Evidence map›Paper›PMID 31785815›Full record

ArticleBiochemical and biophysical research communications2020

PRRT2 frameshift mutation reduces its mRNA stability resulting loss of function in paroxysmal kinesigenic dyskinesia.

Yongcheng Pan, Qiong Liu, Jennifer Zhang, Yang Yang, Yun Tian, Junsheng Zeng, Peng Yin, Lin Mei, Wen-Cheng Xiong, Xiao-Jiang Li and 2 more

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

6 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Four NovelInternational journal of molecular sciences · 2022
    Article
  5. Article
  6. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 5 institutions in 2 countries.

Yongcheng PanKey Laboratory of Hunan Province in Neurodegenerative Disorders, Xiangya Hospital, Central South University, Changsha, Hunan, China; Department of Human Genetics, Emory University School of Medicine, Atlanta, GA, 30322, USA.
Qiong LiuKey Laboratory of Hunan Province in Neurodegenerative Disorders, Xiangya Hospital, Central South University, Changsha, Hunan, China; Department of Human Genetics, Emory University School of Medicine, Atlanta, GA, 30322, USA.
Jennifer ZhangDepartment of Human Genetics, Emory University School of Medicine, Atlanta, GA, 30322, USA.
Yang YangDepartment of Neurology, Xiangya Hospital, Central South University, Changsha, Hunan, China.
Yun TianDepartment of Geriatrics, Xiangya Hospital, Central South University, Changsha, Hunan, China; Department of Neurosciences, Case Western Reserve University, Cleveland, OH, 44106, USA.
Junsheng ZengDepartment of Neurology, Xiangya Hospital, Central South University, Changsha, Hunan, China.
Peng YinGuangdong-Hongkong-Macau Institute of CNS Regeneration, Ministry of Education CNS Regeneration Collaborative Joint Laboratory, Jinan University, Guangzhou, China.
Lin MeiDepartment of Neurosciences, Case Western Reserve University, Cleveland, OH, 44106, USA.
Wen-Cheng XiongDepartment of Neurosciences, Case Western Reserve University, Cleveland, OH, 44106, USA.
Xiao-Jiang LiGuangdong-Hongkong-Macau Institute of CNS Regeneration, Ministry of Education CNS Regeneration Collaborative Joint Laboratory, Jinan University, Guangzhou, China. Electronic address: xjli33@jnu.edu.cn.
Shihua LiGuangdong-Hongkong-Macau Institute of CNS Regeneration, Ministry of Education CNS Regeneration Collaborative Joint Laboratory, Jinan University, Guangzhou, China. Electronic address: lishihualis@jnu.edu.cn.
Beisha TangKey Laboratory of Hunan Province in Neurodegenerative Disorders, Xiangya Hospital, Central South University, Changsha, Hunan, China; Department of Neurology, Xiangya Hospital, Central South University, Changsha, Hunan, China; National Clinical Research Center for Geriatric Disorders, Xiangya Hospital, Central South University, Changsha, Hunan, China; Center for Medical Genetics, School of Life Sciences, Central South University, Changsha, Hunan, China. Electronic address: bstang7398@163.com.
Case Western Reserve University · USJinan University · CNCentral South University · CNEmory University · USXiangya Hospital Central South University · CN

Funding

Neuronal function of huntingtin-associated proteinR01NS036232 · NINDS · EMORY UNIVERSITY · PI ESCAYG, ANDREW P · 1998 to 2021
$6.7M
NINDS NIH HHS R01 NS036232
6 · The paper itself

Abstract

A heterozygous frameshift PRRT2 mutation (c.649_650InsC) has been identified as the major causative mutation in several paroxysmal disorders, including paroxysmal kinesigenic dyskinesia (PKD). Since PKD is an autosomal dominant disorder and since the frameshift mutations of PRRT2 may create a truncated protein, it remains unclear whether this mutation causes toxic gain of function or loss of function. By generating Prrt2 knock-in (KI) mice that express human PRRT2 with the c.649_650InsC mutation and by comparing the phenotypes of Prrt2 KI mice with knockout (KO) mice, we find that both KI and KO mice show the same extents of impaired rotarod and balance beam performance as well as the same sensitivity to seizure induction. Both KI and KO mice show altered formation of SNARE complex and number of synaptic vesicles. In addition, western blotting of KI mouse brain tissues could not detect truncated PRRT2 protein that might be generated by the c.649_650InsC mutation. Moreover, the level of PRRT2 mRNA in KI mice is significantly decreased, recapitulating the reduction of PRRT2 mRNA reported in PKD patients. Furthermore, mutant PRRT2 mRNA is unstable and showed shortened half-life than wild-type PRRT2 mRNA. Our studies suggest that PRRT2 frameshift mutation leads to the loss of function by affecting its mRNA stability, a mechanism that is different from haploinsufficiency due to dysfunctional protein or gain of function caused by truncated protein.

Indexed as

Frameshift MutationAnimalsDystoniaGene Knock-In TechniquesHumansLoss of Function MutationMembrane ProteinsMiceMice, KnockoutNerve Tissue ProteinsRNA, MessengerMembrane ProteinsNerve Tissue ProteinsPRRT2 protein, humanRNA, MessengerDecreased mRNA stabilityFrameshift mutationLoss of functionPrrt2 KI miceTruncated protein

Identifiers

PMID31785815
PMCPMC6981028
OpenAlexW2991604209

What OpenQuestion holds

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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.