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Published in: Breast Cancer Research 1/2007

01-02-2007 | Review

HER2 therapy. HER2 (ERBB2): functional diversity from structurally conserved building blocks

Author: Ralf Landgraf

Published in: Breast Cancer Research | Issue 1/2007

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Abstract

EGFR-type receptor tyrosine kinases achieve a broad spectrum of cellular responses by utilizing a set of structurally conserved building blocks. Based on available crystal structures and biochemical information, significant new insights have emerged into modes of receptor control, its deregulation in cancer, and the nuances that differentiate the four human receptors. This review gives an overview of current models of the control of receptor activity with a special emphasis on HER2 and HER3.
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Literature
1.
go back to reference Nahta R, Esteva FJ: Herceptin: mechanisms of action and resistance. Cancer Lett. 2006, 232: 123-138. 10.1016/j.canlet.2005.01.041.CrossRefPubMed Nahta R, Esteva FJ: Herceptin: mechanisms of action and resistance. Cancer Lett. 2006, 232: 123-138. 10.1016/j.canlet.2005.01.041.CrossRefPubMed
2.
go back to reference Pinkas-Kramarski R, Soussan L, Waterman H, Levkowitz G, Alroy I, Klapper L, Lavi S, Seger R, Ratzkin BJ, Sela M, et al: Diversification of Neu differentiation factor and epidermal growth factor signaling by combinatorial receptor interactions. EMBO J. 1996, 15: 2452-2467.PubMedPubMedCentral Pinkas-Kramarski R, Soussan L, Waterman H, Levkowitz G, Alroy I, Klapper L, Lavi S, Seger R, Ratzkin BJ, Sela M, et al: Diversification of Neu differentiation factor and epidermal growth factor signaling by combinatorial receptor interactions. EMBO J. 1996, 15: 2452-2467.PubMedPubMedCentral
3.
go back to reference Rubin I, Yarden Y: The basic biology of HER2. AnnOncol. 2001, S3-S8. 12 Suppl 1 Rubin I, Yarden Y: The basic biology of HER2. AnnOncol. 2001, S3-S8. 12 Suppl 1
4.
go back to reference Jones RB, Gordus A, Krall JA, MacBeath G: A quantitative protein interaction network for the ErbB receptors using protein microarrays. Nature. 2006, 439: 168-174. 10.1038/nature04177.CrossRefPubMed Jones RB, Gordus A, Krall JA, MacBeath G: A quantitative protein interaction network for the ErbB receptors using protein microarrays. Nature. 2006, 439: 168-174. 10.1038/nature04177.CrossRefPubMed
5.
go back to reference Bose R, Molina H, Patterson AS, Bitok JK, Periaswamy B, Bader JS, Pandey A, Cole PA: Phosphoproteomic analysis of Her2/neu signaling and inhibition. Proc Natl Acad Sci USA. 2006, 103: 9773-9778. 10.1073/pnas.0603948103.CrossRefPubMedPubMedCentral Bose R, Molina H, Patterson AS, Bitok JK, Periaswamy B, Bader JS, Pandey A, Cole PA: Phosphoproteomic analysis of Her2/neu signaling and inhibition. Proc Natl Acad Sci USA. 2006, 103: 9773-9778. 10.1073/pnas.0603948103.CrossRefPubMedPubMedCentral
6.
go back to reference Guy PM, Platko JV, Cantley LC, Cerione RA, Carraway KLR: Insect cell-expressed p180erbB3 possesses an impaired tyrosine kinase activity. Proc Natl Acad Sci USA. 1994, 91: 8132-8136. 10.1073/pnas.91.17.8132.CrossRefPubMedPubMedCentral Guy PM, Platko JV, Cantley LC, Cerione RA, Carraway KLR: Insect cell-expressed p180erbB3 possesses an impaired tyrosine kinase activity. Proc Natl Acad Sci USA. 1994, 91: 8132-8136. 10.1073/pnas.91.17.8132.CrossRefPubMedPubMedCentral
7.
