Two Chimeric Receptors of Epidermal Growth Factor Receptor and c-Ros That Differ in Their Transmembrane Domains Have Opposite Effects on Cell Growth

REFERENCES

• Berharu, P., A. M. Rohilla, and W. J. Rutter. 1990. Replacement of the human insulin receptor transmembrane and cytoplasmic domains by corresponding domains of the oncogene product v-ros leads to accelerated in-ternalization, degradation and down regulation. J. Biol. Chem. 265:9505–9511.
   PubMedGoogle Scholar
• Birchmeier, C., K. O’Neill, M. Riggs, and M. Wigler. 1990. Characterization of ROS 1 cDNA from a human glioblastoma cell line. Proc. Natl. Acad. Sci. USA 87:4799–4803.
   PubMed Web of Science ®Google Scholar
• Birchmeier, C., S. Sharma, and M. Wigler. 1987. Expression and rearrangement of the ROS1 gene in human glioblastoma cells. Proc. Natl. Acad. Sci. USA 84:9270–9274.
   PubMed Web of Science ®Google Scholar
• Cantley, L. C., K. R. Auger, C. Carpenter, B. Duckworth, A. Grazianti, R. Kapeller, and S. Soltoff. 1991. Oncogenes and signal transduction. Cell 64:281–302.
   PubMed Web of Science ®Google Scholar
• Chen, J., M. Heller, B. Poon, L. Kang, and L.-H. Wang. 1991. The protooncogene c-ros codes for a transmembrane tyrosine kinase sharing sequence and structural homology with sevenless protein of Drosophila melanogaster. Oncogene 6:257–264.
   PubMed Web of Science ®Google Scholar
• Chen, J., and L.-H. Wang. Unpublished data.
   Google Scholar
• Chen, J., Q. Xiong, and L.-H. Wang. Unpublished data.
   Google Scholar
• Chen, J., C. S. Zong, and L.-H. Wang. 1994. Tissue and epithelial cell-specific expression of chicken proto-oncogene c-ros in several organs suggests that it may play roles in their development and mature functions. Oncogene 9:773–780.
   PubMedGoogle Scholar
• Chen, W. S., L. S. Lazar, K. A. Lund, J. B. Welsh, C. P. Chang, G. M. Walton, L. J. Der, H. S. Wiley, G. N. Gill, and M. G. Rosenfeld. 1989. Functional independence of the epidermal growth factor receptor from a domain required for ligand-induced internalization and calcium regulation. Cell 59:33–43.
   PubMed Web of Science ®Google Scholar
• Di Fiore, P. P., O. Segatto, F. Conardo, F. Fazioli, J. H. Pierce, and S. A. Aaronson. 1990. The carboxy-terminal domains of erbB-2 and epidermal growth factor receptor exert different regulatory effects on intrinsic receptor tyrosine kinase function and transforming activity. Mol. Cell. Biol. 10:2749–2756.
   PubMedGoogle Scholar
• Dikic, I., J. Schlessinger, and I. Lax. 1994. PC12 cells overexpressing the insulin receptor undergo insulin-dependent neuronal differentiation. Curr. Biol. 4:702–708.
   PubMed Web of Science ®Google Scholar
• Ellis, L., E. Clauser, D. O. Morgan, M. Edery, R. A. Roth, and W. J. Rutter. 1986. Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated activity and uptake of 2-deoxyglucose. Cell 45:721–732.
   PubMed Web of Science ®Google Scholar
• Feldman, R. A., L.-H. Wang, H. Hanafusa, and P. C. Balduzzi. 1982. Avian sarcoma virus UR2 encodes a transforming protein which is associated with a unique protein kinase activity. J. Virol. 42:128–136.
   Google Scholar
• Filmus, J., J. M. Trent, M. N. Pollak, and R. N. Buick. 1987. Epidermal growth factor receptor gene-amplified MDA-468 breast cancer cell line and its nonamplified variants. Mol. Cell. Biol. 7:251–257.
