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Architecture of the mitochondrial calcium uniporter

Author

Listed:
  • Kirill Oxenoid

    (Harvard Medical School)

  • Ying Dong

    (State Key Laboratory of Molecular Biology, National Center for Protein Science Shanghai, Shanghai Institute of Biochemistry and Cell Biology, Shanghai Science Research Center, Chinese Academy of Sciences)

  • Chan Cao

    (Harvard Medical School
    State Key Laboratory of Elemento-Organic Chemistry and College of Chemistry, Nankai University)

  • Tanxing Cui

    (Harvard Medical School)

  • Yasemin Sancak

    (Massachusetts General Hospital)

  • Andrew L. Markhard

    (Massachusetts General Hospital)

  • Zenon Grabarek

    (Massachusetts General Hospital)

  • Liangliang Kong

    (State Key Laboratory of Molecular Biology, National Center for Protein Science Shanghai, Shanghai Institute of Biochemistry and Cell Biology, Shanghai Science Research Center, Chinese Academy of Sciences)

  • Zhijun Liu

    (State Key Laboratory of Molecular Biology, National Center for Protein Science Shanghai, Shanghai Institute of Biochemistry and Cell Biology, Shanghai Science Research Center, Chinese Academy of Sciences)

  • Bo Ouyang

    (State Key Laboratory of Molecular Biology, National Center for Protein Science Shanghai, Shanghai Institute of Biochemistry and Cell Biology, Shanghai Science Research Center, Chinese Academy of Sciences)

  • Yao Cong

    (State Key Laboratory of Molecular Biology, National Center for Protein Science Shanghai, Shanghai Institute of Biochemistry and Cell Biology, Shanghai Science Research Center, Chinese Academy of Sciences)

  • Vamsi K. Mootha

    (Massachusetts General Hospital)

  • James J. Chou

    (Harvard Medical School
    State Key Laboratory of Molecular Biology, National Center for Protein Science Shanghai, Shanghai Institute of Biochemistry and Cell Biology, Shanghai Science Research Center, Chinese Academy of Sciences)

Abstract

The structure of the core region of the mitochondrial calcium uniporter (MCU) is determined by NMR and electron microscopy, revealing that MCU is a homo-pentamer with a specific transmembrane helix forming a hydrophilic pore across the membrane, and representing one of the largest membrane protein structures characterized by NMR spectroscopy.

Suggested Citation

  • Kirill Oxenoid & Ying Dong & Chan Cao & Tanxing Cui & Yasemin Sancak & Andrew L. Markhard & Zenon Grabarek & Liangliang Kong & Zhijun Liu & Bo Ouyang & Yao Cong & Vamsi K. Mootha & James J. Chou, 2016. "Architecture of the mitochondrial calcium uniporter," Nature, Nature, vol. 533(7602), pages 269-273, May.
    • Handle: RePEc:nat:nature:v:533:y:2016:i:7602:d:10.1038_nature17656
    DOI: 10.1038/nature17656
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    Cited by:

    1. Enrique Balderas & David R. Eberhardt & Sandra Lee & John M. Pleinis & Salah Sommakia & Anthony M. Balynas & Xue Yin & Mitchell C. Parker & Colin T. Maguire & Scott Cho & Marta W. Szulik & Anna Bakhti, 2022. "Mitochondrial calcium uniporter stabilization preserves energetic homeostasis during Complex I impairment," Nature Communications, Nature, vol. 13(1), pages 1-17, December.

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