go back to reference Kim HH, Vijapurkar U, Hellyer NJ, Bravo D, Koland JG: Signal transduction by epidermal growth factor and heregulin via the kinase-deficient ErbB3 protein. Biochem J. 1998, 334: 189-195.CrossRefPubMedPubMedCentral Kim HH, Vijapurkar U, Hellyer NJ, Bravo D, Koland JG: Signal transduction by epidermal growth factor and heregulin via the kinase-deficient ErbB3 protein. Biochem J. 1998, 334: 189-195.CrossRefPubMedPubMedCentral
8.
go back to reference Stove C, Bracke M: Roles for neuregulins in human cancer. Clin Exp Metastasis. 2004, 21: 665-684. 10.1007/s10585-004-6917-6.CrossRefPubMed Stove C, Bracke M: Roles for neuregulins in human cancer. Clin Exp Metastasis. 2004, 21: 665-684. 10.1007/s10585-004-6917-6.CrossRefPubMed
9.
go back to reference Zhou BB, Peyton M, He B, Liu C, Girard L, Caudler E, Lo Y, Barib-aud F, Mikami I, Reguart N, et al: Targeting ADAM-mediated ligand cleavage to inhibit HER3 and EGFR pathways in non-small cell lung cancer. Cancer Cell. 2006, 10: 39-50. 10.1016/j.ccr.2006.05.024.CrossRefPubMedPubMedCentral Zhou BB, Peyton M, He B, Liu C, Girard L, Caudler E, Lo Y, Barib-aud F, Mikami I, Reguart N, et al: Targeting ADAM-mediated ligand cleavage to inhibit HER3 and EGFR pathways in non-small cell lung cancer. Cancer Cell. 2006, 10: 39-50. 10.1016/j.ccr.2006.05.024.CrossRefPubMedPubMedCentral
10.
go back to reference Warren CM, Kani K, Landgraf R: The N-terminal domains of neuregulin 1 confer signal attenuation. J Biol Chem. 2006, 281: 27306-27316. 10.1074/jbc.M512887200.CrossRefPubMed Warren CM, Kani K, Landgraf R: The N-terminal domains of neuregulin 1 confer signal attenuation. J Biol Chem. 2006, 281: 27306-27316. 10.1074/jbc.M512887200.CrossRefPubMed
11.
go back to reference Kani K, Warren CM, Kaddis CS, Loo JA, Landgraf R: Oligomers of ERBB3 have two distinct interfaces that differ in their sensitivity to disruption by heregulin. J Biol Chem. 2005, 280: 8238-8247. 10.1074/jbc.M410944200.CrossRefPubMed Kani K, Warren CM, Kaddis CS, Loo JA, Landgraf R: Oligomers of ERBB3 have two distinct interfaces that differ in their sensitivity to disruption by heregulin. J Biol Chem. 2005, 280: 8238-8247. 10.1074/jbc.M410944200.CrossRefPubMed
12.
go back to reference Burgess AW, Cho HS, Eigenbrot C, Ferguson KM, Garrett TP, Leahy DJ, Lemmon MA, Sliwkowski MX, Ward CW, Yokoyama S: An open-and-shut case? Recent insights into the activation of EGF/ErbB receptors. Mol Cell. 2003, 12: 541-552. 10.1016/S1097-2765(03)00350-2.CrossRefPubMed Burgess AW, Cho HS, Eigenbrot C, Ferguson KM, Garrett TP, Leahy DJ, Lemmon MA, Sliwkowski MX, Ward CW, Yokoyama S: An open-and-shut case? Recent insights into the activation of EGF/ErbB receptors. Mol Cell. 2003, 12: 541-552. 10.1016/S1097-2765(03)00350-2.CrossRefPubMed
13.
go back to reference Leahy DJ: Structure and function of the epidermal growth factor (EGF/ErbB) family of receptors. Adv Protein Chem. 2004, 68: 1-27.CrossRefPubMed Leahy DJ: Structure and function of the epidermal growth factor (EGF/ErbB) family of receptors. Adv Protein Chem. 2004, 68: 1-27.CrossRefPubMed
14.
