Modified N-linked glycosylation status predicts trafficking defective human Piezo1 channel mutations

Li et al. investigates the role of N-linked glycosylation for the function of mechanosensitive ion channel Piezo1. They show that disease-linked loss of function mutations in Piezo1 that are trafficking defective lack N-linked glycosylation.

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Autores principales: Jinyuan Vero Li, Chai-Ann Ng, Delfine Cheng, Zijing Zhou, Mingxi Yao, Yang Guo, Ze-Yan Yu, Yogambha Ramaswamy, Lining Arnold Ju, Philip W. Kuchel, Michael P. Feneley, Diane Fatkin, Charles D. Cox
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Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/838c42e3bd25417ab25bf8adfdc60922
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spelling oai:doaj.org-article:838c42e3bd25417ab25bf8adfdc609222021-12-02T17:19:12ZModified N-linked glycosylation status predicts trafficking defective human Piezo1 channel mutations10.1038/s42003-021-02528-w2399-3642https://doaj.org/article/838c42e3bd25417ab25bf8adfdc609222021-09-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-02528-whttps://doaj.org/toc/2399-3642Li et al. investigates the role of N-linked glycosylation for the function of mechanosensitive ion channel Piezo1. They show that disease-linked loss of function mutations in Piezo1 that are trafficking defective lack N-linked glycosylation.Jinyuan Vero LiChai-Ann NgDelfine ChengZijing ZhouMingxi YaoYang GuoZe-Yan YuYogambha RamaswamyLining Arnold JuPhilip W. KuchelMichael P. FeneleyDiane FatkinCharles D. CoxNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-17 (2021)
institution DOAJ
collection DOAJ
language EN
topic Biology (General)
QH301-705.5
spellingShingle Biology (General)
QH301-705.5
Jinyuan Vero Li
Chai-Ann Ng
Delfine Cheng
Zijing Zhou
Mingxi Yao
Yang Guo
Ze-Yan Yu
Yogambha Ramaswamy
Lining Arnold Ju
Philip W. Kuchel
Michael P. Feneley
Diane Fatkin
Charles D. Cox
Modified N-linked glycosylation status predicts trafficking defective human Piezo1 channel mutations
description Li et al. investigates the role of N-linked glycosylation for the function of mechanosensitive ion channel Piezo1. They show that disease-linked loss of function mutations in Piezo1 that are trafficking defective lack N-linked glycosylation.
format article
author Jinyuan Vero Li
Chai-Ann Ng
Delfine Cheng
Zijing Zhou
Mingxi Yao
Yang Guo
Ze-Yan Yu
Yogambha Ramaswamy
Lining Arnold Ju
Philip W. Kuchel
Michael P. Feneley
Diane Fatkin
Charles D. Cox
author_facet Jinyuan Vero Li
Chai-Ann Ng
Delfine Cheng
Zijing Zhou
Mingxi Yao
Yang Guo
Ze-Yan Yu
Yogambha Ramaswamy
Lining Arnold Ju
Philip W. Kuchel
Michael P. Feneley
Diane Fatkin
Charles D. Cox
author_sort Jinyuan Vero Li
title Modified N-linked glycosylation status predicts trafficking defective human Piezo1 channel mutations
title_short Modified N-linked glycosylation status predicts trafficking defective human Piezo1 channel mutations
title_full Modified N-linked glycosylation status predicts trafficking defective human Piezo1 channel mutations
title_fullStr Modified N-linked glycosylation status predicts trafficking defective human Piezo1 channel mutations
title_full_unstemmed Modified N-linked glycosylation status predicts trafficking defective human Piezo1 channel mutations
title_sort modified n-linked glycosylation status predicts trafficking defective human piezo1 channel mutations
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/838c42e3bd25417ab25bf8adfdc60922
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