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Structure of the thermo-sensitive TRP channel TRP1 from the alga Chlamydomonas reinhardtii

Author

Listed:
  • Luke L. McGoldrick

    (Columbia University
    Columbia University)

  • Appu K. Singh

    (Columbia University)

  • Lusine Demirkhanyan

    (The University of Illinois College of Medicine at Peoria)

  • Ting-Yu Lin

    (Columbia University)

  • Ryan G. Casner

    (Columbia University
    Columbia University)

  • Eleonora Zakharian

    (The University of Illinois College of Medicine at Peoria)

  • Alexander I. Sobolevsky

    (Columbia University)

Abstract

Algae produce the largest amount of oxygen on earth and are invaluable for human nutrition and biomedicine, as well as for the chemical industry, energy production and agriculture. The mechanisms by which algae can detect and respond to changes in their environments can rely on membrane receptors, including TRP ion channels. Here we present a 3.5-Å resolution cryo-EM structure of the transient receptor potential (TRP) channel crTRP1 from the alga Chlamydomonas reinhardtii that opens in response to increased temperature and is positively regulated by the membrane lipid PIP2. The structure of crTRP1 significantly deviates from the structures of other TRP channels and has a unique 2-fold symmetrical rose-shape architecture with elbow domains and ankyrin repeat domains submerged and dipping into the membrane, respectively. Our study provides a structure of a TRP channel from a micro-organism and a structural framework for better understanding algae biology and TRP channel evolution.

Suggested Citation

  • Luke L. McGoldrick & Appu K. Singh & Lusine Demirkhanyan & Ting-Yu Lin & Ryan G. Casner & Eleonora Zakharian & Alexander I. Sobolevsky, 2019. "Structure of the thermo-sensitive TRP channel TRP1 from the alga Chlamydomonas reinhardtii," Nature Communications, Nature, vol. 10(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-12121-9
    DOI: 10.1038/s41467-019-12121-9
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