go back to reference Kohda D, Odaka M, Lax I, Kawasaki H, Suzuki K, Ullrich A, Schlessinger J, Inagaki F: A 40-kDa epidermal growth factor/transforming growth factor alpha- binding domain produced by limited proteolysis of the extracellular domain of the epidermal growth factor receptor. J Biol Chem. 1993, 268: 1976-1981.PubMed Kohda D, Odaka M, Lax I, Kawasaki H, Suzuki K, Ullrich A, Schlessinger J, Inagaki F: A 40-kDa epidermal growth factor/transforming growth factor alpha- binding domain produced by limited proteolysis of the extracellular domain of the epidermal growth factor receptor. J Biol Chem. 1993, 268: 1976-1981.PubMed
15.
go back to reference Singer EM, Landgraf R, Horan T, Slamon DJ, Eisenberg D: Identification of a heregulin binding site in HER3 extracellular domain. J Biol Chem. 2001, 276: 44266-44274. 10.1074/jbc.M105428200.CrossRefPubMed Singer EM, Landgraf R, Horan T, Slamon DJ, Eisenberg D: Identification of a heregulin binding site in HER3 extracellular domain. J Biol Chem. 2001, 276: 44266-44274. 10.1074/jbc.M105428200.CrossRefPubMed
16.
go back to reference Kani K, Park E, Landgraf R: The extracellular domains of ErbB3 retain high ligand binding affinity at endosome pH and in the locked conformation. Biochemistry. 2005, 44: 15842-15857. 10.1021/bi0515220.CrossRefPubMed Kani K, Park E, Landgraf R: The extracellular domains of ErbB3 retain high ligand binding affinity at endosome pH and in the locked conformation. Biochemistry. 2005, 44: 15842-15857. 10.1021/bi0515220.CrossRefPubMed
17.
go back to reference Kim JH, Saito K, Yokoyama S: Chimeric receptor analyses of the interactions of the ectodomains of ErbB-1 with epidermal growth factor and of those of ErbB-4 with neuregulin. Eur J Biochem. 2002, 269: 2323-2329. 10.1046/j.1432-1033.2002.02877.x.CrossRefPubMed Kim JH, Saito K, Yokoyama S: Chimeric receptor analyses of the interactions of the ectodomains of ErbB-1 with epidermal growth factor and of those of ErbB-4 with neuregulin. Eur J Biochem. 2002, 269: 2323-2329. 10.1046/j.1432-1033.2002.02877.x.CrossRefPubMed
18.
go back to reference Ogiso H, Ishitani R, Nureki O, Fukai S, Yamanaka M, Kim JH, Saito K, Sakamoto A, Inoue M, Shirouzu M, Yokoyama S: Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains. Cell. 2002, 110: 775-787. 10.1016/S0092-8674(02)00963-7.CrossRefPubMed Ogiso H, Ishitani R, Nureki O, Fukai S, Yamanaka M, Kim JH, Saito K, Sakamoto A, Inoue M, Shirouzu M, Yokoyama S: Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains. Cell. 2002, 110: 775-787. 10.1016/S0092-8674(02)00963-7.CrossRefPubMed
19.
go back to reference Garrett TP, McKern NM, Lou M, Elleman TC, Adams TE, Lovrecz GO, Zhu HJ, Walker F, Frenkel MJ, Hoyne PA, et al: Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha. Cell. 2002, 110: 763-773. 10.1016/S0092-8674(02)00940-6.CrossRefPubMed Garrett TP, McKern NM, Lou M, Elleman TC, Adams TE, Lovrecz GO, Zhu HJ, Walker F, Frenkel MJ, Hoyne PA, et al: Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha. Cell. 2002, 110: 763-773. 10.1016/S0092-8674(02)00940-6.CrossRefPubMed
20.
