Phosphorylation of threonine residues on Shc promotes ligand binding and mediates crosstalk between MAPK and Akt pathways in breast cancer cells
dc.contributor.author | Suen, K.M. | |
dc.contributor.author | Lin, C.C. | |
dc.contributor.author | Seiler, C. | |
dc.contributor.author | George, R. | |
dc.contributor.author | Poncet-Montange, G. | |
dc.contributor.author | Biter, A.B. | |
dc.contributor.author | Ahmed, Z. | |
dc.contributor.author | Arold, Stefan T. | |
dc.contributor.author | Ladbury, J.E. | |
dc.date.accessioned | 2017-12-14T12:34:04Z | |
dc.date.available | 2017-12-14T12:34:04Z | |
dc.date.issued | 2017-12-06 | |
dc.identifier.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. | |
dc.identifier.issn | 1357-2725 | |
dc.identifier.pmid | 29208567 | |
dc.identifier.doi | 10.1016/j.biocel.2017.11.014 | |
dc.identifier.uri | http://hdl.handle.net/10754/626378 | |
dc.description.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. | |
dc.description.sponsorship | We are grateful to Dr. David Hawke for his assistance in proteomics analysis. | |
dc.publisher | Elsevier BV | |
dc.relation.url | http://www.sciencedirect.com/science/article/pii/S1357272517303059 | |
dc.rights | NOTICE: this is the author’s version of a work that was accepted for publication in The International Journal of Biochemistry & Cell Biology. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in The International Journal of Biochemistry & Cell Biology, 5 December 2017. DOI: 10.1016/j.biocel.2017.11.014. © 2017. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/ | |
dc.subject | Signal transduction Serine threonine phosphorylation Erk Cancer | |
dc.title | Phosphorylation of threonine residues on Shc promotes ligand binding and mediates crosstalk between MAPK and Akt pathways in breast cancer cells | |
dc.type | Article | |
dc.contributor.department | Biological and Environmental Sciences and Engineering (BESE) Division | |
dc.contributor.department | Bioscience Program | |
dc.contributor.department | Computational Bioscience Research Center (CBRC) | |
dc.identifier.journal | The International Journal of Biochemistry & Cell Biology | |
dc.eprint.version | Post-print | |
dc.contributor.institution | Graduate School of Biological Sciences, The University of Texas MD Anderson Cancer Center, Unit 1954, 1515 Holcombe Blvd, Houston, TX 77030, USA | |
dc.contributor.institution | Department of Biochemistry and Molecular Biology, The University of Texas MD Anderson Cancer Center, Unit 1954, 1515 Holcombe Blvd, Houston, TX 77030, USA | |
dc.contributor.institution | School of Molecular and Cellular Biology, University of Leeds, LC Miall Building, Leeds, LS2 9JT, UK | |
dc.contributor.institution | Structural Biology STP, The Francis Crick Institute, Lincolns Inn Fields Laboratory, 44 Lincolns Inn Fields, Holborn, London, WC2A 3LY, UK | |
dc.contributor.institution | Orthogon Therapeutics, 960 Turnpike Street, Unit 10, Canton, MA 02021, USA | |
dc.contributor.institution | Sabin Vaccine Institute and Texas Children's Hospital Center for Vaccine Development, 1102 Bates Avenue, Houston, TX 77030, USA | |
kaust.person | Arold, Stefan T. | |
refterms.dateFOA | 2018-12-05T00:00:00Z | |
dc.date.published-online | 2017-12-06 | |
dc.date.published-print | 2018-01 |
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