Evidence map›Paper›PMID 30571846›Full record

ArticleCell biology international2019

RXXPEG motif of MERIT40 is required to maintain spindle structure and function through its interaction with Tankyrase1.

Duo Zheng, Wangqing Xie, Li Li, Wenqi Jiang, Yongdong Zou, Chengyao Chiang, Genze Shao, Kaowen Yan

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell biology international, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.2field-weighted citation impact, top 45% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Review
  2. Functional roles of ADP-ribosylation writers, readers and erasers.Frontiers in cell and developmental biology · 2022
    Review
  3. Review
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

8 authors at 4 institutions in 1 country.

Duo ZhengShenzhen Longhua District Central Hospital, Shenzhen, 518110, China.
Wangqing XieShenzhen Longhua District Central Hospital, Shenzhen, 518110, China.
Li LiDepartment of Cell Biology, School of Basic Medical Sciences, Peking University, Beijing, 100191, China.
Wenqi JiangGuangdong Key Laboratory for Genome Stability and Disease Prevention, Shenzhen University International Cancer Center, Department of Cell Biology and Genetics, Shenzhen University Health Science Center, Shenzhen, 518060, China.
Yongdong ZouGuangdong Key Laboratory for Genome Stability and Disease Prevention, Shenzhen University International Cancer Center, Department of Cell Biology and Genetics, Shenzhen University Health Science Center, Shenzhen, 518060, China.
Chengyao ChiangGuangdong Key Laboratory for Genome Stability and Disease Prevention, Shenzhen University International Cancer Center, Department of Cell Biology and Genetics, Shenzhen University Health Science Center, Shenzhen, 518060, China.
Genze ShaoDepartment of Cell Biology, School of Basic Medical Sciences, Peking University, Beijing, 100191, China.
Kaowen YanInstitute for Translational Medicine, Qingdao University, Qingdao, 266071, China.ORCID https://orcid.org/0000-0002-4234-5571
Shenzhen University Health Science Center · CNLonggang Central Hospital · CNPeking University · CNQingdao University · CN

Funding

China Postdoctoral Science Foundation 2017M612188National Natural Science Foundation of China 31701175Natural Science Foundation of Shandong Province ZR2017BC003Shenzhen Municipal Government of China JCYJ20160427105140594
6 · The paper itself

Abstract

Deubiquitinase BRISC complex plays important role in the maintenance of spindle structure and function; however, the underlying mechanism remains largely undefined. Here we demonstrated that MERIT40, a core component of BRISC complex, directly interacts with the RXXPEG motif in the ARC-V domain of Tankyrase1(TNKS1). Mutation of the RXXPEG motif in the MERIT40 (R28A) disrupted its interaction with TNKS1. Consistent with these data, R28A mutant cells displayed multiple mitotic defects including aberrant spindle assembly and chromosome misalignment. These results support a critical role of RXXPEG motif of MERIT40 in BRISC-mediated regulation of TNKS1 function during spindle assembly.

Indexed as

3' Untranslated RegionsAdaptor Proteins, Signal TransducingAmino Acid MotifsDeubiquitinating EnzymesHeLa CellsHumansMembrane ProteinsMutagenesis, Site-DirectedProtein BindingRNA InterferenceRNA, Small InterferingSequence AlignmentSpindle ApparatusTankyrases3' Untranslated RegionsAdaptor Proteins, Signal TransducingBABAM1 protein, humanBRCC3 protein, humanDeubiquitinating EnzymesMembrane ProteinsRNA, Small InterferingTankyrasesTNKS protein, humangenome stabilityMERIT40RXXPEG motifTNKS1

Identifiers

PMID30571846
PMCPMC13397392
OpenAlexW2906507625

What OpenQuestion holds

Textmetadata
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.