go back to reference Elleman TC, Domagala T, McKern NM, Nerrie M, Lonnqvist B, Adams TE, Lewis J, Lovrecz GO, Hoyne PA, Richards KM, et al: Identification of a determinant of epidermal growth factor receptor ligand-binding specificity using a truncated, high-affinity form of the ectodomain. Biochemistry. 2001, 40: 8930-8939. 10.1021/bi010037b.CrossRefPubMed Elleman TC, Domagala T, McKern NM, Nerrie M, Lonnqvist B, Adams TE, Lewis J, Lovrecz GO, Hoyne PA, Richards KM, et al: Identification of a determinant of epidermal growth factor receptor ligand-binding specificity using a truncated, high-affinity form of the ectodomain. Biochemistry. 2001, 40: 8930-8939. 10.1021/bi010037b.CrossRefPubMed
21.
go back to reference Dawson JP, Berger MB, Lin CC, Schlessinger J, Lemmon MA, Ferguson KM: Epidermal growth factor receptor dimerization and activation require ligand-induced conformational changes in the dimer interface. Mol Cell Biol. 2005, 25: 7734-7742. 10.1128/MCB.25.17.7734-7742.2005.CrossRefPubMedPubMedCentral Dawson JP, Berger MB, Lin CC, Schlessinger J, Lemmon MA, Ferguson KM: Epidermal growth factor receptor dimerization and activation require ligand-induced conformational changes in the dimer interface. Mol Cell Biol. 2005, 25: 7734-7742. 10.1128/MCB.25.17.7734-7742.2005.CrossRefPubMedPubMedCentral
22.
go back to reference Garrett TP, McKern NM, Lou M, Frenkel MJ, Bentley JD, Lovrecz GO, Elleman TC, Cosgrove LJ, Ward CW: Crystal structure of the first three domains of the type-1 insulin-like growth factor receptor. Nature. 1998, 394: 395-399. 10.1038/28668.CrossRefPubMed Garrett TP, McKern NM, Lou M, Frenkel MJ, Bentley JD, Lovrecz GO, Elleman TC, Cosgrove LJ, Ward CW: Crystal structure of the first three domains of the type-1 insulin-like growth factor receptor. Nature. 1998, 394: 395-399. 10.1038/28668.CrossRefPubMed
23.
go back to reference Cho HS, Mason K, Ramyar KX, Stanley AM, Gabelli SB, Denney DW, Leahy DJ: Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab. Nature. 2003, 421: 756-760. 10.1038/nature01392.CrossRefPubMed Cho HS, Mason K, Ramyar KX, Stanley AM, Gabelli SB, Denney DW, Leahy DJ: Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab. Nature. 2003, 421: 756-760. 10.1038/nature01392.CrossRefPubMed
24.
go back to reference Cho HS, Leahy DJ: Structure of the extracellular region of HER3 reveals an interdomain tether. Science. 2002, 297: 1330-1333. 10.1126/science.1074611.CrossRefPubMed Cho HS, Leahy DJ: Structure of the extracellular region of HER3 reveals an interdomain tether. Science. 2002, 297: 1330-1333. 10.1126/science.1074611.CrossRefPubMed
25.
go back to reference Ferguson KM, Berger MB, Mendrola JM, Cho HS, Leahy DJ, Lemmon MA: EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization. Mol Cell. 2003, 11: 507-517. 10.1016/S1097-2765(03)00047-9.CrossRefPubMed Ferguson KM, Berger MB, Mendrola JM, Cho HS, Leahy DJ, Lemmon MA: EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization. Mol Cell. 2003, 11: 507-517. 10.1016/S1097-2765(03)00047-9.CrossRefPubMed
26.
go back to reference Li S, Schmitz KR, Jeffrey PD, Wiltzius JJ, Kussie P, Ferguson KM: Structural basis for inhibition of the epidermal growth factor receptor by cetuximab. Cancer Cell. 2005, 7: 301-311. 10.1016/j.ccr.2005.03.003.CrossRefPubMed Li S, Schmitz KR, Jeffrey PD, Wiltzius JJ, Kussie P, Ferguson KM: Structural basis for inhibition of the epidermal growth factor receptor by cetuximab. Cancer Cell. 2005, 7: 301-311. 10.1016/j.ccr.2005.03.003.CrossRefPubMed
27.
