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    Tyrosine phosphorylation controls Runx2-mediated subnuclear targeting of YAP to repress transcription

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    Authors
    Zaidi, Sayyed K.
    Sullivan, Andrew J.
    Medina, Ricardo F.
    Ito, Yoshiaki
    Van Wijnen, Andre J.
    Stein, Janet L.
    Lian, Jane B.
    Stein, Gary S.
    UMass Chan Affiliations
    Graduate School of Biomedical Sciences
    Department of Cell Biology
    Document Type
    Journal Article
    Publication Date
    2004-02-07
    Keywords
    Amino Acid Motifs; Animals; Cell Line, Tumor; Cell Nucleus; Chromatin; Core Binding Factor Alpha 1 Subunit; DNA-Binding Proteins; Humans; Nuclear Proteins; Osteoblasts; Osteocalcin; Phosphorylation; Rats; Signal Transduction; Trans-Activators; Transcription Factor AP-2; Transcription Factors; Transcription, Genetic; Tyrosine; src-Family Kinases
    Life Sciences
    Medicine and Health Sciences
    
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    Link to Full Text
    http://dx.doi.org/10.1038/sj.emboj.7600073
    Abstract
    Src/Yes tyrosine kinase signaling contributes to the regulation of bone homeostasis and inhibits osteoblast activity. Here we show that the endogenous Yes-associated protein (YAP), a mediator of Src/Yes signaling, interacts with the native Runx2 protein, an osteoblast-related transcription factor, and suppresses Runx2 transcriptional activity in a dose-dependent manner. Runx2, through its PY motif, recruits YAP to subnuclear domains in situ and to the osteocalcin (OC) gene promoter in vivo. Inhibition of Src/Yes kinase blocks tyrosine phosphorylation of YAP and dissociates endogenous Runx2-YAP complexes. Consequently, recruitment of the YAP co-repressor to subnuclear domains is abrogated and expression of the endogenous OC gene is induced. Our results suggest that Src/Yes signals are integrated through organization of Runx2-YAP transcriptional complexes at subnuclear sites to attenuate skeletal gene expression.
    Source
    EMBO J. 2004 Feb 25;23(4):790-9. Epub 2004 Feb 12. Link to article on publisher's site
    DOI
    10.1038/sj.emboj.7600073
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/34061
    PubMed ID
    14765127
    Related Resources
    Link to Article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1038/sj.emboj.7600073
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    Morningside Graduate School of Biomedical Sciences Scholarly Publications

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