   PubMed Web of Science ®Google Scholar
• Gill, G. N., and L. S. Lazar. 1981. Increased phosphotyrosine content and inhibition of proliferation in EGF-treated A431 cells. Nature (London) 293:305–307.
   PubMed Web of Science ®Google Scholar
• Gonclalves, E., K. Yamada, H. S. Thatte, J. M. Backer, D. E. Golan, C. R. Kahn, and S. E. Shoelson. 1993. Optimizing transmembrane domain helicity accelerates insulin receptor internalization and lateral mobility. Proc. Natl. Acad. Sci. USA 90:5762–5766.
   PubMedGoogle Scholar
• Gospodarowicz, D., G. Greenburg, H. Biaslecki, and B. R. Zether. 1978. Factors involved in the modulation of cell proliferation in vivo and in vitro: the role of fibroblast and epidermal growth factors in the proliferative response of mammalian cells. In Vitro (Rockville) 14:85–118.
   PubMedGoogle Scholar
• Graham, F. L., and A. J. Van Der Eb. 1973. A new technique for the assay of infectivity of human adenovirus DNA. Virology 52:456–467.
   PubMed Web of Science ®Google Scholar
• Haft, C. R., R. D. Klausner, and S. I. Taylor. 1994. Involvement of dileucine motifs in the internalization and degradation of the insulin receptor. J. Biol. Chem. 269:26286–26294.
   PubMedGoogle Scholar
• Hanafusa, H. 1969. Rapid transformation of cells by Rous sarcoma virus. Proc. Natl. Acad. Sci. USA 63:318–325.
   PubMedGoogle Scholar
• Hirai, M., S. Gamous, S. Minoshima, and N. Shimizu. 1988. Two independent mechanisms for escaping EGF-mediated growth inhibition in EGFR-hyperproducing human tumor cells. J. Cell Biol. 107:791–799.
   PubMedGoogle Scholar
• Hunter, T., and J. Pines. 1995. Cyclins and cancer II: cyclin D and CDK inhibitors. Cell 79:573–582.
   Google Scholar
• Jiang, Y., J. Chan, C. Zong, and L.-H. Wang. Unpublished data.
   Google Scholar
• Jong, S. M., and L.-H. Wang. 1987. The transforming protein p68gag-ros of avian sarcoma virus UR2 is a transmembrane protein with the gag protein protruding extracellularly. Oncogene Res. 1:7–21.
   PubMedGoogle Scholar
• Jong, S. M., and L.-H. Wang. 1990. Role of gag sequence in the biochemical properties and transforming activity of the avian sarcoma virus UR2-en-coded gag-ros fusion protein. J. Virol. 64:5997–6009.
   PubMedGoogle Scholar
• Jong, S. M., and L.-H. Wang. 1991. Two point mutations in the transmem-brane domain of P68gag-ros inactivate its transforming activity and cause a delay in membrane association. J. Virol. 65:180–189.
   PubMedGoogle Scholar
• Kaburagi, Y., K. Momomura, R. Yamamoto-Honda, K. Tobe, Y. Tamor, H. Sakura, Y. Akanuma, Y. Yazaki, and T. Kadowaki. 1993. Site-directed mu-tagenesis of the juxtamembrane domain of the human insulin receptor. J. Biol. Chem. 268:16610–16622.
   PubMedGoogle Scholar
• Kraus, M. H., P. Fedi, V. Starks, R. Muraro, and S. A. Aaronson. 1993. Demonstration of ligand-dependent signaling by the erbB3 tyrosine kinase and its constitutive activation in human breast tumor cells. Proc. Natl. Acad. Sci. USA 90:2900–2904.
   PubMed Web of Science ®Google Scholar
• Lammers, R., A. Gray, J. Schlessinger, and A. Ullrich. 1989. Differential signaling potential of insulin and IGF1-receptor cytoplasmic domains. EMBO J. 8:1369–1375.