go back to reference Bouyain S, Longo PA, Li S, Ferguson KM, Leahy DJ: The extracellular region of ErbB4 adopts a tethered conformation in the absence of ligand. Proc Natl Acad Sci USA. 2005, 102: 15024-15029. 10.1073/pnas.0507591102.CrossRefPubMedPubMedCentral Bouyain S, Longo PA, Li S, Ferguson KM, Leahy DJ: The extracellular region of ErbB4 adopts a tethered conformation in the absence of ligand. Proc Natl Acad Sci USA. 2005, 102: 15024-15029. 10.1073/pnas.0507591102.CrossRefPubMedPubMedCentral
28.
go back to reference Garrett TP, McKern NM, Lou M, Elleman TC, Adams TE, Lovrecz GO, Kofler M, Jorissen RN, Nice EC, Burgess AW, et al: The crystal structure of a truncated ErbB2 ectodomain reveals an active conformation, poised to interact with other ErbB receptors. Mol Cell. 2003, 11: 495-505. 10.1016/S1097-2765(03)00048-0.CrossRefPubMed Garrett TP, McKern NM, Lou M, Elleman TC, Adams TE, Lovrecz GO, Kofler M, Jorissen RN, Nice EC, Burgess AW, et al: The crystal structure of a truncated ErbB2 ectodomain reveals an active conformation, poised to interact with other ErbB receptors. Mol Cell. 2003, 11: 495-505. 10.1016/S1097-2765(03)00048-0.CrossRefPubMed
29.
go back to reference Walker F, Orchard SG, Jorissen RN, Hall NE, Zhang H-H, Hoyne PA, Adams TE, Johns TG, Ward C, Garrett TPJ, et al: CR1/CR2 interactions modulate the functions of the cell surface epidermal growth factor receptor. J Biol Chem. 2004, 279: 22387-22398. 10.1074/jbc.M401244200.CrossRefPubMed Walker F, Orchard SG, Jorissen RN, Hall NE, Zhang H-H, Hoyne PA, Adams TE, Johns TG, Ward C, Garrett TPJ, et al: CR1/CR2 interactions modulate the functions of the cell surface epidermal growth factor receptor. J Biol Chem. 2004, 279: 22387-22398. 10.1074/jbc.M401244200.CrossRefPubMed
30.
go back to reference Ozcan F, Klein P, Lemmon MA, Lax I, Schlessinger J: On the nature of low- and high-affinity EGF receptors on living cells. Proc Natl Acad Sci USA. 2006, 103: 5735-5740. 10.1073/pnas.0601469103.CrossRefPubMedPubMedCentral Ozcan F, Klein P, Lemmon MA, Lax I, Schlessinger J: On the nature of low- and high-affinity EGF receptors on living cells. Proc Natl Acad Sci USA. 2006, 103: 5735-5740. 10.1073/pnas.0601469103.CrossRefPubMedPubMedCentral
31.
go back to reference Wang Y, Pennock S, Chen X, Wang Z: Endosomal signaling of epidermal growth factor receptor stimulates signal transduction pathways leading to cell survival. Mol Cell Biol. 2002, 22: 7279-7290. 10.1128/MCB.22.20.7279-7290.2002.CrossRefPubMedPubMedCentral Wang Y, Pennock S, Chen X, Wang Z: Endosomal signaling of epidermal growth factor receptor stimulates signal transduction pathways leading to cell survival. Mol Cell Biol. 2002, 22: 7279-7290. 10.1128/MCB.22.20.7279-7290.2002.CrossRefPubMedPubMedCentral
32.
