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

Yong Yu, Maximilian H. Ulbrich, Ming-hui Li, Scott Dobbins, Wei K. Zhang, Liang Tong, Ehud Y. Isacoff and Jian Yang ()
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Yong Yu: Columbia University
Maximilian H. Ulbrich: University of California
Ming-hui Li: Columbia University
Scott Dobbins: Columbia University
Wei K. Zhang: Columbia University
Liang Tong: Columbia University
Ehud Y. Isacoff: University of California
Jian Yang: Columbia University

Nature Communications, 2012, vol. 3, issue 1, 1-11

Abstract: 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.

Date: 2012
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DOI: 10.1038/ncomms2257

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