N. Gaborit, M. Lindzen, and Y. Yarden, Emerging anti-cancer antibodies and combination therapies targeting HER3/ ErbB3, Hum Vaccin Immunother, vol.12, pp.576-593, 2016.

H. Friess, Y. Yamanaka, M. S. Kobrin, D. A. Do, M. W. Buchler et al., Enhanced erbB-3 expression in human pancreatic cancer correlates with tumor progression, Clin Cancer Res, vol.1, pp.1413-1420, 1995.

M. Hayashi, M. Inokuchi, Y. Takagi, H. Yamada, K. Kojima et al., High expression of HER3 is associated with a decreased survival in gastric cancer, Clin Cancer Res, vol.14, pp.7843-7849, 2008.

R. Naidu, M. Yadav, S. Nair, and M. K. Kutty, Expression of c-erbB3 protein in primary breast carcinomas, Br J Cancer, vol.78, pp.1385-1390, 1998.

M. Reschke, D. Mihic-probst, E. H. Van-der-horst, P. Knyazev, P. J. Wild et al., HER3 is a determinant for poor prognosis in melanoma, Clin Cancer Res, vol.14, pp.5188-5197, 2008.

M. Takikita, R. Xie, J. Y. Chung, H. Cho, K. Ylaya et al., Membranous expression of Her3 is associated with a decreased survival in head and neck squamous cell carcinoma, J Transl Med, vol.9, pp.126-136, 2011.

B. Tanner, D. Hasenclever, K. Stern, W. Schormann, M. Bezler et al., ErbB-3 predicts survival in ovarian cancer, J Clin Oncol, vol.24, pp.4317-4323, 2006.

G. Schaefer, L. Haber, L. M. Crocker, S. Shia, L. Shao et al., A two-in-one antibody against HER3 and EGFR has superior inhibitory activity compared with monospecific antibodies, Cancer Cell, vol.20, pp.472-486, 2011.

B. Schoeberl, E. A. Pace, J. B. Fitzgerald, B. D. Harms, L. Xu et al., Therapeutically targeting ErbB3: a key node in ligand-induced activation of the ErbB receptor-PI3K axis, Sci Signal, vol.2, p.31, 2009.

A. Beji, D. Horst, J. Engel, T. Kirchner, and A. Ullrich, Toward the prognostic significance and therapeutic potential of HER3 receptor tyrosine kinase in human colon cancer, Clin Cancer Res, vol.18, pp.956-968, 2012.

E. Blackburn, S. Zona, M. L. Murphy, I. R. Brown, S. K. Chan et al., A monoclonal antibody to the human HER3 receptor inhibits Neuregulin 1-beta binding and co-operates with Herceptin in inhibiting the growth of breast cancer derived cell lines, Breast Cancer Res Treat, vol.134, pp.53-59, 2012.

B. Schoeberl, A. C. Faber, D. Li, M. C. Liang, K. Crosby et al.,

A. Fulgham, Y. Song, and U. B. Nielsen, An ErbB3 antibody, MM-121, is active in cancers with ligand-dependent activation, Cancer Res, vol.70, pp.2485-2494, 2010.

M. R. Campbell, D. Amin, and M. M. Moasser, HER3 comes of age: new insights into its functions and role in signalling, tumor biology, and cancer therapy, Clin Cancer Res, vol.16, pp.1373-1383, 2010.

Q. Sheng, X. Liu, E. Fleming, K. Yuan, H. Piao et al., An activated ErbB3/ NRG1 autocrine loop supports in vivo proliferation in ovarian cancer cells, Cancer Cell, vol.17, pp.298-310, 2010.

Y. Lazrek, O. Dubreuil, V. Garambois, N. Gaborit, C. Larbouret et al., Anti-HER3 domain 1 and 3 antibodies reduce tumor growth by hindering HER2/HER3 dimerization and AKT-induced MDM2, XIAP, and FoxO1 phosphorylation, Neoplasia, vol.15, pp.335-347, 2013.
URL : https://hal.archives-ouvertes.fr/inserm-00815985

S. Lipkowitz, The role of the ubiquitination-proteasome pathway in breast cancer: ubiquitin mediated degradation of growth factor receptors in the pathogenesis and treatment of cancer, Breast Cancer Res, vol.5, pp.8-15, 2003.

A. M. Weissman, N. Shabek, and A. Ciechanover, The predator becomes the prey: regulating the ubiquitin system by ubiquitylation and degradation, Nat Rev Mol Cell Biol, vol.12, pp.605-620, 2011.