go back to reference Teis D, Wunderlich W, Huber LA: Localization of the MP1-MAPK scaffold complex to endosomes is mediated by p14 and required for signal transduction. Dev Cell. 2002, 3: 803-814. 10.1016/S1534-5807(02)00364-7.CrossRefPubMed Teis D, Wunderlich W, Huber LA: Localization of the MP1-MAPK scaffold complex to endosomes is mediated by p14 and required for signal transduction. Dev Cell. 2002, 3: 803-814. 10.1016/S1534-5807(02)00364-7.CrossRefPubMed
33.
go back to reference Jiang G, Hunter T: Receptor signaling: when dimerization is not enough. Curr Biol. 1999, 9: R568-R571. 10.1016/S0960-9822(99)80357-1.CrossRefPubMed Jiang G, Hunter T: Receptor signaling: when dimerization is not enough. Curr Biol. 1999, 9: R568-R571. 10.1016/S0960-9822(99)80357-1.CrossRefPubMed
34.
go back to reference Sorokin A, Lemmon MA, Ullrich A, Schlessinger J: Stabilization of an active dimeric form of the epidermal growth factor receptor by introduction of an inter-receptor disulfide bond. J Biol Chem. 1994, 269: 9752-9759.PubMed Sorokin A, Lemmon MA, Ullrich A, Schlessinger J: Stabilization of an active dimeric form of the epidermal growth factor receptor by introduction of an inter-receptor disulfide bond. J Biol Chem. 1994, 269: 9752-9759.PubMed
35.
go back to reference Cao H, Bangalore L, Dompe C, Bormann BJ, Stern DF: An extra cysteine proximal to the transmembrane domain induces differential cross-linking of p185neu and p185neu. J Biol Chem. 1992, 267: 20489-20492.PubMed Cao H, Bangalore L, Dompe C, Bormann BJ, Stern DF: An extra cysteine proximal to the transmembrane domain induces differential cross-linking of p185neu and p185neu. J Biol Chem. 1992, 267: 20489-20492.PubMed
36.
go back to reference Moriki T, Maruyama H, Maruyama IN: Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain. J Mol Biol. 2001, 311: 1011-1026. 10.1006/jmbi.2001.4923.CrossRefPubMed Moriki T, Maruyama H, Maruyama IN: Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain. J Mol Biol. 2001, 311: 1011-1026. 10.1006/jmbi.2001.4923.CrossRefPubMed
37.
go back to reference Burke CL, Lemmon MA, Coren BA, Engelman DM, Stern DF: Dimerization of the p185neu transmembrane domain is necessary but not sufficient for transformation. Oncogene. 1997, 14: 687-696. 10.1038/sj.onc.1200873.CrossRefPubMed Burke CL, Lemmon MA, Coren BA, Engelman DM, Stern DF: Dimerization of the p185neu transmembrane domain is necessary but not sufficient for transformation. Oncogene. 1997, 14: 687-696. 10.1038/sj.onc.1200873.CrossRefPubMed
38.
go back to reference Zhang X, Gureasko J, Shen K, Cole PA, Kuriyan J: An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. Cell. 2006, 125: 1137-1149. 10.1016/j.cell.2006.05.013.CrossRefPubMed Zhang X, Gureasko J, Shen K, Cole PA, Kuriyan J: An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. Cell. 2006, 125: 1137-1149. 10.1016/j.cell.2006.05.013.CrossRefPubMed
39.
go back to reference Huang GC, Ouyang X, Epstein RJ: Proxy activation ofprotein ErbB2 by heterologous ligands implies a heterotetrameric mode of receptor tyrosine kinase interaction. Biochem J. 1998, 331: 113-119.CrossRefPubMedPubMedCentral Huang GC, Ouyang X, Epstein RJ: Proxy activation ofprotein ErbB2 by heterologous ligands implies a heterotetrameric mode of receptor tyrosine kinase interaction. Biochem J. 1998, 331: 113-119.CrossRefPubMedPubMedCentral
40.
