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Molecular mechanism of the assembly of an acid-sensing receptor ion channel complex

Author

Listed:
  • Yong Yu

    (Columbia University
    Present address: Department of Biological Sciences, St John’s University, Queens, New York 11439, USA)

  • Maximilian H. Ulbrich

    (University of California
    Institute of Physiology, University of Freiburg
    BIOSS Centre for Biological Signalling Studies, University of Freiburg)

  • Ming-hui Li

    (Columbia University)

  • Scott Dobbins

    (Columbia University)

  • Wei K. Zhang

    (Columbia University)

  • Liang Tong

    (Columbia University)

  • Ehud Y. Isacoff

    (University of California
    Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA)

  • Jian Yang

    (Columbia University)

Abstract

Polycystic kidney disease (PKD) family proteins associate with transient receptor potential (TRP) channel family proteins to form functionally important complexes. PKD proteins differ from known ion channel-forming proteins and are generally thought to act as membrane receptors. Here we find that PKD1L3, a PKD protein, functions as a channel-forming subunit in an acid-sensing heteromeric complex formed by PKD1L3 and TRPP3, a TRP channel protein. Single amino-acid mutations in the putative pore region of both proteins alter the channel’s ion selectivity. The PKD1L3/TRPP3 complex in the plasma membrane of live cells contains one PKD1L3 and three TRPP3. A TRPP3 C-terminal coiled-coil domain forms a trimer in solution and in crystal, and has a crucial role in the assembly and surface expression of the PKD1L3/TRPP3 complex. These results demonstrate that PKD subunits constitute a new class of channel-forming proteins, enriching our understanding of the function of PKD proteins and PKD/TRPP complexes.

Suggested Citation

  • Yong Yu & Maximilian H. Ulbrich & Ming-hui Li & Scott Dobbins & Wei K. Zhang & Liang Tong & Ehud Y. Isacoff & Jian Yang, 2012. "Molecular mechanism of the assembly of an acid-sensing receptor ion channel complex," Nature Communications, Nature, vol. 3(1), pages 1-11, January.
    • Handle: RePEc:nat:natcom:v:3:y:2012:i:1:d:10.1038_ncomms2257
    DOI: 10.1038/ncomms2257
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