Evidence map›Paper›PMID 34489534›Full record

ArticleCommunications biology2021

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

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 and 3 more

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.4field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

25 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. The Sirt1-Piezo1 Axis Promotes Bone Formation and Repair in Mice.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Open biology · 2025
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Mechanisms of PIEZO Channel Inactivation.International journal of molecular sciences · 2023
    Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors at 3 institutions in 2 countries.

Jinyuan Vero LiMolecular Cardiology and Biophysics Division, Victor Chang Cardiac Research Institute, Sydney, Australia.
Chai-Ann NgMolecular Cardiology and Biophysics Division, Victor Chang Cardiac Research Institute, Sydney, Australia.
Delfine ChengMolecular Cardiology and Biophysics Division, Victor Chang Cardiac Research Institute, Sydney, Australia.
Zijing ZhouMolecular Cardiology and Biophysics Division, Victor Chang Cardiac Research Institute, Sydney, Australia.
Mingxi YaoMechanobiology Institute, National University of Singapore, Singapore, Singapore.
Yang GuoMolecular Cardiology and Biophysics Division, Victor Chang Cardiac Research Institute, Sydney, Australia.
Ze-Yan YuMolecular Cardiology and Biophysics Division, Victor Chang Cardiac Research Institute, Sydney, Australia.
Yogambha RamaswamySchool of Biomedical Engineering, Faculty of Engineering, The University of Sydney, Camperdown, NSW, Australia.
Lining Arnold JuSchool of Biomedical Engineering, Faculty of Engineering, The University of Sydney, Camperdown, NSW, Australia.ORCID http://orcid.org/0000-0002-7591-0864
Philip W KuchelSchool of Life and Environmental Sciences, University of Sydney, Sydney, NSW, Australia.
Michael P FeneleyMolecular Cardiology and Biophysics Division, Victor Chang Cardiac Research Institute, Sydney, Australia.
Diane FatkinMolecular Cardiology and Biophysics Division, Victor Chang Cardiac Research Institute, Sydney, Australia.
Charles D CoxMolecular Cardiology and Biophysics Division, Victor Chang Cardiac Research Institute, Sydney, Australia. c.cox@victorchang.edu.au.ORCID http://orcid.org/0000-0002-3802-6746
Victor Chang Cardiac Research Institute · AUThe University of Sydney · AUNational University of Singapore · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mechanosensitive 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.

Indexed as

Ion Channel GatingMechanotransduction, CellularMutationCell MembraneGlycosylationHumansIon ChannelsIon ChannelsPIEZO1 protein, human

Identifiers

PMID34489534
PMCPMC8421374
OpenAlexW3196666911

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.