maintain proteostasis. We show how impaired turnover of de nova mitochondrial proteins leads to aberrant protein accumulation in the mitochondrial inner membrane. This creates a stress in the inner membrane that progressively dissipates the mitochondrial membrane potential, which in turn stalls mitochondrial protein synthesis and fragments the mitochondrial network. The mitochondrial m-AAA protease subunit AFG3L2 is critical to this surveillance mechanism that we propose acts as a sensor to couple the synthesis of mitochondrial proteins with organelle fitness, thus ensuring coordinated assembly of the oxidative phosphorylation complexes from two sets of ribosomes.
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