Differential responses to kinase inhibition in FGFR2-addicted triple negative breast cancer cells: a quantitative phosphoproteomics study
Fibroblast Growth Factor (FGF) dependent signalling is frequently activated in cancer by a variety of different mechanisms. However, the downstream signal transduction pathways involved are poorly characterised. Here a quantitative differential phosphoproteomics approach, SILAC, is applied to identi...
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Published in | Scientific reports Vol. 10; no. 1; p. 7950 |
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Main Authors | , , , , , , , , , |
Format | Journal Article |
Language | English |
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14.05.2020
Nature Publishing Group UK |
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Abstract | Fibroblast Growth Factor (FGF) dependent signalling is frequently activated in cancer by a variety of different mechanisms. However, the downstream signal transduction pathways involved are poorly characterised. Here a quantitative differential phosphoproteomics approach, SILAC, is applied to identify FGF-regulated phosphorylation events in two triple- negative breast tumour cell lines, MFM223 and SUM52, that exhibit amplified expression of FGF receptor 2 (FGFR2) and are dependent on continued FGFR2 signalling for cell viability. Comparative Gene Ontology proteome analysis revealed that SUM52 cells were enriched in proteins associated with cell metabolism and MFM223 cells enriched in proteins associated with cell adhesion and migration. FGFR2 inhibition by SU5402 impacts a significant fraction of the observed phosphoproteome of these cells. This study expands the known landscape of FGF signalling and identifies many new targets for functional investigation. FGF signalling pathways are found to be flexible in architecture as both shared, and divergent, responses to inhibition of FGFR2 kinase activity in the canonical RAF/MAPK/ERK/RSK and PI3K/AKT/PDK/mTOR/S6K pathways are identified. Inhibition of phosphorylation-dependent negative-feedback pathways is observed, defining mechanisms of intrinsic resistance to FGFR2 inhibition. These findings have implications for the therapeutic application of FGFR inhibitors as they identify both common and divergent responses in cells harbouring the same genetic lesion and pathways of drug resistance. |
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AbstractList | Abstract
Fibroblast Growth Factor (FGF) dependent signalling is frequently activated in cancer by a variety of different mechanisms. However, the downstream signal transduction pathways involved are poorly characterised. Here a quantitative differential phosphoproteomics approach, SILAC, is applied to identify FGF-regulated phosphorylation events in two triple- negative breast tumour cell lines, MFM223 and SUM52, that exhibit amplified expression of FGF receptor 2 (FGFR2) and are dependent on continued FGFR2 signalling for cell viability. Comparative Gene Ontology proteome analysis revealed that SUM52 cells were enriched in proteins associated with cell metabolism and MFM223 cells enriched in proteins associated with cell adhesion and migration. FGFR2 inhibition by SU5402 impacts a significant fraction of the observed phosphoproteome of these cells. This study expands the known landscape of FGF signalling and identifies many new targets for functional investigation. FGF signalling pathways are found to be flexible in architecture as both shared, and divergent, responses to inhibition of FGFR2 kinase activity in the canonical RAF/MAPK/ERK/RSK and PI3K/AKT/PDK/mTOR/S6K pathways are identified. Inhibition of phosphorylation-dependent negative-feedback pathways is observed, defining mechanisms of intrinsic resistance to FGFR2 inhibition. These findings have implications for the therapeutic application of FGFR inhibitors as they identify both common and divergent responses in cells harbouring the same genetic lesion and pathways of drug resistance. Fibroblast Growth Factor (FGF) dependent signalling is frequently activated in cancer by a variety of different mechanisms. However, the downstream signal transduction pathways involved are poorly characterised. Here a quantitative differential phosphoproteomics approach, SILAC, is applied to identify FGF-regulated phosphorylation events in two triple- negative breast tumour cell lines, MFM223 and SUM52, that exhibit amplified expression of FGF receptor 2 (FGFR2) and are dependent on continued FGFR2 signalling for cell viability. Comparative Gene Ontology proteome analysis revealed that SUM52 cells were enriched in proteins associated with cell metabolism and MFM223 cells enriched in proteins associated with cell adhesion and migration. FGFR2 inhibition by SU5402 impacts a significant fraction of the observed phosphoproteome of these cells. This study expands the known landscape of FGF signalling and identifies many new targets for functional investigation. FGF signalling pathways are found to be flexible in architecture as both shared, and divergent, responses to inhibition of FGFR2 kinase activity in the canonical RAF/MAPK/ERK/RSK and PI3K/AKT/PDK/mTOR/S6K pathways are identified. Inhibition of phosphorylation-dependent negative-feedback pathways is observed, defining mechanisms of intrinsic resistance to FGFR2 inhibition. These findings have implications for the therapeutic application of FGFR inhibitors as they identify both common and divergent responses in cells harbouring the same genetic lesion and pathways of drug resistance.Fibroblast Growth Factor (FGF) dependent signalling is frequently activated in cancer by a variety of different mechanisms. However, the downstream signal transduction pathways involved are poorly characterised. Here a quantitative differential phosphoproteomics approach, SILAC, is applied to identify FGF-regulated phosphorylation events in two triple- negative breast tumour cell lines, MFM223 and SUM52, that exhibit amplified expression of FGF receptor 2 (FGFR2) and are dependent on continued FGFR2 signalling for cell viability. Comparative Gene Ontology proteome analysis revealed that SUM52 cells were enriched in proteins associated with cell metabolism and MFM223 cells enriched in proteins associated with cell adhesion and migration. FGFR2 