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

Author

Listed:
  • Chengyang Li

    (Huazhong Agricultural University
    Hubei Hongshan Laboratory)

  • Patrick Duckney

    (Durham University)

  • Tong Zhang

    (Huazhong Agricultural University
    Hubei Hongshan Laboratory)

  • Yanshu Fu

    (Huazhong Agricultural University
    Hubei Hongshan Laboratory)

  • Xin Li

    (Huazhong Agricultural University)

  • Johan Kroon

    (Durham University)

  • Geert Jaeger

    (Ghent University
    VIB Center for Plant Systems Biology)

  • Yunjiang Cheng

    (Huazhong Agricultural University)

  • Patrick J. Hussey

    (Durham University)

  • Pengwei Wang

    (Huazhong Agricultural University
    Hubei Hongshan Laboratory)

Abstract

ER-mitochondrial 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.

Suggested Citation

  • Chengyang Li & Patrick Duckney & Tong Zhang & Yanshu Fu & Xin Li & Johan Kroon & Geert Jaeger & Yunjiang Cheng & Patrick J. Hussey & Pengwei Wang, 2022. "TraB family proteins are components of ER-mitochondrial contact sites and regulate ER-mitochondrial interactions and mitophagy," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
  • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-33402-w
    DOI: 10.1038/s41467-022-33402-w
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    References listed on IDEAS

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    1. Rajat Puri & Xiu-Tang Cheng & Mei-Yao Lin & Ning Huang & Zu-Hang Sheng, 2019. "Mul1 restrains Parkin-mediated mitophagy in mature neurons by maintaining ER-mitochondrial contacts," Nature Communications, Nature, vol. 10(1), pages 1-19, December.
    2. Maho Hamasaki & Nobumichi Furuta & Atsushi Matsuda & Akiko Nezu & Akitsugu Yamamoto & Naonobu Fujita & Hiroko Oomori & Takeshi Noda & Tokuko Haraguchi & Yasushi Hiraoka & Atsuo Amano & Tamotsu Yoshimo, 2013. "Autophagosomes form at ER–mitochondria contact sites," Nature, Nature, vol. 495(7441), pages 389-393, March.
    3. Faiz Rasul & Fan Zheng & Fenfen Dong & Jiajia He & Ling Liu & Wenyue Liu & Javairia Yousuf Cheema & Wenfan Wei & Chuanhai Fu, 2021. "Emr1 regulates the number of foci of the endoplasmic reticulum-mitochondria encounter structure complex," Nature Communications, Nature, vol. 12(1), pages 1-14, December.
    4. Pengwei Wang & Roman Pleskot & Jingze Zang & Joanna Winkler & Jie Wang & Klaas Yperman & Tong Zhang & Kun Wang & Jinli Gong & Yajie Guan & Christine Richardson & Patrick Duckney & Michael Vandorpe & E, 2019. "Plant AtEH/Pan1 proteins drive autophagosome formation at ER-PM contact sites with actin and endocytic machinery," Nature Communications, Nature, vol. 10(1), pages 1-16, December.
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    1. Luciana Renna & Giovanni Stefano & Maria Paola Puggioni & Sang-Jin Kim & Anastasiya Lavell & John E. Froehlich & Graham Burkart & Stefano Mancuso & Christoph Benning & Federica Brandizzi, 2024. "ER-associated VAP27-1 and VAP27-3 proteins functionally link the lipid-binding ORP2A at the ER-chloroplast contact sites," Nature Communications, Nature, vol. 15(1), pages 1-18, December.

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