Cryo-EM reveals a right-handed double-helix dimer architecture of PCDH15

Tip links connect the stereocilia of mechanosensory hair cells in the inner ear and transmit force onto mechanotransduction (MET) channels. Tip links consist of protocadherin 15 (PCDH15) and cadherin 23, which assemble into an extracellular filament approximately 150 nm in length. Rare freeze-etched electron microscopy (EM) images have suggested that tip links could be right-handed double helices in vivo, but direct structural evidence has been lacking. Using cryo-EM we determined the structure of a large part of the extracellular PCDH15 domain. Two PCDH15 molecules form a parallel cis dimer stabilized by several dimerization interfaces, including two strand crossovers and two parallel contacts, yielding a right-handed double helix. Functional studies show that mutations in PCDH15 dimerization-domains impair MET. Our results establish the molecular foundation for how PCDH15 forms a right-handed double helix to enable mechanical sensing.

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Publication Details

Journal
Proceedings of the National Academy of Sciences
Published
2026-06-09
DOI
https://doi.org/10.1073/pnas.2607573123
Primary Topic
Hearing, Cochlea, Tinnitus, Genetics
Type
article
Field-Weighted Citation Impact
0.00

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article

Cryo-EM reveals a right-handed double-helix dimer architecture of PCDH15

Edward C. Twomey, Xufeng Qiu, Ulrich Müller, Roshan Pathak et al.
Proceedings of the National Academy of Sciences
Hearing, Cochlea, Tinnitus, Genetics
article

Cryo-EM reveals a right-handed double-helix dimer architecture of PCDH15

Edward C. Twomey, Xufeng Qiu, Ulrich Müller, Roshan Pathak, Xiaoping Liang, Lucas Dillard
article en

Abstract

Tip links connect the stereocilia of mechanosensory hair cells in the inner ear and transmit force onto mechanotransduction (MET) channels. Tip links consist of protocadherin 15 (PCDH15) and cadherin 23, which assemble into an extracellular filament approximately 150 nm in length. Rare freeze-etched electron microscopy (EM) images have suggested that tip links could be right-handed double helices in vivo, but direct structural evidence has been lacking. Using cryo-EM we determined the structure of a large part of the extracellular PCDH15 domain. Two PCDH15 molecules form a parallel cis dimer stabilized by several dimerization interfaces, including two strand crossovers and two parallel contacts, yielding a right-handed double helix. Functional studies show that mutations in PCDH15 dimerization-domains impair MET. Our results establish the molecular foundation for how PCDH15 forms a right-handed double helix to enable mechanical sensing.

Proceedings of the National Academy of SciencesVol. 123(24)
Johns Hopkins University (US), Johns Hopkins Medicine (US)
National Institute on Deafness and Other Communication Disorders, National Institute of General Medical Sciences
Openalex Percentile: Top 8%
Hearing, Cochlea, Tinnitus, Genetics
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Cryo-EM reveals a right-handed double-helix dimer architecture of PCDH15 — Edward C. Twomey, Xufeng Qiu, et al. · Proceedings of the National Academy of Sciences (2026) | TGRS Research Map | TGRS