inhibition by SU5402 impacts a significant fraction of the observed phosphoproteome of these cells. This study expands the known landscape of FGF signalling and identifies many new targets for functional investigation. FGF signalling pathways are found to be flexible in architecture as both shared, and divergent, responses to inhibition of FGFR2 kinase activity in the canonical RAF/MAPK/ERK/RSK and PI3K/AKT/PDK/mTOR/S6K pathways are identified. Inhibition of phosphorylation-dependent negative-feedback pathways is observed, defining mechanisms of intrinsic resistance to FGFR2 inhibition. These findings have implications for the therapeutic application of FGFR inhibitors as they identify both common and divergent responses in cells harbouring the same genetic lesion and pathways of drug resistance. Fibroblast Growth Factor (FGF) dependent signalling is frequently activated in cancer by a variety of different mechanisms. However, the downstream signal transduction pathways involved are poorly characterised. Here a quantitative differential phosphoproteomics approach, SILAC, is applied to identify FGF-regulated phosphorylation events in two triple- negative breast tumour cell lines, MFM223 and SUM52, that exhibit amplified expression of FGF receptor 2 (FGFR2) and are dependent on continued FGFR2 signalling for cell viability. Comparative Gene Ontology proteome analysis revealed that SUM52 cells were enriched in proteins associated with cell metabolism and MFM223 cells enriched in proteins associated with cell adhesion and migration. FGFR2 inhibition by SU5402 impacts a significant fraction of the observed phosphoproteome of these cells. This study expands the known landscape of FGF signalling and identifies many new targets for functional investigation. FGF signalling pathways are found to be flexible in architecture as both shared, and divergent, responses to inhibition of FGFR2 kinase activity in the canonical RAF/MAPK/ERK/RSK and PI3K/AKT/PDK/mTOR/S6K pathways are identified. Inhibition of phosphorylation-dependent negative-feedback pathways is observed, defining mechanisms of intrinsic resistance to FGFR2 inhibition. These findings have implications for the therapeutic application of FGFR inhibitors as they identify both common and divergent responses in cells harbouring the same genetic lesion and pathways of drug resistance. |
ArticleNumber | 7950 |
Author | Ferguson, Harriet R Brookes, Katie Creese, Andrew J Marusiak, Anna A Cooper, Helen J Heath, John K Sarhan, Adil R Zhao, Hongyan Larkins, Katherine P B Cunningham, Debbie L |
Author_xml | – sequence: 1 givenname: Debbie L surname: Cunningham fullname: Cunningham, Debbie L email: d.cunningham@bham.ac.uk organization: School of Biosciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK. d.cunningham@bham.ac.uk – sequence: 2 givenname: Adil R surname: Sarhan fullname: Sarhan, Adil R organization: Department of Medical Laboratory Techniques, Nasiriyah Technical Institute, Southern Technical University, Nasiriyah, 6400, Iraq – sequence: 3 givenname: Andrew J surname: Creese fullname: Creese, Andrew J organization: Immunocore, 101 Park Drive, Milton Park, Abingdon, Oxfordshire, OX14 4RY, UK – sequence: 4 givenname: Katherine P B surname: Larkins fullname: Larkins, Katherine P B organization: School of Biosciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK – sequence: 5 givenname: Hongyan surname: Zhao fullname: Zhao, Hongyan organization: School of Biosciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK – sequence: 6 givenname: Harriet R surname: Ferguson fullname: Ferguson, Harriet R organization: Division of Molecular and Cellular Function, School of Biological Science, Faculty of Biology Medicine and Health, The University of Manchester, Manchester, M13 9PT, UK – sequence: 7 givenname: Katie surname: Brookes fullname: Brookes, Katie organization: School of Biosciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK – sequence: 8 givenname: Anna A surname: Marusiak fullname: Marusiak, Anna A organization: Laboratory of Experimental Medicine, Centre of New Technologies, University of Warsaw, 02-097, Warszawa, Poland – sequence: 9 givenname: Helen J surname: Cooper fullname: Cooper, Helen J organization: School of Biosciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK – sequence: 10 givenname: John K surname: Heath fullname: Heath, John K email: J.K.Heath@bham.ac.uk organization: School of Biosciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK. J.K.Heath@bham.ac.uk |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/32409632$$D View this record in MEDLINE/PubMed |
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CitedBy_id | crossref_primary_10_1038_s41598_023_46586_y crossref_primary_10_1038_s41467_021_22101_7 crossref_primary_10_3390_ijms22042008 crossref_primary_10_1098_rsob_210373 crossref_primary_10_1007_s10552_022_01574_x crossref_primary_10_3390_biomedicines10030601 crossref_primary_10_1038_s41401_022_01017_y |
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Snippet | Fibroblast Growth Factor (FGF) dependent signalling is frequently activated in cancer by a variety of different mechanisms. However, the downstream signal... Abstract Fibroblast Growth Factor (FGF) dependent signalling is frequently activated in cancer by a variety of different mechanisms. However, the downstream... |
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SubjectTerms | 1-Phosphatidylinositol 3-kinase AKT protein Breast cancer Cell adhesion Cell adhesion & migration Cell Line, Tumor Cell migration Cell viability Drug resistance Extracellular signal-regulated kinase Fibroblast growth factor receptor 2 Fibroblast growth factor receptors Gene Ontology Humans Kinases MAP kinase Phosphoproteins - metabolism Phosphorylation Protein Kinase Inhibitors - pharmacology Proteomes Proteomics Raf protein Receptor, Fibroblast Growth Factor, Type 2 - antagonists & inhibitors Receptor, Fibroblast Growth Factor, Type 2 - metabolism Signal transduction TOR protein Triple Negative Breast Neoplasms - pathology Tumor cell lines Tumors |
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Title | Differential responses to kinase inhibition in FGFR2-addicted triple negative breast cancer cells: a quantitative phosphoproteomics study |
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