go back to reference Jeffrey PD, Russo AA, Polyak K, Gibbs E, Hurwitz J, Massague J, Pavletich NP: Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex. Nature. 1995, 376: 313-320. 10.1038/376313a0.CrossRefPubMed Jeffrey PD, Russo AA, Polyak K, Gibbs E, Hurwitz J, Massague J, Pavletich NP: Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex. Nature. 1995, 376: 313-320. 10.1038/376313a0.CrossRefPubMed
41.
go back to reference Berger MB, Mendrola JM, Lemmon MA: ErbB3/HER3 does nothomodimerize upon neuregulin binding at the cell surface. FEBS Lett. 2004, 569: 332-336. 10.1016/j.febslet.2004.06.014.CrossRefPubMed Berger MB, Mendrola JM, Lemmon MA: ErbB3/HER3 does nothomodimerize upon neuregulin binding at the cell surface. FEBS Lett. 2004, 569: 332-336. 10.1016/j.febslet.2004.06.014.CrossRefPubMed
42.
go back to reference Mendrola JM, Berger MB, King MC, Lemmon MA: The single transmembrane domains of ErbB receptors self-associate in cell membranes. J Biol Chem. 2002, 277: 4704-4712. 10.1074/jbc.M108681200.CrossRefPubMed Mendrola JM, Berger MB, King MC, Lemmon MA: The single transmembrane domains of ErbB receptors self-associate in cell membranes. J Biol Chem. 2002, 277: 4704-4712. 10.1074/jbc.M108681200.CrossRefPubMed
43.
go back to reference Fleishman SJ, Schlessinger J, Ben-Tal N: A putative molecular-activation switch in the transmembrane domain of erbB2. Proc Natl Acad Sci USA. 2002, 99: 15937-15940. 10.1073/pnas.252640799.CrossRefPubMedPubMedCentral Fleishman SJ, Schlessinger J, Ben-Tal N: A putative molecular-activation switch in the transmembrane domain of erbB2. Proc Natl Acad Sci USA. 2002, 99: 15937-15940. 10.1073/pnas.252640799.CrossRefPubMedPubMedCentral
44.
go back to reference Schaefer G, Akita RW, Sliwkowski MX: A discrete three-amino acid segment (LVI) at the C-terminal end of kinase-impaired ErbB3 is required for transactivation of ErbB2. J Biol Chem. 1999, 274: 859-866. 10.1074/jbc.274.2.859.CrossRefPubMed Schaefer G, Akita RW, Sliwkowski MX: A discrete three-amino acid segment (LVI) at the C-terminal end of kinase-impaired ErbB3 is required for transactivation of ErbB2. J Biol Chem. 1999, 274: 859-866. 10.1074/jbc.274.2.859.CrossRefPubMed
45.
go back to reference Landau M, Fleishman SJ, Ben-Tal N: A putative mechanism for down regulation of the catalytic activity of the EGF receptor via direct contact between its kinase and C-terminal domains. Structure. 2004, 12: 2265-2275. 10.1016/j.str.2004.10.006.CrossRefPubMed Landau M, Fleishman SJ, Ben-Tal N: A putative mechanism for down regulation of the catalytic activity of the EGF receptor via direct contact between its kinase and C-terminal domains. Structure. 2004, 12: 2265-2275. 10.1016/j.str.2004.10.006.CrossRefPubMed
46.
go back to reference Citri A, Gan J, Mosesson Y, Vereb G, Szollosi J, Yarden Y: Hsp90 restrains ErbB-2/HER2 signalling by limiting heterodimer formation. EMBO Rep. 2004, 5: 1165-1170. 10.1038/sj.embor.7400300.CrossRefPubMedPubMedCentral Citri A, Gan J, Mosesson Y, Vereb G, Szollosi J, Yarden Y: Hsp90 restrains ErbB-2/HER2 signalling by limiting heterodimer formation. EMBO Rep. 2004, 5: 1165-1170. 10.1038/sj.embor.7400300.CrossRefPubMedPubMedCentral
47.
