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    Phosphorylation of threonine residues on Shc promotes ligand binding and mediates crosstalk between MAPK and Akt pathways in breast cancer cells

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    Type
    Article
    Authors
    Suen, K.M.
    Lin, C.C.
    Seiler, C.
    George, R.
    Poncet-Montange, G.
    Biter, A.B.
    Ahmed, Z.
    Arold, Stefan T. cc
    Ladbury, J.E.
    KAUST Department
    Biological and Environmental Sciences and Engineering (BESE) Division
    Bioscience Program
    Computational Bioscience Research Center (CBRC)
    Date
    2017-12-06
    Online Publication Date
    2017-12-06
    Print Publication Date
    2018-01
    Permanent link to this record
    http://hdl.handle.net/10754/626378
    
    Metadata
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    Abstract
    Scaffold proteins play important roles in regulating signalling network fidelity, the absence of which is often the basis for diseases such as cancer. In the present work, we show that the prototypical scaffold protein Shc is phosphorylated by the extracellular signal-regulated kinase, Erk. In addition, Shc threonine phosphorylation is specifically up-regulated in two selected triple-negative breast cancer (TNBC) cell lines. To explore how Erk-mediated threonine phosphorylation on Shc might play a role in the dysregulation of signalling events, we investigated how Shc affects pathways downstream of EGF receptor. Using an in vitro model and biophysical analysis, we show that Shc threonine phosphorylation is responsible for elevated Akt and Erk signalling, potentially through the recruitment of the 14-3-3 ζ and Pin-1 proteins.
    Citation
    Suen KM, Lin CC, Seiler C, George R, Poncet-Montange G, et al. (2017) Phosphorylation of threonine residues on Shc promotes ligand binding and mediates crosstalk between MAPK and Akt pathways in breast cancer cells. The International Journal of Biochemistry & Cell Biology. Available: http://dx.doi.org/10.1016/j.biocel.2017.11.014.
    Sponsors
    We are grateful to Dr. David Hawke for his assistance in proteomics analysis.
    Publisher
    Elsevier BV
    Journal
    The International Journal of Biochemistry & Cell Biology
    DOI
    10.1016/j.biocel.2017.11.014
    PubMed ID
    29208567
    Additional Links
    http://www.sciencedirect.com/science/article/pii/S1357272517303059
    ae974a485f413a2113503eed53cd6c53
    10.1016/j.biocel.2017.11.014
    Scopus Count
    Collections
    Articles; Biological and Environmental Science and Engineering (BESE) Division; Bioscience Program; Computational Bioscience Research Center (CBRC)

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