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The ion channel function of polycystin‐1 in the polycystin‐1/polycystin‐2 complex
Author(s) -
Wang Zhifei,
Ng Courtney,
Liu Xiong,
Wang Yan,
Li Bin,
Kashyap Parul,
Chaudhry Haroon A,
Castro Alexis,
Kalontar Enessa M,
Ilyayev Leah,
Walker Rebecca,
Alexander R Todd,
Qian Feng,
Chen XingZhen,
Yu Yong
Publication year - 2019
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.15252/embr.201948336
Subject(s) - ion channel , function (biology) , microbiology and biotechnology , chemistry , biology , biophysics , biochemistry , receptor
Abstract Autosomal dominant polycystic kidney disease ( ADPKD ) is caused by mutations in PKD 1 or PKD 2 gene, encoding the polycystic kidney disease protein polycystin‐1 and the transient receptor potential channel polycystin‐2 (also known as TRPP 2), respectively. Polycystin‐1 and polycystin‐2 form a receptor–ion channel complex located in primary cilia. The function of this complex, especially the role of polycystin‐1, is largely unknown due to the lack of a reliable functional assay. In this study, we dissect the role of polycystin‐1 by directly recording currents mediated by a gain‐of‐function ( GOF ) polycystin‐1/polycystin‐2 channel. Our data show that this channel has distinct properties from that of the homomeric polycystin‐2 channel. The polycystin‐1 subunit directly contributes to the channel pore, and its eleven transmembrane domains are sufficient for its channel function. We also show that the cleavage of polycystin‐1 at the N‐terminal G protein‐coupled receptor proteolysis site is not required for the activity of the GOF polycystin‐1/polycystin‐2 channel. These results demonstrate the ion channel function of polycystin‐1 in the polycystin‐1/polycystin‐2 complex, enriching our understanding of this channel and its role in ADPKD .

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