A protein interaction mechanism for suppressing the mechanosensitive Piezo channels

Tingxin Zhang, Shaopeng Chi, Fan Jiang, Qiancheng Zhao and Bailong Xiao ()
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Tingxin Zhang: Tsinghua University
Shaopeng Chi: Tsinghua University
Fan Jiang: Tsinghua University
Qiancheng Zhao: Tsinghua University
Bailong Xiao: Tsinghua University

Nature Communications, 2017, vol. 8, issue 1, 1-13

Abstract: Abstract Piezo proteins are bona fide mammalian mechanotransduction channels for various cell types including endothelial cells. The mouse Piezo1 of 2547 residues forms a three-bladed, propeller-like homo-trimer comprising a central pore-module and three propeller-structures that might serve as mechanotransduction-modules. However, the mechanogating and regulation of Piezo channels remain unclear. Here we identify the sarcoplasmic /endoplasmic-reticulum Ca2+ ATPase (SERCA), including the widely expressed SERCA2, as Piezo interacting proteins. SERCA2 strategically suppresses Piezo1 via acting on a 14-residue-constituted intracellular linker connecting the pore-module and mechanotransduction-module. Mutating the linker impairs mechanogating and SERCA2-mediated modulation of Piezo1. Furthermore, the synthetic linker-peptide disrupts the modulatory effects of SERCA2, demonstrating the key role of the linker in mechanogating and regulation. Importantly, the SERCA2-mediated regulation affects Piezo1-dependent migration of endothelial cells. Collectively, we identify SERCA-mediated regulation of Piezos and the functional significance of the linker, providing important insights into the mechanogating and regulation mechanisms of Piezo channels.

Date: 2017
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DOI: 10.1038/s41467-017-01712-z

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