go back to reference Citri A, Harari D, Shohat G, Ramakrishnan P, Gan J, Lavi S, Eisen-stein M, Kimchi A, Wallach D, Pietrokovski S, et al: Hsp90 recognizes a common surface on client kinases. J Biol Chem. 2006, 281: 14361-14369. 10.1074/jbc.M512613200.CrossRefPubMed Citri A, Harari D, Shohat G, Ramakrishnan P, Gan J, Lavi S, Eisen-stein M, Kimchi A, Wallach D, Pietrokovski S, et al: Hsp90 recognizes a common surface on client kinases. J Biol Chem. 2006, 281: 14361-14369. 10.1074/jbc.M512613200.CrossRefPubMed
48.
go back to reference Li H, Ruano MJ, Villalobo A: Endogenous calmodulin interacts with the epidermal growth factor receptor in living cells. FEBS Lett. 2004, 559: 175-180. 10.1016/S0014-5793(04)00067-5.CrossRefPubMed Li H, Ruano MJ, Villalobo A: Endogenous calmodulin interacts with the epidermal growth factor receptor in living cells. FEBS Lett. 2004, 559: 175-180. 10.1016/S0014-5793(04)00067-5.CrossRefPubMed
49.
go back to reference Li H, Sanchez-Torres J, Del Carpio A, Salas V, Villalobo A: The ErbB2/Neu/HER2 receptor is a new calmodulin-binding protein. Biochem J. 2004, 381: 257-266. 10.1042/BJ20031008.CrossRefPubMedPubMedCentral Li H, Sanchez-Torres J, Del Carpio A, Salas V, Villalobo A: The ErbB2/Neu/HER2 receptor is a new calmodulin-binding protein. Biochem J. 2004, 381: 257-266. 10.1042/BJ20031008.CrossRefPubMedPubMedCentral
50.
go back to reference McLaughlin S, Smith SO, Hayman MJ, Murray D: An electrostatic engine model for autoinhibition and activation of the epidermal growth factor receptor (EGFR/ErbB) family. J Gen Physiol. 2005, 126: 41-53. 10.1085/jgp.200509274.CrossRefPubMedPubMedCentral McLaughlin S, Smith SO, Hayman MJ, Murray D: An electrostatic engine model for autoinhibition and activation of the epidermal growth factor receptor (EGFR/ErbB) family. J Gen Physiol. 2005, 126: 41-53. 10.1085/jgp.200509274.CrossRefPubMedPubMedCentral
51.
go back to reference Franklin MC, Carey KD, Vajdos FF, Leahy DJ, de Vos AM, Sli-wkowski MX: Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex. Cancer Cell. 2004, 5: 317-328. 10.1016/S1535-6108(04)00083-2.CrossRefPubMed Franklin MC, Carey KD, Vajdos FF, Leahy DJ, de Vos AM, Sli-wkowski MX: Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex. Cancer Cell. 2004, 5: 317-328. 10.1016/S1535-6108(04)00083-2.CrossRefPubMed
52.
go back to reference Molina MA, Codony-Servat J, Albanell J, Rojo F, Arribas J, Baselga J: Trastuzumab (herceptin), a humanized anti-Her2 receptor monoclonal antibody, inhibits basal and activated Her2 ecto-domain cleavage in breast cancer cells. Cancer Res. 2001, 61: 4744-4749.PubMed Molina MA, Codony-Servat J, Albanell J, Rojo F, Arribas J, Baselga J: Trastuzumab (herceptin), a humanized anti-Her2 receptor monoclonal antibody, inhibits basal and activated Her2 ecto-domain cleavage in breast cancer cells. Cancer Res. 2001, 61: 4744-4749.PubMed
Metadata
Title
HER2 therapy. HER2 (ERBB2): functional diversity from structurally conserved building blocks
Author
Ralf Landgraf
Publication date
01-02-2007
Publisher
BioMed Central
Published in
Breast Cancer Research / Issue 1/2007
Electronic ISSN: 1465-542X
DOI
https://doi.org/10.1186/bcr1633

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