Combinatorial inhibition of PTPN12-regulated receptors leads to a broadly effective therapeutic strategy in triple-negative breast cancer

  • 1.

    Anders, C. Carey, L.A. Understanding and treating triple-negative breast cancer. Oncology (Williston Park) 22, 1233–1239; discussion 1239–1240, 1243 (2008).

  • 2.

    Anders, C.K., Zagar, T.M. Carey, L.A. The management of early-stage and metastatic triple-negative breast cancer: a review. Hematol. Oncol. Clin. North. Am. 27, 737–749 viii (2013).

  • 3.

    Bianchini, G., Balko, J.M., Mayer, I.A., Sanders, M.E. Gianni, L. Triple-negative breast cancer: challenges and opportunities of a heterogeneous disease. Nat. Rev. Clin. Oncol. 13, 674–690 (2016).

  • 4.

    Lehmann, B.D. et al. Identification of human triple-negative breast cancer subtypes and preclinical models for selection of targeted therapies. J. Clin. Invest. 121, 2750–2767 (2011).

  • 5.

    Hochgräfe, F. et al. Tyrosine phosphorylation profiling reveals the signaling network characteristics of Basal breast cancer cells. Cancer Res. 70, 9391–9401 (2010).

  • 6.

    Duncan, J.S. et al. Dynamic reprogramming of the kinome in response to targeted MEK inhibition in triple-negative breast cancer. Cell 149, 307–321 (2012).

  • 7.

    Nielsen, T.O. et al. Immunohistochemical and clinical characterization of the basal-like subtype of invasive breast carcinoma. Clin Cancer Res. 10, 5367–5374 (2004).

  • 8.

    Mertins, P. et al. Proteogenomics connects somatic mutations to signalling in breast cancer. Nature 534, 55–62 (2016).

  • 9.

    Sun, T. et al. Activation of multiple proto-oncogenic tyrosine kinases in breast cancer via loss of the PTPN12 phosphatase. Cell 144, 703–718 (2011).

  • 10.

    Wu, M.Q. et al. Low expression of tyrosine-protein phosphatase nonreceptor type 12 is associated with lymph node metastasis and poor prognosis in operable triple-negative breast cancer. Asian Pac. J. Cancer Prev. 14, 287–292 (2013).

  • 11.

    Villa-Moruzzi, E. PTPN12 controls PTEN and the AKT signalling to FAK and HER2 in migrating ovarian cancer cells. Mol. Cell. Biochem. 375, 151–157 (2013).

  • 12.

    Zheng, Y. et al. Temporal regulation of EGF signalling networks by the scaffold protein Shc1. Nature 499, 166–171 (2013).

  • 13.

    Charest, A., Wagner, J., Kwan, M. Tremblay, M.L. Coupling of the murine protein tyrosine phosphatase PEST to the epidermal growth factor (EGF) receptor through a Src homology 3 (SH3) domain-mediated association with Grb2. Oncogene 14, 1643–1651 (1997).

  • 14.

    Markova, B., Herrlich, P., Rönnstrand, L. Böhmer, F.D. Identification of protein tyrosine phosphatases associating with the PDGF receptor. Biochemistry 42, 2691–2699 (2003).

  • 15.

    Ambjørn, M. et al. A loss-of-function screen for phosphatases that regulate neurite outgrowth identifies PTPN12 as a negative regulator of TrkB tyrosine phosphorylation. PLoS One 8, e65371 (2013).

  • 16.

    Li, H. et al. Crystal structure and substrate specificity of PTPN12. Cell Rep. 15, 1345–1358 (2016).

  • 17.

    Barr, A.J. et al. Large-scale structural analysis of the classical human protein tyrosine phosphatome. Cell 136, 352–363 (2009).

  • 18.

    Li, J. et al. Loss of PTPN12 stimulates progression of ErbB2-dependent breast cancer by enhancing cell survival, migration, and epithelial-to-mesenchymal transition. Mol. Cell. Biol. 35, 4069–4082 (2015).

  • 19.

    Yao, Z. et al. A global analysis of the receptor tyrosine kinase-protein phosphatase interactome. Mol. Cell 65, 347–360 (2017).

  • 20.

    Hoadley, K.A. et al. EGFR associated expression profiles vary with breast tumor subtype. BMC Genomics 8, 258 (2007).

  • 21.

    Prat, A. et al. Molecular characterization of basal-like and non-basal-like triple-negative breast cancer. Oncologist 18, 123–133 (2013).

  • 22.

    Zagouri, F. et al. High MET expression is an adverse prognostic factor in patients with triple-negative breast cancer. Br. J. Cancer 108, 1100–1105 (2013).

  • 23.

    Cancer Genome Atlas, N.. Cancer Genome Atlas Network. Comprehensive molecular portraits of human breast tumours. Nature 490, 61–70 (2012).

  • 24.

    Forbes, S.A. et al. The catalogue of somatic mutations in cancer (COSMIC). Curr. Protoc. Hum. Genet. Chapter 10, Unit 10 11 (2008).

  • 25.

    Katsonis, P. Lichtarge, O. A formal perturbation equation between genotype and phenotype determines the evolutionary action of protein-coding variations on fitness. Genome Res. 24, 2050–2058 (2014).

  • 26.

    Carey, L.A. et al. TBCRC 001: randomized phase II study of cetuximab in combination with carboplatin in stage IV triple-negative breast cancer. J. Clin. Oncol. 30, 2615–2623 (2012).

  • 27.

    Miller, K. et al. Paclitaxel plus bevacizumab versus paclitaxel alone for metastatic breast cancer. N. Engl. J. Med. 357, 2666–2676 (2007).

