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TraB family proteins are components of ER-mitochondrial contact sites and regulate ER-mitochondrial interactions and mitophagy

Li, Chengyang; Duckney, Patrick; Zhang, Tong; Fu, Yanshu; Li, Xin; Kroon, Johan; De Jaeger, Geert; Cheng, Yunjiang; Hussey, Patrick J.; Wang, Pengwei

TraB family proteins are components of ER-mitochondrial contact sites and regulate ER-mitochondrial interactions and mitophagy Thumbnail


Authors

Chengyang Li

Tong Zhang

Yanshu Fu

Xin Li

Geert De Jaeger

Yunjiang Cheng

Pengwei Wang



Abstract

ER-mitochondria contact sites (EMCSs) are important for mitochondrial function. Here, we have identified a EMCS complex, comprising a family of uncharacterised mitochondrial outer membrane proteins, TRB1, TRB2 and the ER protein, VAP27-1. In Arabidopsis, there are three TraB family isoforms and the trb1 trb2 double mutant exhibits abnormal mitochondrial morphology, strong starch accumulation and impaired energy metabolism, indicating that these proteins are essential for normal mitochondrial function. Moreover, TRB1 and TRB2 proteins also interact with ATG8 in order to regulate mitochondrial degradation (mitophagy). The turnover of depolarised mitochondria is significantly reduced in both trb1 trb2 and VAP27 mutants (vap27-1,3,4,6) under mitochondrial stress conditions, with an increased population of dysfunctional mitochondria present in the cytoplasm. Consequently, plant recovery after stress is significantly perturbed, suggesting that TRB1 regulated mitophagy and ER-mitochondrial interaction are two closely related processes. Taken together, we ascribe a dual role to TraB family proteins which are component of the EMCS complex in eukaryotes, regulating both interaction of the mitochondria to the ER and mitophagy.

Citation

Li, C., Duckney, P., Zhang, T., Fu, Y., Li, X., Kroon, J., De Jaeger, G., Cheng, Y., Hussey, P. J., & Wang, P. (2022). TraB family proteins are components of ER-mitochondrial contact sites and regulate ER-mitochondrial interactions and mitophagy. Nature Communications, 13, Article 5658. https://doi.org/10.1038/s41467-022-33402-w

Journal Article Type Article
Acceptance Date Sep 16, 2022
Online Publication Date Sep 26, 2022
Publication Date 2022
Deposit Date Sep 26, 2022
Publicly Available Date Sep 27, 2022
Journal Nature Communications
Publisher Nature Research
Peer Reviewed Peer Reviewed
Volume 13
Article Number 5658
DOI https://doi.org/10.1038/s41467-022-33402-w
Public URL https://durham-repository.worktribe.com/output/1191107

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http://creativecommons.org/licenses/by/4.0/

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This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.






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