K. L. Carraway, E3 ubiquitin ligases in ErbB receptor quantity control, Semin Cell Dev Biol, vol.21, pp.936-943, 2010.

C. B. Thien and W. Y. Langdon, c-Cbl and Cbl-b ubiquitin ligases: substrate diversity and the negative regulation of signalling responses, Biochem J, vol.391, pp.153-166, 2005.

W. Xu, M. Marcu, X. Yuan, E. Mimnaugh, C. Patterson et al., Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu, Proc Natl Acad Sci USA, vol.99, pp.12847-12852, 2002.

S. M. Feng, R. S. Muraoka-cook, D. Hunter, M. A. Sandahl, L. S. Caskey et al., Earp HS 3rd. The E3 ubiquitin ligase WWP1 selectively targets HER4 and its proteolytically derived signalling isoforms for degradation, Mol Cell Biol, vol.29, pp.892-906, 2009.

J. Omerovic, L. Santangelo, E. M. Puggioni, J. Marrocco, C. Dall'armi et al., The E3 ligase Aip4/Itch ubiquitinates and targets ErbB-4 for degradation, Faseb J, vol.21, pp.2849-2862, 2007.

D. L. Wheeler, S. Huang, T. J. Kruser, M. M. Nechrebecki, E. A. Armstrong et al., Mechanisms of acquired resistance to cetuximab: role of HER (ErbB) family members, Oncogene, vol.27, pp.3944-3956, 2008.

D. A. Ferraro, N. Gaborit, R. Maron, H. Cohen-dvashi, Z. Porat et al., Inhibition of triple-negative breast cancer models by combinations of antibodies to EGFR, Proc Natl Acad Sci USA, vol.110, pp.1815-1820, 2013.

T. Ben-kasus, B. Schechter, S. Lavi, Y. Yarden, and M. Sela, Persistent elimination of ErbB-2/HER2-overexpressing tumors using combinations of monoclonal antibodies: relevance of receptor endocytosis, Proc Natl Acad Sci USA, vol.106, pp.3294-3299, 2009.

R. Maron, B. Schechter, M. Mancini, G. Mahlknecht, Y. Yarden et al., Inhibition of pancreatic carcinoma by homo-and heterocombinations of antibodies against EGFreceptor and its kin HER2/ErbB-2, Proc Natl Acad Sci USA, vol.110, pp.15389-15394, 2013.

J. B. Spangler, J. R. Neil, S. Abramovitch, Y. Yarden, F. M. White et al., Combination antibody treatment down-regulates epidermal growth factor receptor by inhibiting endosomal recycling, Proc Natl Acad Sci USA, vol.107, pp.13252-13257, 2010.

L. M. Friedman, A. Rinon, B. Schechter, L. Lyass, S. Lavi et al., Synergistic down-regulation of receptor tyrosine kinases by combinations of mAbs: implications for cancer immunotherapy, Proc Natl Acad Sci USA, vol.102, pp.1915-1920, 2005.

L. N. Klapper, H. Waterman, M. Sela, and Y. Yarden, Tumorinhibitory antibodies to HER-2/ErbB-2 may act by recruiting c-Cbl and enhancing ubiquitination of HER-2, Cancer Res, vol.60, pp.3384-3388, 2000.

J. M. Lee, B. Kim, S. B. Lee, Y. Jeong, Y. M. Oh et al., Cbl-independent degradation of Met: ways to avoid agonism of bivalent Met-targeting antibody, Oncogene, vol.33, pp.34-43, 2014.

A. J. Diamonti, P. M. Guy, C. Ivanof, K. Wong, C. Sweeney et al., An RBCC protein implicated in maintenance of steady-state neuregulin receptor levels, Proc Natl Acad Sci USA, vol.99, pp.2866-2871, 2002.

X. B. Qiu and A. L. Goldberg, Nrdp1/FLRF is a ubiquitin ligase promoting ubiquitination and degradation of the epidermal growth factor receptor family member, ErbB3, Proc Natl Acad Sci USA, vol.99, pp.14843-14848, 2002.

Z. Huang, B. K. Choi, K. Mujoo, X. Fan, M. Fa et al., The E3 ubiquitin ligase NEDD4 negatively regulates HER3/ErbB3 level and signalling, Oncogene, vol.34, pp.1105-1115, 2015.