   PubMed Web of Science ®Google Scholar
• Lehvaslaiho, H., L. Lehtola, L. Sistonen, and K. Alitalo. 1989. A chimeric EGFR-neu proto-oncogene allows EGF to regulate Neu tyrosine kinase and cell transformation. EMBO J. 8:159–166.
   PubMedGoogle Scholar
• Lhotak, V., and T. Pawson. 1993. Biological and biochemical activities of a chimeric epidermal growth factor-Elk receptor tyrosine kinase. Mol. Cell. Biol. 13:7071–7079.
   PubMedGoogle Scholar
• Lifshitz, A., L. S. Lazar, J. Buss, and G. N. Gill. 1983. Analysis of morphology and receptor metabolism in clonal variant A431 cells with differing growth response to EGF. J. Cell. Physiol. 115:235–242.
   PubMedGoogle Scholar
• Liu, D.-L., W. J. Rutter, and L.-H. Wang. 1993. Modulating effects of the extracellular sequence of the human insulin-like growth factor 1 receptor on its transforming and tumorigenic potential. J. Virol. 67:9–18.
   PubMedGoogle Scholar
• Lund, K. A., L. S. Lazar, W. S. Chen, B. J. Walsh, J. B. Welsh, J. J. Herbst, G. M. Walton, M. G. Rosenfeld, G. N. Gill, and H. S. Wiley. 1990. Phos-phorylation of the epidermal growth factor receptor at threonine 654 inhibits ligand-mediated internalization and down-regulation. J. Biol. Chem. 265:20517–20523.
   PubMed Web of Science ®Google Scholar
• Matsushime, H., and M. Shibuya. 1990. Tissue-specific expression of rat c-ros-1 gene and partial structural similarity of its predicted products with sev protein of Drosophila melanogaster. J. Virol. 64:2117–2125.
   PubMed Web of Science ®Google Scholar
• Mori, S., L. Claesson-Welsh, and L. H. Heldin. 1991. Identification of a hydrophobic region in the carboxyl terminus of the platelet-derived growth factor beta-receptor which is important for ligand-mediated endocytosis. J. Biol. Chem. 266:21156–21164.
   Google Scholar
• Nicoletti, I., F. Gribnani, T. Pawson, and P. G. Pelicci. 1992. A novel transforming protein (Shc) with an SH2 domain is implicated in mitogen transduction. Cell 70:93–104.
   PubMedGoogle Scholar
• Nurse, P. 1995. Ordering S phase and M phase in the cell cycle. Cell 79:547–550.
   Google Scholar
• Pandiella, A., H. Lehvaslaiho, M. Magni, K. Altitalo, and J. Meldolesi. 1989. Activation of an EGFR/Neu chimeric receptor: early intracellular signals and cell proliferation responses. Oncogene 4:1299–1305.
   PubMedGoogle Scholar
• Pardee, A. B. 1989. G1 events and regulation of cell proliferation. Science 246:603–608.
   PubMed Web of Science ®Google Scholar
• Prager, D., H.-L. Li, H. Yamasaki, and S. Melmed. 1994. Human insulin-like growth factor 1 receptor internalization: role of the juxtamembrane domain. J. Biol. Chem. 269:11934–11937.
   PubMedGoogle Scholar
• Rajagopalan, M., J. L. Neidigh, and D. A. McClain. 1991. Amino acid sequence Gly-Pro-Leu-Tyr and Asn-Pro-Glu-Tyr in the submembrane domain of the insulin receptor are required for normal endocytosis. J. Biol. Chem. 266:23068–23073.
   PubMedGoogle Scholar
• Riedel, H., T. J. Dull, A. M. Honegger, J. Schlessinger, and A. Ullrich. 1989. Cytoplasmic domains determine signal specificity, cellular routing characteristics and influence ligand binding of epidermal growth factor and insulin receptors. EMBO J. 8:2943–2954.