  • 28.

    Yardley, D.A. et al. Phase I/II trial of neoadjuvant sunitinib administered with weekly paclitaxel/carboplatin in patients with locally advanced triple-negative breast cancer. Breast Cancer Res. Treat. 152, 557–567 (2015).

  • 29.

    Bianchi, G. et al. Phase II multicenter, uncontrolled trial of sorafenib in patients with metastatic breast cancer. Anticancer Drugs 20, 616–624 (2009).

  • 30.

    Finn, R.S. et al. Estrogen receptor, progesterone receptor, human epidermal growth factor receptor 2 (HER2), and epidermal growth factor receptor expression and benefit from lapatinib in a randomized trial of paclitaxel with lapatinib or placebo as first-line treatment in HER2-negative or unknown metastatic breast cancer. J. Clin. Oncol. 27, 3908–3915 (2009).

  • 31.

    Prenen, H. et al. Efficacy of the kinase inhibitor SU11248 against gastrointestinal stromal tumor mutants refractory to imatinib mesylate. Clin. Cancer Res. 12, 2622–2627 (2006).

  • 32.

    Guida, T. et al. Sorafenib inhibits imatinib-resistant KIT and platelet-derived growth factor receptor beta gatekeeper mutants. Clin. Cancer Res. 13, 3363–3369 (2007).

  • 33.

    Qi, J. et al. Multiple mutations and bypass mechanisms can contribute to development of acquired resistance to MET inhibitors. Cancer Res. 71, 1081–1091 (2011).

  • 34.

    Sørlie, T. et al. Gene expression patterns of breast carcinomas distinguish tumor subclasses with clinical implications. Proc. Natl. Acad. Sci. USA 98, 10869–10874 (2001).

  • 35.

    Zhang, X. et al. A renewable tissue resource of phenotypically stable, biologically and ethnically diverse, patient-derived human breast cancer xenograft models. Cancer Res. 73, 4885–4897 (2013).

  • 36.

    Xunyi, Y. et al. Clinicopathological significance of PTPN12 expression in human breast cancer. Braz. J. Med. Biol. Res. 45, 1334–1340 (2012).

  • 37.

    Wu, P., Nielsen, T.E. Clausen, M.H. Small-molecule kinase inhibitors: an analysis of FDA-approved drugs. Drug Discov. Today 21, 5–10 (2016).

  • 38.

    Su, Z. et al. PTPN12 inhibits oral squamous epithelial carcinoma cell proliferation and invasion and can be used as a prognostic marker. Med. Oncol. 30, 618 (2013).

  • 39.

    Cao, X. et al. Tyrosine-protein phosphatase non-receptor type 12 expression is a good prognostic factor in resectable non-small cell lung cancer. Oncotarget 6, 11704–11713 (2015).

  • 40.

    Cao, X. et al. Tyrosine-protein phosphatase nonreceptor type 12 is a novel prognostic biomarker for esophageal squamous cell carcinoma. Ann. Thorac. Surg. 93, 1674–1680 (2012).

  • 41.

    Luo, R.Z. et al. Decreased expression of PTPN12 correlates with tumor recurrence and poor survival of patients with hepatocellular carcinoma. PLoS One 9, e85592 (2014).

  • 42.

    Zhang, X.K. et al. The prognostic significance of tyrosine-protein phosphatase nonreceptor type 12 expression in nasopharyngeal carcinoma. Tumour Biol. 36, 5201–5208 (2015).

  • 43.

    Meerbrey, K.L. et al. The pINDUCER lentiviral toolkit for inducible RNA interference in vitro and in vivo. Proc. Natl. Acad. Sci. USA 108, 3665–3670 (2011).

  • 44.

    Lichtarge, O., Bourne, H.R. Cohen, F.E. An evolutionary trace method defines binding surfaces common to protein families. J. Mol. Biol. 257, 342–358 (1996).

  • 45.

    Mihalek, I., Res, I. Lichtarge, O. A family of evolution-entropy hybrid methods for ranking protein residues by importance. J. Mol. Biol. 336, 1265–1282 (2004).

  • 46.

    Edgar, R.C. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 32, 1792–1797 (2004).

  • 47.

    Mihalek, I., Res, I., Yao, H. Lichtarge, O. Combining inference from evolution and geometric probability in protein structure evaluation. J. Mol. Biol. 331, 263–279 (2003).

  • 48.

    Baameur, F. et al. Role for the regulator of G-protein signaling homology domain of G protein-coupled receptor kinases 5 and 6 in beta 2-adrenergic receptor and rhodopsin phosphorylation. Mol. Pharmacol. 77, 405–415 (2010).

  • 49.

    Lichtarge, O., Yamamoto, K.R. Cohen, F.E. Identification of functional surfaces of the zinc binding domains of intracellular receptors. J. Mol. Biol. 274, 325–337 (1997).

  • 50.

    Ribes-Zamora, A., Mihalek, I., Lichtarge, O. Bertuch, A.A. Distinct faces of the Ku heterodimer mediate DNA repair and telomeric functions. Nat. Struct. Mol. Biol. 14, 301–307 (2007).

  • 51.

    Lua, R.C. Lichtarge, O. PyETV: a PyMOL evolutionary trace viewer to analyze functional site predictions in protein complexes. Bioinformatics 26, 2981–2982 (2010).

  • 52.

    Söderberg, O. et al. Direct observation of individual endogenous protein complexes in situ by proximity ligation. Nat. Methods 3, 995–1000 (2006).

  • Leave a Reply

    Your email address will not be published. Required fields are marked *