D. N. Amin, N. Sergina, L. Lim, A. Goga, and M. M. Moasser, HER3 signalling is regulated through a multitude of redundant mechanisms in HER2-driven tumour cells, Biochem J, vol.447, pp.417-425, 2012.

S. Wee, Z. Jagani, K. X. Xiang, A. Loo, M. Dorsch et al., PI3K pathway activation mediates resistance to MEK inhibitors in KRAS mutant cancers, Cancer Res, vol.69, pp.4286-4293, 2009.

Z. Cao, X. Wu, Y. L. Sweeney, C. Carraway, and K. L. , Neuregulin-induced ErbB3 downregulation is mediated by a protein stability cascade involving the E3 ubiquitin ligase Nrdp1, Mol Cell Biol, vol.3, pp.2180-2188, 2007.

M. Sundvall, A. Korhonen, I. Paatero, E. Gaudio, G. Melino et al., Isoform-specific www.impactjournals.com/oncotarget monoubiquitination, endocytosis, and degradation of alternatively spliced ErbB4 isoforms, Proc Natl Acad Sci USA, vol.105, pp.4162-4167, 2008.

F. Zeng, J. Xu, and R. C. Harris, Nedd4 mediates ErbB4 JM-a/ CYT-1 ICD ubiquitination and degradation in MDCK II cells, Faseb J, vol.23, pp.1935-1945, 2009.

E. Gallagher, M. Gao, Y. C. Liu, and M. Karin, Activation of the E3 ubiquitin ligase Itch through a phosphorylation-induced conformational change, Proc Natl Acad Sci USA, vol.103, pp.1717-1722, 2006.

F. Scialpi, M. Malatesta, A. Peschiaroli, M. Rossi, G. Melino et al., Itch self-polyubiquitylation occurs through lysine-63 linkages, Biochem Pharmacol, vol.76, pp.1515-1521, 2008.

A. Oberst, M. Malatesta, R. I. Aqeilan, M. Rossi, P. Salomoni et al., The Nedd4-binding partner 1 (N4BP1) protein is an inhibitor of the E3 ligase Itch, Proc Natl Acad Sci USA, vol.104, pp.11280-11285, 2007.

C. Riling, H. Kamadurai, S. Kumar, C. E. O'leary, K. P. Wu et al., Itch WW Domains Inhibit Its E3 Ubiquitin Ligase Activity by Blocking E2-E3 Ligase Trans-thiolation, J Biol Chem, vol.290, pp.23875-23887, 2015.

N. C. Noyes, B. Hampton, M. Migliorini, and D. K. Strickland, Regulation of Itch and Nedd4 E3 Ligase Activity and Degradation by LRAD3, Biochemistry, vol.55, pp.1204-1213, 2016.

Y. Li, Z. Zhou, M. Alimandi, and C. Chen, WW domain containing E3 ubiquitin protein ligase 1 targets the full-length ErbB4 for ubiquitin-mediated degradation in breast cancer, Oncogene, vol.28, pp.2948-2958, 2009.

A. Panner, C. A. Crane, C. Weng, A. Feletti, S. Fang et al., Ubiquitin-specific protease 8 links the PTENAkt-AIP4 pathway to the control of FLIPS stability and TRAIL sensitivity in glioblastoma multiforme, Cancer Res, vol.70, pp.5046-5053, 2010.

P. A. Perez-mancera, A. G. Rust, L. Van-der-weyden, G. Kristiansen, A. Li et al., The deubiquitinase USP9X suppresses pancreatic ductal adenocarcinoma, Nature, vol.486, pp.266-270, 2012.

R. Mouchantaf, B. A. Azakir, P. S. Mcpherson, S. M. Millard, S. A. Wood et al., The ubiquitin ligase itch is autoubiquitylated in vivo and in vitro but is protected from degradation by interacting with the deubiquitylating enzyme FAM/USP9X, J Biol Chem, vol.28, pp.38738-38747, 2006.

X. Wu, Y. L. Irwin, L. Sweeney, C. Carraway, and K. L. , Stabilization of the E3 ubiquitin ligase Nrdp1 by the deubiquitinating enzyme USP8, Mol Cell Biol, vol.24, pp.7748-7757, 2004.

J. L. Cox, P. J. Wilder, E. L. Wuebben, M. M. Ouellette, M. A. Hollingsworth et al., Context-dependent function of the deubiquitinating enzyme USP9X in pancreatic ductal adenocarcinoma, Cancer Biol Ther, vol.15, pp.1042-1052, 2014.

