Evidence map›Paper›PMID 34169608›Full record

ArticleStem cells (Dayton, Ohio)2021

DUSP5 promotes osteogenic differentiation through SCP1/2-dependent phosphorylation of SMAD1.

Xuejiao Liu, Xuenan Liu, Yangge Du, Menglong Hu, Yueming Tian, Zheng Li, Longwei Lv, Xiao Zhang, Yunsong Liu, Yongsheng Zhou and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Stem cells (Dayton, Ohio), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

13 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. [Advances in oral and craniofacial bone regeneration modulated by stem cells and biomaterials].Beijing da xue xue bao. Yi xue ban = Journal of Peking University. Health sciences · 2026
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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

11 authors at 1 institution in 1 country.

Xuejiao LiuDepartment of Prosthodontics, School and Hospital of Stomatology, Peking University, Beijing, People's Republic of China.ORCID 0000-0002-2713-5779
Xuenan LiuDepartment of Prosthodontics, School and Hospital of Stomatology, Peking University, Beijing, People's Republic of China.
Yangge DuDepartment of Prosthodontics, School and Hospital of Stomatology, Peking University, Beijing, People's Republic of China.
Menglong HuDepartment of Prosthodontics, School and Hospital of Stomatology, Peking University, Beijing, People's Republic of China.
Yueming TianDepartment of Prosthodontics, School and Hospital of Stomatology, Peking University, Beijing, People's Republic of China.
Zheng LiDepartment of Prosthodontics, School and Hospital of Stomatology, Peking University, Beijing, People's Republic of China.ORCID 0000-0003-0215-4401
Longwei LvDepartment of Prosthodontics, School and Hospital of Stomatology, Peking University, Beijing, People's Republic of China.
Xiao ZhangDepartment of Prosthodontics, School and Hospital of Stomatology, Peking University, Beijing, People's Republic of China.
Yunsong LiuDepartment of Prosthodontics, School and Hospital of Stomatology, Peking University, Beijing, People's Republic of China.
Yongsheng ZhouDepartment of Prosthodontics, School and Hospital of Stomatology, Peking University, Beijing, People's Republic of China.
Ping ZhangDepartment of Prosthodontics, School and Hospital of Stomatology, Peking University, Beijing, People's Republic of China.
Peking University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dual-specificity phosphatases (DUSPs) are defined by their capability to dephosphorylate both phosphoserine/phosphothreonine (pSer/pThr) and phosphotyrosine (pTyr). DUSP5, a member of DUSPs superfamily, is located in the nucleus and plays crucially regulatory roles in the signaling pathway transduction. In our present study, we discover that DUSP5 significantly promotes osteogenic differentiation of mesenchymal stromal cells (MSCs) by activating SMAD1 signaling pathway. Mechanistically, DUSP5 physically interacts with the phosphatase domain of small C-terminal phosphatase 1/2 (SCP1/2, SMAD1 phosphatases) by the linker region. In addition, we further confirm that DUSP5 activates SMAD1 signaling through a SCP1/2-dependent manner. Specifically, DUSP5 attenuates the SCP1/2-SMAD1 interaction by competitively binding to SCP1/2, which is responsible for the SMAD1 dephosphorylation, and thus results in the activation of SMAD1 signaling. Importantly, DUSP5 expression in mouse bone marrow MSCs is significantly reduced in ovariectomized (OVX) mice in which osteogenesis is highly passive, and overexpression of Dusp5 via tail vein injection reverses the bone loss of OVX mice efficiently. Collectively, this work demonstrates that the linker region of DUSP5 maybe a novel chemically modifiable target for controlling MSCs fate choices and for osteoporosis treatment.

Indexed as

Dual-Specificity PhosphatasesOsteogenesisSmad1 ProteinAnimalsCarrier ProteinsCell DifferentiationMicePhosphoprotein PhosphatasesPhosphorylationSignal TransductionCarrier ProteinsDual-Specificity PhosphatasesDusp5 protein, mousePhosphoprotein PhosphatasesScp1 protein, mouseSmad1 ProteinSmad1 protein, mousesterol carrier proteinsDUSP5osteogenesisosteoporosisSCP1/2SMAD1 signaling

Identifiers

PMID34169608
PMCPMC8518947
OpenAlexW3175303020

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.