Unknown

Dataset Information

0

A protein interaction mechanism for suppressing the mechanosensitive Piezo channels.


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.

SUBMITTER: Zhang T 

PROVIDER: S-EPMC5702604 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications

A protein interaction mechanism for suppressing the mechanosensitive Piezo channels.

Zhang Tingxin T   Chi Shaopeng S   Jiang Fan F   Zhao Qiancheng Q   Xiao Bailong B  

Nature communications 20171127 1


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 Ca<sup>2+</sup> ATPase (SERCA), including the widel  ...[more]

Similar Datasets

| S-EPMC5563776 | biostudies-other
| S-EPMC5854696 | biostudies-literature
| S-EPMC4527171 | biostudies-literature
| S-EPMC5231890 | biostudies-other
| S-EPMC7407875 | biostudies-literature
| S-EPMC6487666 | biostudies-literature
| S-EPMC6349400 | biostudies-literature
| S-EPMC7882944 | biostudies-literature
| S-EPMC5129625 | biostudies-literature
| S-EPMC5079242 | biostudies-literature