Evidence map›Paper›PMID 16751101›Full record

ArticleCell2006

PPM1A functions as a Smad phosphatase to terminate TGFbeta signaling.

Xia Lin, Xueyan Duan, Yao-Yun Liang, Ying Su, Katharine H Wrighton, Jianyin Long, Min Hu, Candi M Davis, Jinrong Wang, F Charles Brunicardi and 4 more

RetractedOpen access · bronzeAbstract read
In one paragraph

Article in Cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 248 papers.

0numbers the graph read from it
0cells of the map it votes in
248citing papers in PubMed
16.4field-weighted citation impact, top 1% 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

248 citing papers in PubMed, 479 citations in OpenAlex.

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  19. Review
  20. TGF-β signaling in health, disease, and therapeutics.Signal transduction and targeted therapy · 2024
    Review

188 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors at 4 institutions in 2 countries.

Xia LinMichael E. DeBakey Department of Surgery, Baylor College of Medicine, Houston, TX 77030, USA. xialin@bcm.edu
Xueyan Duan
Yao-Yun Liang
Ying Su
Katharine H Wrighton
Jianyin Long
Min Hu
Candi M Davis
Jinrong Wang
F Charles Brunicardi
Yigong Shi
Ye-Guang Chen
Anming Meng
Xin-Hua Feng
Baylor College of Medicine · USTsinghua University · CNPrinceton University · USMichael E. DeBakey VA Medical Center · US

Funding

Regulation of TGF-beta Receptor Signaling by HSP90R01GM063773 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI FENG, XIN-HUA · 2001 to 2010
$2.3M
STRUCTURAL STUDIES OF SMAD PROTEINS IN TGF BETA SIGNALINR01CA082171 · NCI · PRINCETON UNIVERSITY · PI SHI, YIGONG · 1999 to 2008
$2.1M
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
NCI NIH HHS R01 CA082171NCI NIH HHS R01 CA108454NCI NIH HHS R01CA108454NCI NIH HHS R01CA82171NCI NIH HHS R21CA11293NIAMS NIH HHS R01 AR053591NIDDK NIH HHS R01 DK073932NIDDK NIH HHS R01DK073932NIGMS NIH HHS R01 GM063773NIGMS NIH HHS R01GM63773
6 · The paper itself

Abstract

TGFbeta signaling controls diverse normal developmental processes and pathogenesis of diseases including cancer and autoimmune and fibrotic diseases. TGFbeta responses are generally mediated through transcriptional functions of Smads. A key step in TGFbeta signaling is ligand-induced phosphorylation of receptor-activated Smads (R-Smads) catalyzed by the TGFbeta type I receptor kinase. However, the potential of Smad dephosphorylation as a regulatory mechanism of TGFbeta signaling and the identity of Smad-specific phosphatases remain elusive. Using a functional genomic approach, we have identified PPM1A/PP2Calpha as a bona fide Smad phosphatase. PPM1A dephosphorylates and promotes nuclear export of TGFbeta-activated Smad2/3. Ectopic expression of PPM1A abolishes TGFbeta-induced antiproliferative and transcriptional responses, whereas depletion of PPM1A enhances TGFbeta signaling in mammalian cells. Smad-antagonizing activity of PPM1A is also observed during Nodal-dependent early embryogenesis in zebrafish. This work demonstrates that PPM1A/PP2Calpha, through dephosphorylation of Smad2/3, plays a critical role in terminating TGFbeta signaling.

Indexed as

Active Transport, Cell NucleusActivin Receptors, Type IAnimalsCell LineCell Line, TumorEmbryo, NonmammalianHumansPhosphoprotein PhosphatasesPhosphorylationProtein Phosphatase 2CProtein Serine-Threonine KinasesReceptors, Transforming Growth Factor betaReceptor, Transforming Growth Factor-beta Type ISignal TransductionSmad2 ProteinSmad3 ProteinActivin Receptors, Type IPhosphoprotein PhosphatasesPPM1A protein, humanProtein Phosphatase 2CProtein Serine-Threonine KinasesReceptors, Transforming Growth Factor betaReceptor, Transforming Growth Factor-beta Type ISmad2 ProteinSMAD2 protein, humanSmad3 ProteinSMAD3 protein, humanTransforming Growth Factor beta

Identifiers

PMID16751101
PMCPMC6309366
OpenAlexW2034779933

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.