Evidence map›Paper›PMID 34149831›Full record

ArticleThe journal of venomous animals and toxins including tropical diseases2021

Glycosylation of β1 subunit plays a pivotal role in the toxin sensitivity and activation of BK channels.

Xiaoli Wang, Qian Xiao, Yudan Zhu, Hong Qi, Dongxiao Qu, Yu Yao, Yuxiang Jia, Jingkan Guo, Jiwei Cheng, Yonghua Ji and 2 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The journal of venomous animals and toxins including tropical diseases, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 48% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
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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

12 authors at 3 institutions in 1 country.

Xiaoli WangInstitute of Biomembrane and Biopharmaceutics, Shanghai University, Shanghai, China.
Qian XiaoDepartment of Neurology and Central Laboratory, Putuo Hospital, Shanghai University of Traditional Chinese Medicine, Shanghai, China.
Yudan ZhuDepartment of Neurology and Central Laboratory, Putuo Hospital, Shanghai University of Traditional Chinese Medicine, Shanghai, China.
Hong QiInstitute of Biomembrane and Biopharmaceutics, Shanghai University, Shanghai, China.
Dongxiao QuDepartment of Neurology and Central Laboratory, Putuo Hospital, Shanghai University of Traditional Chinese Medicine, Shanghai, China.
Yu YaoInstitute of Biomembrane and Biopharmaceutics, Shanghai University, Shanghai, China.
Yuxiang JiaInstitute of Biomembrane and Biopharmaceutics, Shanghai University, Shanghai, China.
Jingkan GuoInstitute of Biomembrane and Biopharmaceutics, Shanghai University, Shanghai, China.
Jiwei ChengDepartment of Neurology and Central Laboratory, Putuo Hospital, Shanghai University of Traditional Chinese Medicine, Shanghai, China.
Yonghua JiInstitute of Biomembrane and Biopharmaceutics, Shanghai University, Shanghai, China.ORCID 0000-0002-1866-3211
Guoyi LiDepartment of Neurology and Central Laboratory, Putuo Hospital, Shanghai University of Traditional Chinese Medicine, Shanghai, China.ORCID 0000-0002-3089-2404
Jie TaoDepartment of Neurology and Central Laboratory, Putuo Hospital, Shanghai University of Traditional Chinese Medicine, Shanghai, China.ORCID 0000-0002-3873-2413
Shanghai University of Traditional Chinese Medicine · CNShanghai University · CNShanghai Cancer Institute · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe accessory β1 subunits, regulating the pharmacological and biophysical properties of BK channels, always undergo post-translational modifications, especially glycosylation. To date, it remains elusive whether the glycosylation contributes to the regulation of BK channels by β1 subunits.

methodsHerein, we combined the electrophysiological approach with molecular mutations and biochemical manipulation to investigate the function roles of N-glycosylation in β1 subunits.

resultsThe results show that deglycosylation of β1 subunits through double-site mutations (β1 N80A/N142A or β1 N80Q/N142Q) could significantly increase the inhibitory potency of iberiotoxin, a specific BK channel blocker. The deglycosylated channels also have a different sensitivity to martentoxin, another BK channel modulator with some remarkable effects as reported before. On the contrary to enhancing effects of martentoxin on glycosylated BK channels under the presence of cytoplasmic Ca

conclusionThe present study reveals that glycosylation is an indispensable determinant of the modulation of β1-subunit on BK channel pharmacology and its activation. The loss of glycosylation of β1 subunits could lead to the dysfunction of BK channel, resulting in a pathological state.

Indexed as

BK channelsGlycosylationKinetic propertyToxin sensitivityβ1-subunit

Identifiers

PMID34149831
PMCPMC8183112
OpenAlexW3166618447

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Registered trials

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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.