ArticleThe Journal of biological chemistry2013
Myotubularin-related protein 4 (MTMR4) attenuates BMP/Dpp signaling by dephosphorylation of Smad proteins.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- The Myotubularin Related Proteins and the Untapped Interaction Potential of Their Disordered C-Terminal Regions.Proteins · 2025Article
- Optimal performance objectives in the highly conserved bone morphogenetic protein signaling pathway.NPJ systems biology and applications · 2024Article
- Review
- Socioeconomic status and DNA methylation from birth through mid-childhood: a prospective study in Project Viva.Epigenomics · 2019Article
- Novel insight into the genetic basis of high-altitude pulmonary hypertension in Kyrgyz highlanders.European journal of human genetics : EJHG · 2019Article
- TGF-β Signaling from Receptors to Smads.Cold Spring Harbor perspectives in biology · 2016Review
- Drosophila Dullard functions as a Mad phosphatase to terminate BMP signaling.Scientific reports · 2016Article
- Novel loci affecting iron homeostasis and their effects in individuals at risk for hemochromatosis.Nature communications · 2014Article
- C-terminal domain (CTD) small phosphatase-like 2 modulates the canonical bone morphogenetic protein (BMP) signaling and mesenchymal differentiation via Smad dephosphorylation.The Journal of biological chemistry · 2014Article
- Crystallization and preliminary X-ray crystallographic analysis of the PH-GRAM domain of human MTMR4.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Specific control of BMP signaling and mesenchymal differentiation by cytoplasmic phosphatase PPM1H.Cell research · 2014Article
- TGF-β cascade regulation by PPP1 and its interactors -impact on prostate cancer development and therapy.Journal of cellular and molecular medicine · 2014Review
- The modulation of phosphatase expression impacts the proliferation efficiency of HSV-1 in infected astrocytes.PloS one · 2013Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bone morphogenetic proteins (BMPs) signaling essentially regulates a wide range of biological responses. Although multiple regulators at different layers of the receptor-effectors axis have been identified, the mechanisms of homeostatic BMP signaling remain vague. Herein we demonstrated that myotubularin-related protein 4 (MTMR4), a FYVE domain-containing dual-specificity protein phosphatase (DUSP), preferentially associated with and dephosphorylated the activated R-Smads in cytoplasm, which is a critical checkpoint in BMP signal transduction. Therefore, transcriptional activation by BMPs was tightly controlled by the expression level and the intrinsic phosphatase activity of MTMR4. More profoundly, ectopic expression of MTMR4 or its Drosophila homolog CG3632 genetically interacted with BMP/Dpp signaling axis in regulation of the vein development of Drosophila wings. By doing so, MTMR4 could interact with and dephosphorylate Mothers against Decapentaplegic (Mad), the sole R-Smad in Drosophila BMP pathway, and hence affected the target genes expression of Mad. In conclusion, this study has suggested that MTMR4 is a necessary negative modulator for the homeostasis of BMP/Dpp signaling.
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