Evidence map›Paper›PMID 30872372›Full record

ArticleHaematologica2019

Deubiquitylase USP7 regulates human terminal erythroid differentiation by stabilizing GATA1.

Long Liang, Yuanliang Peng, Jieying Zhang, Yibin Zhang, Mridul Roy, Xu Han, Xiaojuan Xiao, Shuming Sun, Hong Liu, Ling Nie and 10 more

Open access · goldAbstract read
In one paragraph

Article in Haematologica, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

30 citing papers in PubMed, 35 citations in OpenAlex.

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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

20 authors at 6 institutions in 2 countries.

Long LiangMolecular Biology Research Center & Center for Medical Genetics, School of Life Sciences, Central South University, Changsha, China.
Yuanliang PengMolecular Biology Research Center & Center for Medical Genetics, School of Life Sciences, Central South University, Changsha, China.
Jieying ZhangMolecular Biology Research Center & Center for Medical Genetics, School of Life Sciences, Central South University, Changsha, China.
Yibin ZhangMolecular Biology Research Center & Center for Medical Genetics, School of Life Sciences, Central South University, Changsha, China.
Mridul RoyMolecular Biology Research Center & Center for Medical Genetics, School of Life Sciences, Central South University, Changsha, China.
Xu HanMolecular Biology Research Center & Center for Medical Genetics, School of Life Sciences, Central South University, Changsha, China.
Xiaojuan XiaoMolecular Biology Research Center & Center for Medical Genetics, School of Life Sciences, Central South University, Changsha, China.
Shuming SunMolecular Biology Research Center & Center for Medical Genetics, School of Life Sciences, Central South University, Changsha, China.
Hong LiuXiangya Hospital, Central South University, Changsha, China.
Ling NieXiangya Hospital, Central South University, Changsha, China.
Yijin KuangMolecular Biology Research Center & Center for Medical Genetics, School of Life Sciences, Central South University, Changsha, China.
Zesen ZhuMolecular Biology Research Center & Center for Medical Genetics, School of Life Sciences, Central South University, Changsha, China.
Jinghui DengMolecular Biology Research Center & Center for Medical Genetics, School of Life Sciences, Central South University, Changsha, China.
Yang XiaDepartment of Biochemistry and Molecular Biology, The University of Texas Health Science Center at Houston, Houston, TX, USA.
Vijay G SankaranBroad Institute of MIT and Harvard, Cambridge, MA, USA.
Christopher D HillyerRed Cell Physiology Laboratory, New York Blood Center, New York, NY, USA.
Narla MohandasRed Cell Physiology Laboratory, New York Blood Center, New York, NY, USA.
Mao YeMolecular Science and Biomedicine Laboratory, State Key Laboratory for Chemo/Biosensing and Chemometrics, College of Biology, College of Chemistry and Chemical Engineering, Hunan University, Changsha, China goldleaf@hnu.edu.cn.
Xiuli AnLaboratory of Membrane Biology, New York Blood Center, New York, NY, USA xan@nybc.org.
Jing LiuMolecular Biology Research Center & Center for Medical Genetics, School of Life Sciences, Central South University, Changsha, China jingliucsu@hotmail.com liujing2@sklmg.edu.cn.
Central South University · CNNew York Blood Center · USXiangya Hospital Central South University · CNBroad Institute · USHunan University · CNThe University of Texas Health Science Center at Houston · US

Funding

YEAST MEMBRANE CYTOSKELETONP01DK032094 · NIDDK · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI NARLA, MOHANDAS · 1987 to 2021
$26.7M
TET3 in Terminal Erythroid DifferentiationR01DK100810 · NIDDK · NEW YORK BLOOD CENTER · PI AN, XIULI · 2014 to 2016
$875k
NIDDK NIH HHS P01 DK032094NIDDK NIH HHS R01 DK100810
6 · The paper itself

Abstract

Ubiquitination is an enzymatic post-translational modification that affects protein fate. The ubiquitin-proteasome system (UPS) was first discovered in reticulocytes where it plays important roles in reticulocyte maturation. Recent studies have revealed that ubiquitination is a dynamic and reversible process and that deubiquitylases are capable of removing ubiquitin from their protein substrates. Given the fact that the UPS is highly active in reticulocytes, it is speculated that deubiquitylases may play important roles in erythropoiesis. Yet, the role of deubiquitylases in erythropoiesis remains largely unexplored. In the present study, we found that the expression of deubiquitylase USP7 is significantly increased during human terminal erythroid differentiation. We further showed that interfering with USP7 function, either by short hairpin RNA-mediated knockdown or USP7-specific inhibitors, impaired human terminal erythroid differentiation due to decreased GATA1 level and that restoration of GATA1 levels rescued the differentiation defect. Mechanistically, USP7 deficiency led to a decreased GATA1 protein level that could be reversed by proteasome inhibitors. Furthermore, USP7 interacts directly with GATA1 and catalyzes the removal of K48-linked poly ubiquitylation chains conjugated onto GATA1, thereby stabilizing GATA1 protein. Collectively, our findings have identified an important role of a deubiquitylase in human terminal erythroid differentiation by stabilizing GATA1, the master regulator of erythropoiesis.

Indexed as

BiomarkersCell DifferentiationErythroid Precursor CellsErythropoiesisGATA1 Transcription FactorGene Expression Regulation, DevelopmentalHumansImmunophenotypingModels, BiologicalProtein BindingProtein StabilityUbiquitinationUbiquitin-Specific Peptidase 7BiomarkersGATA1 protein, humanGATA1 Transcription FactorUbiquitin-Specific Peptidase 7USP7 protein, human

Identifiers

PMID30872372
PMCPMC6821630
OpenAlexW2921107726

What OpenQuestion holds

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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.