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Title:
Targeting promiscuous heterodimerization overcomes innate resistance to ERBB2 dimerization inhibitors in breast cancer | Breast Cancer Research
Description:
Background The oncogenic receptor tyrosine kinase (RTK) ERBB2 is known to dimerize with other EGFR family members, particularly ERBB3, through which it potently activates PI3K signalling. Antibody-mediated inhibition of this ERBB2/ERBB3/PI3K axis has been a cornerstone of treatment for ERBB2-amplified breast cancer patients for two decades. However, the lack of response and the rapid onset of relapse in many patients now question the assumption that the ERBB2/ERBB3 heterodimer is the sole relevant effector target of these therapies. Methods Through a systematic protein-protein interaction screen, we have identified and validated alternative RTKs that interact with ERBB2. Using quantitative readouts of signalling pathway activation and cell proliferation, we have examined their influence upon the mechanism of trastuzumab- and pertuzumab-mediated inhibition of cell growth in ERBB2-amplified breast cancer cell lines and a patient-derived xenograft model. Results We now demonstrate that inactivation of ERBB3/PI3K by these therapeutic antibodies is insufficient to inhibit the growth of ERBB2-amplified breast cancer cells. Instead, we show extensive promiscuity between ERBB2 and an array of RTKs from outside of the EGFR family. Paradoxically, pertuzumab also acts as an artificial ligand to promote ERBB2 activation and ERK signalling, through allosteric activation by a subset of these non-canonical RTKs. However, this unexpected activation mechanism also increases the sensitivity of the receptor network to the ERBB2 kinase inhibitor lapatinib, which in combination with pertuzumab, displays a synergistic effect in single-agent resistant cell lines and PDX models. Conclusions The interaction of ERBB2 with a number of non-canonical RTKs activates a compensatory signalling response following treatment with pertuzumab, although a counter-intuitive combination of ERBB2 antibody therapy and a kinase inhibitor can overcome this innate therapeutic resistance.
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Keywords {🔍}
erbb, pertuzumab, cell, pubmed, cancer, article, breast, trastuzumab, fig, google, scholar, lapatinib, cells, combination, activation, lines, performed, phosphorylation, cas, rtks, treatment, figure, additional, file, antibody, receptor, signalling, line, growth, egfr, interaction, western, blotting, kinase, noncanonical, analysis, family, erk, response, central, data, antibodies, heterodimers, rtk, patients, met, leica, akt, usa, observed,
Topics {✒️}
formalin-fixed paraffin-embedded sections her2-positive breast cancer lower erbb2-expressing mda-mb-361 receptor tyrosine kinases inhibiting ligand-independent hetero-dimerization max nobis bcl-2-expressing breast tumors her2-amplified breast cancer innate therapeutic resistance elgene lim & david erbb2/erbb3/pi3k signalling axis proximity-mediated ligation assays observed ligand-independent hetero-dimerization full-length venus control proximity-mediated ligation assay erbb2-amplified breast cancer innate resistance driven article download pdf patient-derived xenograft model hetero-interactions occur exclusively breast cancer research atypical kinase sgk269/peak1 erbb2-targeted therapies detecting protein-protein interactions ligand-dependent erbb2 signalling erbb2-directed therapy mature advanced breast cancer patient-derived xenograft models single-agent-resistant erbb2+ tumour female nod-scid-il2γr−/− de la haba-rodriguez human breast cancer amaya garcia munoz erbb2-targeting therapeutic antibodies erbb3/pi3k signalling axis elgene lim high erbb2-expressing lines v2-labelled rtk fusions heat-induced antigen retrieval shorter disease-free survival disease-free survival brought functional β-barrel structure high erbb2-expressing zr-75-30 pdest-v2 destination vectors erbb2-targeting monoclonal antibodies anti-erbb3 antibody seribantumab erbb2/erbb3/pi3k axis bimolecular fluorescent complementation inhibit ligand-independent dimerization breast cancer tissue
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headline:Targeting promiscuous heterodimerization overcomes innate resistance to ERBB2 dimerization inhibitors in breast cancer
