ArticleThe Journal of cell biology2006
SHP-2 activates signaling of the nuclear factor of activated T cells to promote skeletal muscle growth.
Article in The Journal of cell biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
What it found
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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.
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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.
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Who cites it
33 citing papers in PubMed, 52 citations in OpenAlex.
- Synergistic effects of deleting the tyrosine phosphatases Shp1 and Shp2 on megakaryopoiesis and thrombopoiesis in mice.bioRxiv : the preprint server for biology · 2025Article
- SHP2 promotes sarcoidosis severity by inhibiting SKP2-targeted ubiquitination of TBET in CD8Science translational medicine · 2023Article
- From Stem to Sternum: The Role of Shp2 in the Skeleton.Calcified tissue international · 2023Review
- Case report: Clinical manifestations and genotype analysis of a child withFrontiers in pediatrics · 2022Article
- Endogenous miR-204 Protects the Kidney against Chronic Injury in Hypertension and Diabetes.Journal of the American Society of Nephrology : JASN · 2020Article
- Connecting the dots between SHP2 and glutamate receptors.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2020Review
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- A ERK/RSK-mediated negative feedback loop regulates M-CSF-evoked PI3K/AKT activation in macrophages.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018Article
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- Regulation of cell-cell fusion by nanotopography.Scientific reports · 2016Article
- Shp2 Associates with and Enhances Nephrin Tyrosine Phosphorylation and Is Necessary for Foot Process Spreading in Mouse Models of Podocyte Injury.Molecular and cellular biology · 2016Article
- Shp2 in forebrain neurons regulates synaptic plasticity, locomotion, and memory formation in mice.Molecular and cellular biology · 2015Article
- SHP2 regulates osteoclastogenesis by promoting preosteoclast fusion.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015Article
- The role of the protein tyrosine phosphatase SHP2 in cardiac development and disease.Seminars in cell & developmental biology · 2015Review
- PZR coordinates Shp2 Noonan and LEOPARD syndrome signaling in zebrafish and mice.Molecular and cellular biology · 2014Article
- Role of the protein tyrosine phosphatase Shp2 in homeostasis of the intestinal epithelium.PloS one · 2014Article
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- Novel role for SHP-2 in nutrient-responsive control of S6 kinase 1 signaling.Molecular and cellular biology · 2013Article
- Protein tyrosine phosphatase-like A regulates myoblast proliferation and differentiation through MyoG and the cell cycling signaling pathway.Molecular and cellular biology · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
The formation of multinucleated myofibers is essential for the growth of skeletal muscle. The nuclear factor of activated T cells (NFAT) promotes skeletal muscle growth. How NFAT responds to changes in extracellular cues to regulate skeletal muscle growth remains to be fully defined. In this study, we demonstrate that mice containing a skeletal muscle-specific deletion of the tyrosine phosphatase SHP-2 (muscle creatine kinase [MCK]-SHP-2 null) exhibited a reduction in both myofiber size and type I slow myofiber number. We found that interleukin-4, an NFAT-regulated cytokine known to stimulate myofiber growth, was reduced in its expression in skeletal muscles of MCK-SHP-2-null mice. When SHP-2 was deleted during the differentiation of primary myoblasts, NFAT transcriptional activity and myotube multinucleation were impaired. Finally, SHP-2 coupled myotube multinucleation to an integrin-dependent pathway and activated NFAT by stimulating c-Src. Thus, SHP-2 transduces extracellular matrix stimuli to intracellular signaling pathways to promote skeletal muscle growth.
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Registered trials
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.