Please use this identifier to cite or link to this item: https://doi.org/10.1038/s42003-021-02528-w
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dc.titleModified N-linked glycosylation status predicts trafficking defective human Piezo1 channel mutations
dc.contributor.authorLi, Jinyuan Vero
dc.contributor.authorNg, Chai-Ann
dc.contributor.authorCheng, Delfine
dc.contributor.authorZhou, Zijing
dc.contributor.authorYao, Mingxi
dc.contributor.authorGuo, Yang
dc.contributor.authorYu, Ze-Yan
dc.contributor.authorRamaswamy, Yogambha
dc.contributor.authorJu, Lining Arnold
dc.contributor.authorKuchel, Philip W.
dc.contributor.authorFeneley, Michael P.
dc.contributor.authorFatkin, Diane
dc.contributor.authorCox, Charles D.
dc.date.accessioned2022-10-12T07:54:54Z
dc.date.available2022-10-12T07:54:54Z
dc.date.issued2021-09-06
dc.identifier.citationLi, Jinyuan Vero, Ng, Chai-Ann, Cheng, Delfine, Zhou, Zijing, Yao, Mingxi, Guo, Yang, Yu, Ze-Yan, Ramaswamy, Yogambha, Ju, Lining Arnold, Kuchel, Philip W., Feneley, Michael P., Fatkin, Diane, Cox, Charles D. (2021-09-06). Modified N-linked glycosylation status predicts trafficking defective human Piezo1 channel mutations. Communications Biology 4 (1) : 1038. ScholarBank@NUS Repository. https://doi.org/10.1038/s42003-021-02528-w
dc.identifier.issn2399-3642
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/232302
dc.description.abstractMechanosensitive channels are integral membrane proteins that sense mechanical stimuli. Like most plasma membrane ion channel proteins they must pass through biosynthetic quality control in the endoplasmic reticulum that results in them reaching their destination at the plasma membrane. Here we show that N-linked glycosylation of two highly conserved asparagine residues in the ‘cap’ region of mechanosensitive Piezo1 channels are necessary for the mature protein to reach the plasma membrane. Both mutation of these asparagines (N2294Q/N2331Q) and treatment with an enzyme that hydrolyses N-linked oligosaccharides (PNGaseF) eliminates the fully glycosylated mature Piezo1 protein. The N-glycans in the cap are a pre-requisite for N-glycosylation in the ‘propeller’ regions, which are present in loops that are essential for mechanotransduction. Importantly, trafficking-defective Piezo1 variants linked to generalized lymphatic dysplasia and bicuspid aortic valve display reduced fully N-glycosylated Piezo1 protein. Thus the N-linked glycosylation status in vitro correlates with efficient membrane trafficking and will aid in determining the functional impact of Piezo1 variants of unknown significance. © 2021, The Author(s).
dc.publisherNature Research
dc.rightsAttribution 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.sourceScopus OA2021
dc.typeArticle
dc.contributor.departmentMECHANOBIOLOGY INSTITUTE
dc.description.doi10.1038/s42003-021-02528-w
dc.description.sourcetitleCommunications Biology
dc.description.volume4
dc.description.issue1
dc.description.page1038
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