Evidence map›Paper›PMID 34561473›Full record

ArticleScientific reports2021

PIGN spatiotemporally regulates the spindle assembly checkpoint proteins in leukemia transformation and progression.

Emmanuel K Teye, Shasha Lu, Fangyuan Chen, Wenrui Yang, Thomas Abraham, Douglas B Stairs, Hong-Gang Wang, Gregory S Yochum, Robert A Brodsky, Jeffrey J Pu

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Scientific reports, 2021. 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 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.6field-weighted citation impact, top 32% 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

7 citing papers in PubMed, 7 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 6 institutions in 2 countries.

Emmanuel K TeyePenn State Cancer Institute, Pennsylvania State University College of Medicine, Hershey, PA, USA.
Shasha LuPenn State Cancer Institute, Pennsylvania State University College of Medicine, Hershey, PA, USA.
Fangyuan ChenRenji Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Wenrui YangPenn State Cancer Institute, Pennsylvania State University College of Medicine, Hershey, PA, USA.
Thomas AbrahamPenn State Cancer Institute, Pennsylvania State University College of Medicine, Hershey, PA, USA.
Douglas B StairsPenn State Cancer Institute, Pennsylvania State University College of Medicine, Hershey, PA, USA.
Hong-Gang WangPenn State Cancer Institute, Pennsylvania State University College of Medicine, Hershey, PA, USA.
Gregory S YochumPenn State Cancer Institute, Pennsylvania State University College of Medicine, Hershey, PA, USA.
Robert A BrodskyDivision of Hematology, Johns Hopkins Medicine, Baltimore, MD, USA.
Jeffrey J PuPenn State Cancer Institute, Pennsylvania State University College of Medicine, Hershey, PA, USA. jeffreypu@gmail.com.
Pennsylvania State University · USJohns Hopkins University · USPeking Union Medical College Hospital · CNRenji Hospital · CNShanghai Jiao Tong University · CNUniversity of Arizona Cancer Center

Funding

Research Training and Educational Component (Component I) p370-385P50DA036107 · NIDA · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI FOULDS, JONATHAN, MUSCAT, JOSHUA E · 2013 to 2018
$19.5M
NIDA NIH HHS P50 DA036107
6 · The paper itself

Abstract

Phosphatidylinositol glycan anchor biosynthesis class N (PIGN) has been linked to the suppression of chromosomal instability. The spindle assembly checkpoint complex is responsible for proper chromosome segregation during mitosis to prevent chromosomal instability. In this study, the novel role of PIGN as a regulator of the spindle assembly checkpoint was unveiled in leukemic patient cells and cell lines. Transient downregulation or ablation of PIGN resulted in impaired mitotic checkpoint activation due to the dysregulated expression of spindle assembly checkpoint-related proteins including MAD1, MAD2, BUBR1, and MPS1. Moreover, ectopic overexpression of PIGN restored the expression of MAD2. PIGN regulated the spindle assembly checkpoint by forming a complex with the spindle assembly checkpoint proteins MAD1, MAD2, and the mitotic kinase MPS1. Thus, PIGN could play a vital role in the spindle assembly checkpoint to suppress chromosomal instability associated with leukemic transformation and progression.

Indexed as

Cell Cycle ProteinsCell LineCell Transformation, NeoplasticChromosomal InstabilityDisease ProgressionGene ExpressionHL-60 CellsHumansK562 CellsLeukemiaMad2 ProteinsPhosphotransferasesProtein Serine-Threonine KinasesProtein-Tyrosine KinasesSpindle ApparatusCell Cycle ProteinsMAD1L1 protein, humanMAD2L1 protein, humanMad2 ProteinsPhosphotransferasesPIGN protein, humanProtein Serine-Threonine KinasesProtein-Tyrosine KinasesTTK protein, human

Identifiers

PMID34561473
PMCPMC8463542
OpenAlexW3199243567

What Socratic holds

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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 Socratic graph.