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Fibroblast growth factor receptor 2 phosphorylation on serine 779 couples to 14-3-3 and regulates cell survival and proliferation

Lonic, Ana, Barry, Emma F., Quach, Cindy, Kobe, Bostjan, Saunders, Neil and Guthridge, Mark A. 2008, Fibroblast growth factor receptor 2 phosphorylation on serine 779 couples to 14-3-3 and regulates cell survival and proliferation, Molecular and Cellular Biology, vol. 28, no. 10, pp. 3372-3385, doi: 10.1128/MCB.01837-07.

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Title Fibroblast growth factor receptor 2 phosphorylation on serine 779 couples to 14-3-3 and regulates cell survival and proliferation
Author(s) Lonic, Ana
Barry, Emma F.
Quach, Cindy
Kobe, Bostjan
Saunders, Neil
Guthridge, Mark A.ORCID iD for Guthridge, Mark A. orcid.org/0000-0002-0536-3471
Journal name Molecular and Cellular Biology
Volume number 28
Issue number 10
Start page 3372
End page 3385
Total pages 14
Publisher American Society for Microbiology
Place of publication Washington, D.C.
Publication date 2008-05-01
ISSN 0270-7306
1098-5549
Keyword(s) Science & Technology
Life Sciences & Biomedicine
Biochemistry & Molecular Biology
Cell Biology
GROWTH-FACTOR RECEPTOR
ELIMINATES PHOSPHATIDYLINOSITOL HYDROLYSIS
POINT MUTATION
STRUCTURAL BASIS
TYROSINE PHOSPHORYLATION
SIGNAL-TRANSDUCTION
PHOSPHOLIPASE-C
PC12 CELLS
SH2 DOMAIN
PROTEIN
Summary The fibroblast growth factors (FGFs) exert their diverse (or pleiotropic) biological responses through the binding and activation of specific cell surface receptors (FGFRs). While FGFRs are known to initiate intracellular signaling through receptor tyrosine phosphorylation, the precise mechanisms by which the FGFRs regulate pleiotropic biological responses remain unclear. We now identify a new mechanism by which FGFR2 is able to regulate intracellular signaling and cellular responses. We show that FGFR2 is phosphorylated on serine 779 (S779) in response to FGF2. S779, which lies adjacent to the phospholipase Cγ binding site at Y766, provides a docking site for the 14-3-3 phosphoserine-binding proteins and is essential for the full activation of the phosphatidylinositol 3-kinase and Ras/mitogen-activated protein kinase pathways. Furthermore, S779 signaling is essential for promoting cell survival and proliferation in both Ba/F3 cells and BALB/c 3T3 fibroblasts. This new mode of FGFR2 phosphoserine signaling via the 14-3-3 proteins may provide an increased repertoire of signaling outputs to allow the regulation of pleiotropic biological responses. In this regard, we have identified conserved putative phosphotyrosine/phosphoserine motifs in the cytoplasmic domains of diverse cell surface receptors, suggesting that they may perform important functional roles beyond the FGFRs.
Language eng
DOI 10.1128/MCB.01837-07
Indigenous content off
Field of Research 06 Biological Sciences
11 Medical and Health Sciences
HERDC Research category C1 Refereed article in a scholarly journal
Copyright notice ©200, American Society for Microbiology
Free to Read? Yes
Persistent URL http://hdl.handle.net/10536/DRO/DU:30132412

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Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.