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    Structural Basis for Activation of Fibroblast Growth Factor Signaling by Sucrose Octasulfate

    Author
    Yeh, Brian K.; Eliseenkova, Anna V.; Plotnikov, Alexander N.; Green, David; Pinnell, Jared; Polat, Tulay; Gritli-Linde, Amel; Linhardt, Robert J.; Mohammadi, Moosa
    ORCID
    https://orcid.org/0000-0003-2219-5833
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    Other Contributors
    Date Issued
    2002-10-01
    Subject
    Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
    Degree
    Terms of Use
    In Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/;
    Full Citation
    Structural Basis for Activation of Fibroblast Growth Factor Signaling by Sucrose Octasulfate, B.K. Yeh, A.V. Eliseenkova, A.N. Plotnikov, D. Green, J. Pinnell, T. Polat, A. Gritli-Linde, R.J. Linhardt, M. Mohammadi, Molecular and Cellular Biology, 22, 7184-7192, 2002.
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    URI
    https://doi.org/10.1128/MCB.22.20.7184-7192.2002; https://hdl.handle.net/20.500.13015/5827
    Abstract
    Sucrose octasulfate (SOS) is believed to stimulate fibroblast growth factor (FGF) signaling by binding and stabilizing FGFs. In this report, we show that SOS induces FGF-dependent dimerization of FGF receptors (FGFRs). The crystal structure of the dimeric FGF2-FGFR1-SOS complex at 2.6-Å resolution reveals a symmetric assemblage of two 1:1:1 FGF2-FGFR1-SOS ternary complexes. Within each ternary complex SOS binds to FGF and FGFR and thereby increases FGF-FGFR affinity. SOS also interacts with the adjoining FGFR and thereby promotes protein-protein interactions that stabilize dimerization. This structural finding is supported by the inability of selectively desulfated SOS molecules to promote receptor dimerization. Thus, we propose that SOS potentiates FGF signaling by imitating the dual role of heparin in increasing FGF-FGFR affinity and promoting receptor dimerization. Hence, the dimeric FGF-FGFR-SOS structure substantiates the recently proposed “two-end” model, by which heparin induces FGF-FGFR dimerization. Moreover, the FGF-FGFR-SOS structure provides an attractive template for the development of easily synthesized SOS-related heparin agonists and antagonists that may hold therapeutic potential.;
    Description
    Molecular and Cellular Biology, 22, 7184-7192; Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
    Department
    The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
    Relationships
    The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; Molecular and Cellular Biology; https://harc.rpi.edu/;
    Access
    https://login.libproxy.rpi.edu/login?url=https://doi.org/10.1128/MCB.22.20.7184-7192.2002;
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