   PubMed Web of Science ®Google Scholar
• Riedel, H., T. J. Dull, J. Schlessinger, and A. Ullrich. 1986. A chimeric receptor allows insulin to stimulate tyrosine kinase activity of epidermal growth factor receptor. Nature (London) 324:68–70.
   PubMed Web of Science ®Google Scholar
• Riethmacher, D., O. Langhalz, S. Goddecke, M. Sachs, and L. Birchmeier. 1994. Biochemical and functional characterization of the murine ros protooncogene. Oncogene 9:3617–3626.
   PubMedGoogle Scholar
• Sell, L., G. Dumenil, L. Deveaud, M. Miura, D. Coppola, T. DeAngelis, R. Rubin, A. Efstratiadis, and R. Baserga. 1994. Effect of a null mutation of the insulin-like growth factor I receptor gene on growth and transformation of mouse embryo fibroblasts. Mol. Cell. Biol. 14:3604–3612.
   PubMed Web of Science ®Google Scholar
• Sherr, C. J. 1995. G1 phase progression: cycling on cue. Cell 79:551–555.
   Google Scholar
• Shiota, G., D. B. Rhoad, T. C. Wang, T. Nakamura, and E. V. Schmidt. 1992. Hepatocyte growth factor inhibits growth of hepatocellular carcinoma cells. Proc. Natl. Acad. Sci. USA 89:373–377.
   PubMed Web of Science ®Google Scholar
• Skolink, E. Y., C. H. Lee, A. Ratzer et al. 1993. The SH2/SH3 domain-containing protein Grb2 interacts with tyrosine phosphorylated IRS1 and Shc: implication for insulin control of ras signalling. EMBO J. 12:1929–1936.
   PubMedGoogle Scholar
• Sonnenberg, E., A. Godecke, B. Walter, F. Bladt, and C. Birchmeier. 1991. Transient and locally restricted expression of the ros1 proto-oncogene during mouse development. EMBO J. 10:3693–3702.
   PubMed Web of Science ®Google Scholar
• Sun, X. J., P. Rothenberg, C. R. Kahn, J. M. Backer, E. Araki, P. A. Wilden, D. A. Cahill, B. J. Goldstein, and M. F. White. 1991. Structure of the insulin receptor substrate IRS1 defines a unique signal transduction protein. Nature (London) 351:73–77.
   Google Scholar
• Tessarollo, L., L. Nagarajan, and L. F. Parada. 1992. c-ros: the vertebrate homolog of the sevenless tyrosine kinase receptor is tightly regulated during organogenesis in mouse embryonic development. Development 115:11–20.
   PubMedGoogle Scholar
• Traverse, S., K. Seedorf, H. Paterson, C. J. Marshall, P. Cohen, and A. Ullrich. 1994. EGF triggers neuronal differentiation of PC12 cells that over-express the EGF receptor. Curr. Biol. 418:694–701.
   Google Scholar
• Ullrich, A., and J. Schlessinger. 1990. Signal transduction by receptors with tyrosine kinase activity. Cell 61:202–212.
   Web of Science ®Google Scholar
• Yan, H., J. Schlessinger, and M. V. Chao. 1991. Chimeric NGF-EGF receptor define domains responsible for neuronal differentiation. Science 252:561–563.
   PubMedGoogle Scholar
• Zong, C. S., B. Poon, J. Chen, and L.-H. Wang. 1993. Molecular and biochemical bases for activation of the transforming potential of the protooncogene c-ros. J. Virol. 67:6453–6462.
   PubMedGoogle Scholar
• Zong, C. S., and L.-H. Wang. 1994. Modulatory effect of the transmembrane domain of the protein-tyrosine kinase encoded by oncogene ros: biological function and substrate interaction. Proc. Natl. Acad. Sci. USA 91:10982–10986.
   PubMedGoogle Scholar