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Nat Commun. 2012;3:1252. doi: 10.1038/ncomms2257.

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

Author information

1
Department of Biological Sciences, Columbia University, New York, New York 10027, USA.

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.

PMID:
23212381
PMCID:
PMC3575195
DOI:
10.1038/ncomms2257
[Indexed for MEDLINE]
Free PMC Article

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