description:The oncogenic receptor tyrosine kinase (RTK) ERBB2 is known to dimerize with other EGFR family members, particularly ERBB3, through which it potently activates PI3K signalling. Antibody-mediated inhibition of this ERBB2/ERBB3/PI3K axis has been a cornerstone of treatment for ERBB2-amplified breast cancer patients for two decades. However, the lack of response and the rapid onset of relapse in many patients now question the assumption that the ERBB2/ERBB3 heterodimer is the sole relevant effector target of these therapies. Through a systematic protein-protein interaction screen, we have identified and validated alternative RTKs that interact with ERBB2. Using quantitative readouts of signalling pathway activation and cell proliferation, we have examined their influence upon the mechanism of trastuzumab- and pertuzumab-mediated inhibition of cell growth in ERBB2-amplified breast cancer cell lines and a patient-derived xenograft model. We now demonstrate that inactivation of ERBB3/PI3K by these therapeutic antibodies is insufficient to inhibit the growth of ERBB2-amplified breast cancer cells. Instead, we show extensive promiscuity between ERBB2 and an array of RTKs from outside of the EGFR family. Paradoxically, pertuzumab also acts as an artificial ligand to promote ERBB2 activation and ERK signalling, through allosteric activation by a subset of these non-canonical RTKs. However, this unexpected activation mechanism also increases the sensitivity of the receptor network to the ERBB2 kinase inhibitor lapatinib, which in combination with pertuzumab, displays a synergistic effect in single-agent resistant cell lines and PDX models. The interaction of ERBB2 with a number of non-canonical RTKs activates a compensatory signalling response following treatment with pertuzumab, although a counter-intuitive combination of ERBB2 antibody therapy and a kinase inhibitor can overcome this innate therapeutic resistance.
datePublished:2019-03-21T00:00:00Z
dateModified:2019-03-21T00:00:00Z
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ERBB2
Pertuzumab
Receptor tyrosine kinases
Breast cancer
Heterodimers
Cancer Research
Oncology
Surgical Oncology
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headline:Targeting promiscuous heterodimerization overcomes innate resistance to ERBB2 dimerization inhibitors in breast cancer
description:The oncogenic receptor tyrosine kinase (RTK) ERBB2 is known to dimerize with other EGFR family members, particularly ERBB3, through which it potently activates PI3K signalling. Antibody-mediated inhibition of this ERBB2/ERBB3/PI3K axis has been a cornerstone of treatment for ERBB2-amplified breast cancer patients for two decades. However, the lack of response and the rapid onset of relapse in many patients now question the assumption that the ERBB2/ERBB3 heterodimer is the sole relevant effector target of these therapies. Through a systematic protein-protein interaction screen, we have identified and validated alternative RTKs that interact with ERBB2. Using quantitative readouts of signalling pathway activation and cell proliferation, we have examined their influence upon the mechanism of trastuzumab- and pertuzumab-mediated inhibition of cell growth in ERBB2-amplified breast cancer cell lines and a patient-derived xenograft model. We now demonstrate that inactivation of ERBB3/PI3K by these therapeutic antibodies is insufficient to inhibit the growth of ERBB2-amplified breast cancer cells. Instead, we show extensive promiscuity between ERBB2 and an array of RTKs from outside of the EGFR family. Paradoxically, pertuzumab also acts as an artificial ligand to promote ERBB2 activation and ERK signalling, through allosteric activation by a subset of these non-canonical RTKs. However, this unexpected activation mechanism also increases the sensitivity of the receptor network to the ERBB2 kinase inhibitor lapatinib, which in combination with pertuzumab, displays a synergistic effect in single-agent resistant cell lines and PDX models. The interaction of ERBB2 with a number of non-canonical RTKs activates a compensatory signalling response following treatment with pertuzumab, although a counter-intuitive combination of ERBB2 antibody therapy and a kinase inhibitor can overcome this innate therapeutic resistance.
datePublished:2019-03-21T00:00:00Z
dateModified:2019-03-21T00:00:00Z
pageStart:1
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license:http://creativecommons.org/publicdomain/zero/1.0/
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ERBB2
Pertuzumab
Receptor tyrosine kinases
Breast cancer
Heterodimers
Cancer Research
Oncology
Surgical Oncology
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