Evidence map›Paper›PMID 25100727›Full record

ArticleThe Journal of biological chemistry2014

C-terminal domain (CTD) small phosphatase-like 2 modulates the canonical bone morphogenetic protein (BMP) signaling and mesenchymal differentiation via Smad dephosphorylation.

Yulan Zhao, Mu Xiao, Baoguo Sun, Zhengmao Zhang, Tao Shen, Xueyan Duan, Paul Borchyung Yu, Xin-Hua Feng, Xia Lin

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

31 citing papers in PubMed, 39 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

9 authors at 3 institutions in 2 countries.

Yulan ZhaoLife Sciences Institute, and Innovation Center for Cell Biology, Zhejiang University, Hangzhou, Zhejiang 310058, China.
Mu XiaoLife Sciences Institute, and Innovation Center for Cell Biology, Zhejiang University, Hangzhou, Zhejiang 310058, China.
Baoguo SunMichael E. DeBakey Department of Surgery, Baylor College of Medicine, Houston, Texas 77030; Department of Molecular Physiology and Biophysics, and Baylor College of Medicine, Houston, Texas 77030.
Zhengmao ZhangMichael E. DeBakey Department of Surgery, Baylor College of Medicine, Houston, Texas 77030.
Tao ShenMichael E. DeBakey Department of Surgery, Baylor College of Medicine, Houston, Texas 77030; Institute of Biosciences and Technology, Texas A&M Health Science Center, Houston, Texas 77030, and.
Xueyan DuanDepartment of Molecular and Cellular Biology, Baylor College of Medicine, Houston, Texas 77030.
Paul Borchyung YuCardiovascular Research Center, Massachusetts General Hospital, Boston, Massachusetts 02114.
Xin-Hua FengLife Sciences Institute, and Innovation Center for Cell Biology, Zhejiang University, Hangzhou, Zhejiang 310058, China,; Michael E. DeBakey Department of Surgery, Baylor College of Medicine, Houston, Texas 77030; Department of Molecular Physiology and Biophysics, and Baylor College of Medicine, Houston, Texas 77030; Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, Texas 77030,. Electronic address: xhfeng@zju.edu.cn.
Xia LinMichael E. DeBakey Department of Surgery, Baylor College of Medicine, Houston, Texas 77030. Electronic address: xialin@bcm.edu.
Baylor College of Medicine · USZhejiang University · CNMassachusetts General Hospital · US

Funding

Novel probes of BMP and TGF-beta signaling and functionR01AR057374 · NIAMS · MASSACHUSETTS GENERAL HOSPITAL · PI YU, PAUL B · 2010 to 2023
$4.5M
Regulation of TGF-beta Receptor Signaling by HSP90R01GM063773 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI FENG, XIN-HUA · 2001 to 2010
$2.3M
Tumor Suppressor Function of Smad4 by UbiquitinR01CA108454 · NCI · BAYLOR COLLEGE OF MEDICINE · PI FENG, XIN-HUA · 2004 to 2010
$1.8M
Roles of Smad1 Dephosphorylation in Osteoblast DifferentiationR01AR053591 · NIAMS · BAYLOR COLLEGE OF MEDICINE · PI FENG, XIN-HUA · 2008 to 2012
$1.5M
Regulation of SMAD2 Signaling by SMP1 PhosphataseR01DK073932 · NIDDK · BAYLOR COLLEGE OF MEDICINE · PI LIN, XIA · 2005 to 2008
$1.1M
The role of the BMP type II receptor in vascular functionK08HL079943 · NHLBI · MASSACHUSETTS GENERAL HOSPITAL · PI YU, PAUL B · 2006 to 2010
$672k
NCI NIH HHS R01 CA108454NCI NIH HHS R01CA108454NHLBI NIH HHS K08 HL079943NIAMS NIH HHS R01 AR053591NIAMS NIH HHS R01AR053591NIAMS NIH HHS R01 AR057374NIDDK NIH HHS R01 DK073932NIDDK NIH HHS R01DK073932NIGMS NIH HHS R01 GM063773NIGMS NIH HHS R01GM63773
6 · The paper itself

Abstract

The bone morphogenetic protein (BMP) signaling pathway regulates a wide range of cellular responses in metazoans. A key step in the canonical BMP signaling is the phosphorylation and activation of transcription factors Smad1, Smad5, and Smad8 (collectively Smad1/5/8) by the type I BMP receptors. We previously identified PPM1A as a phosphatase toward dephosphorylation of all receptor-regulated Smads (R-Smads), including Smad1/5/8. Here we report another nuclear phosphatase named SCP4/CTDSPL2, belonging to the FCP/SCP family, as a novel Smad phosphatase in the nucleus. SCP4 physically interacts with and specifically dephosphorylates Smad1/5/8, and as a result attenuates BMP-induced transcriptional responses. Knockdown of SCP4 in multipotent mesenchymal C2C12 cells leads to increased expression of BMP target genes and consequently promotes BMP-induced osteogenic differentiation. Collectively, our results demonstrate that SCP4, as a Smad phosphatase, plays a critical role in BMP-induced signaling and cellular functions.

Indexed as

Cell DifferentiationProtein Processing, Post-TranslationalAmino Acid MotifsAnimalsBone Morphogenetic ProteinsCatalytic DomainCell LineGene ExpressionHumansInhibitor of Differentiation Protein 1MesodermMiceOsteoblastsPhosphoprotein PhosphatasesPhosphorylationProtein BindingBone Morphogenetic ProteinsCTDSPL2 protein, mouseIdb1 protein, mouseInhibitor of Differentiation Protein 1Phosphoprotein PhosphatasesRNA Polymerase IISmad1 ProteinSmad1 protein, mouseBone Morphogenetic Protein (BMP)OsteoblastPhosphatasePhosphorylationSMAD Transcription FactorTransforming Growth Factor Beta (TGF-β)

Identifiers

PMID25100727
PMCPMC4176200
OpenAlexW2029440397

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.