期刊
STRUCTURE
卷 25, 期 11, 页码 1645-+出版社
CELL PRESS
DOI: 10.1016/j.str.2017.08.013
关键词
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资金
- CNRS [TGIR-RMN-THC Fr3050]
- Program Transversal de Recherche from Institut Pasteur (PTR) [483]
- European Union [FP7-IDEAS-ERC 294809]
- Ministere de l'Enseignement Superieur et de la Recherche [883/2013]
- Comite Berthe Fouassier - Maladies de l'oeil de la Fondation de France [00071779]
Hearing relies on the transduction of sound-evoked vibrations into electric signals, occurring in the stereocilia bundle of hair cells. The bundle is organized in a staircase pattern formed by rows of packed stereocilia. This architecture is pivotal to transduction and involves a network of scaffolding proteins with hitherto uncharacterized features. Key interactions in this network are mediated by PDZ domains. Here, we describe the architecture of the first two PDZ domains of whirlin, a protein involved in these assemblies and associated with congenital deafblindness. C-terminal hairpin extensions of the PDZ domains mediate the transient supramodular assembly, which improves the binding capacity of the first domain. We determined a detailed structural model of the closed conformation of the PDZ tandem and characterized its equilibrium with an ensemble of open conformations. The structural and dynamic behavior of this PDZ tandem provides key insights into the regulatory mechanisms involved in the hearing machinery.
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