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tom9.2 Is a Calmodulin-Binding Protein Critical for tom complex Assembly but Not for Mitochondrial Protein Import in Arabidopsis thaliana

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Molecular Plant 2017年第4期10卷 575-589页

作者： Nargis Parvin Chris Carrie Isabelle Pabst Antonia Laber Debabrata Laha Melanie V. Paul Peter Geigenberger Ralf Heermann Kirsten Jung Ute C. Vothknecht Fatima Chigri Department Biology I Botany Ludwig-Maximilians-University Munich GroBhaderner Stra6e 2-4 82152 Martinsried Germany Department Biology 1 Microbiology Ludwig-Maximilians-University Munich Grobhaderner Strabe 2-4 82152 Martinsried Germany Department of Biology Center for Integrated Protein Science (Munich) Ludwig-Maximilians-University Munich 81377 Munich Germany Center for Plant Molecular Biology Plant Physiology University of Tuebingen Auf der Morgenstelle 32 72076 Tuebingen Germany present address: Plant Cell Biology IZMB University of Bonn Kirschallee 153115 Bonn Germany Present address: Center for Plant Molecular Biology Developmental Genetics University of Tubingen Auf der Morgenstelle 32 72076 Tubingen Germany

The translocon on the outer membrane of mitochondria （tom） facilitates the import of nuclear-encoded proteins. The principal machinery of mitochondrial protein transport seems conserved in eukaryotes; however, divergence in the composition and structure of tom components has been observed between mammals, yeast, and plants. tom9, the plant homolog of yeast tom22, is significantly smaller due to a truncation in the cytosolic receptor domain, and its precise function is not understood. Here we provide evidence showing that tom9.2 from Arabidopsis thaliana is involved in the formation of mature tom com- plex, most likely by influencing the assembly of the pore-forming subunit tom40. Dexamethasone- induced RNAi gene silencing of tom9.2 results in a severe reduction in the mature tom complex, and the assembly of newly imported tom40 into the complex is impaired. Nevertheless, mutant plants are fully viable and no obvious downstream effects of the loss of tom complex, i.e., on mitochondrial import ca- pacity, were observed. Furthermore, we found that tom9.2 can bind calmodulin （CAM） in vitro and that CaM impairs the assembly of tom complex in the isolated wild-type mitochondria, suggesting a regula- tory role of tom9.2 and a possible integration of tom assembly into the cellular calcium signaling network.

关键词： protein import plant mitochondria tom complex calmodulin calcium signaling

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Mitochondrial protein import regulates cytosol protein homeostasis and neuronal integrity

Mitochondrial protein import regulates cytosol protein homeo...

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中国神经科学学会第十二届全国学术会议

作者： Wei Liu Xiuying Duan Xuefei Fang Weina Shang Chao Tong Life Sciences Institute and Innovation Center for Cell Signaling Network Zhejiang University

Neurodegeneration is characterized by protein aggregate deposits and mitochondrial malfunction. It is not clear whether these two phenomena are intrinsically linked or not. RNAi screening data revealed that the loss of tom40, a key subunit of the translocase of the outer mitochondrial membrane complex, leads to abnormal accumulation of large ubiquitin-positive protein aggregates engulfed by autophagosome membranes in cytosol. Autophagy was induced in tom40 RNAi tissues. However, the giant autophagosomes were often not sealed and they failed to fuse with lysosomes. The manipulation of the autophagy pathway in tom40 RNAi tissues indicated that the giant autophagosome-like structures were formed through the fusion of small autophagosomes. The ectopic expression of Pink1 and Park greatly reduced aggregate formation in tom40 RNAi tissues by increasing autophagy/mitophagy. In nerve tissues, the reduction in tom40 activity leads to aggregate formation and neurodegeneration. Surprisingly, rather than diminishing the neurodegeneration phenotypes, the overexpression of Pink1 enhanced the neurodegeneration phenotypes. We proposed a model to demonstrate the mechanism by which mitochondrial protein import defects led to reduced proteasome activity and defective autophagy.

关键词： Neurodegeneration mitochondria tom complex protein aggregates autophagy Drosophila

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