N. Gaborit, A. Abdul-hai, M. Mancini, M. Lindzen, S. Lavi et al., Examination of HER3 targeting in cancer using monoclonal antibodies, Proc Natl Acad Sci USA, vol.112, pp.839-844, 2015.
URL : https://hal.archives-ouvertes.fr/hal-02276327

W. Dai, Y. Li, Q. Zhou, Z. Xu, C. Sun et al., Cetuximab inhibits oral squamous cell carcinoma invasion and metastasis via degradation of epidermal growth factor receptor, J Oral Pathol Med, vol.43, pp.250-257, 2014.

G. Sala, S. Traini, D. 'egidio, M. Vianale, G. Rossi et al., An ErbB-3 antibody, MP-RM-1, inhibits tumor growth by blocking ligand-dependent and independent activation of ErbB-3/Akt signaling, Oncogene, vol.31, pp.1275-1286, 2012.

F. Belleudi, E. Marra, F. Mazzetta, L. Fattore, M. R. Giovagnoli et al., Monoclonal antibody-induced ErbB3 receptor internalization and degradation inhibits growth and migration of human melanoma cells, Cell Cycle, vol.11, pp.1455-1467, 2012.
URL : https://hal.archives-ouvertes.fr/pasteur-00961644

M. Broussas, J. Dupont, A. Gonzalez, A. Blaecke, M. Fournier et al., Molecular mechanisms involved in activity of h7C10, a humanized monoclonal antibody, to IGF-1 receptor, Int J Cancer, vol.124, pp.2281-2293, 2009.

E. Pace, S. Adams, A. Camblin, M. Curley, V. Rimkunas et al., Effect of MM-141 on gemcitabine and nab-paclitaxel potentiation in preclinical models of pancreatic cancer through induction of IGF-1R and ErbB3 degradation, J Clin Oncol, vol.33, p.289, 2015.

X. R. Ren, J. Wang, T. Osada, R. A. Mook, M. A. Morse et al., Perhexiline promotes HER3 ablation through receptor internalization and inhibits tumor growth, Breast Cancer Res, vol.17, p.20, 2015.

G. Melino, R. A. Knight, and G. Cesareni, Degradation of p63 by Itch, Cell Cycle, vol.5, pp.1735-1739, 2006.

M. Rossi, D. Laurenzi, V. Munarriz, E. Green, D. R. Liu et al., The ubiquitin-protein ligase Itch regulates p73 stability, Embo J, vol.24, pp.836-848, 2005.

A. Vecchione, A. Marchese, P. Henry, D. Rotin, and A. Morrione, The Grb10/Nedd4 complex regulates ligand-induced ubiquitination and stability of the insulin-like growth factor I receptor, Mol Cell Biol, vol.23, pp.3363-3372, 2003.

S. Bouyain and D. J. Leahy, Structure-based mutagenesis of the substrate-recognition domain of Nrdp1/FLRF identifies the binding site for the receptor tyrosine kinase ErbB3, Protein Sci, vol.16, pp.654-661, 2007.

C. Chen, Y. Liu, and D. Zheng, An agonistic monoclonal antibody against DR5 induces ROS production, sustained JNK activation and Endo G release in Jurkat leukemia cells, Cell Res, vol.19, pp.984-995, 2009.

R. Stein, P. Gupta, X. Chen, T. M. Cardillo, R. R. Furman et al., Therapy of B-cell malignancies by anti-HLA-DR humanized monoclonal www.impactjournals.com/oncotarget antibody, IMMU-114, is mediated through hyperactivation of ERK and JNK MAP kinase signaling pathways, Blood, vol.115, pp.5180-5190, 2010.

A. Angers, A. R. Ramjaun, and P. S. Mcpherson, The HECT domain ligase itch ubiquitinates endophilin and localizes to the trans-Golgi network and endosomal system, J Biol Chem, vol.279, pp.11471-11479, 2004.

R. Malik, U. J. Soh, J. Trejo, and A. Marchese, Novel roles for the E3 ubiquitin ligase atrophin-interacting protein 4 and signal transduction adaptor molecule 1 in G protein-coupled receptor signalling, J Biol Chem, vol.287, pp.9013-9027, 2012.

G. Thomas, T. Chardès, N. Gaborit, C. Mollevi, W. Leconet et al., HER3 as biomarker and therapeutic target in pancreatic cancer: new insights in pertuzumab therapy in preclinical models, Oncotarget, vol.5, pp.7138-7148, 2014.
URL : https://hal.archives-ouvertes.fr/inserm-01075330