Multiple positive and negative regulators of signaling by the EGF-receptor

Current Opinion in Cell Biology

Volumn 11, Issue 2, 1999, Pages 190-196

  Moghal, Nadeem ^a   Sternberg, Paul W ^a  

^a HOWARD HUGHES MEDICAL INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR; LIGAND; PROTEIN TYROSINE KINASE;

DIMERIZATION; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN LOCALIZATION; REGULATORY MECHANISM; REVIEW; SIGNAL TRANSDUCTION;

EID: 0032939325     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(99)80025-8     Document Type: Article

References (64)

1. Aroian R.V., Sternberg P.W. Multiple functions of let-23, a C. elegans receptor tyrosine kinase gene required for vulval induction. Genetics. 128:1991;251-267.
2. Price J.V., Clifford R.J., Schupbach T. The maternal ventralizing locus torpedo is allelic to faint little ball, an embryonic lethal, and encodes the Drosophila EGF receptor homolog. Cell. 56:1989;1085-1092.
3. Schejter E.D., Shilo B. The Drosophila EGF receptor homolog (DER) gene is allelic to faint little ball, a locus essential for embryonic development. Cell. 56:1989;1093-1104.
4. Sibilia M., Wagner E.F. Strain-dependent epithelial defects in mice lacking the EGF receptor. Science. 269:1995;234-238.
5. Threadgill D.W., Dlugosz A.A., Hansen L.A., Tennenbaum T., Lichti U., Yee D., Lamantia C., Mourton T., Herrup K., Harris R.C.et al. Targeted disruption of mouse EGF receptor - effect of genetic background on mutant phenotype. Science. 269:1995;230-234.
6. Reise D.J.I., Stern D.F. Specificity within the EGF family/ErbB receptor family signaling network. Bioessays. 20:1998;41-48.
7. Graus-Porta D., Beerli R.R., Daly J.M., Hynes N.E. ErbB-2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signaling. EMBO J. 16:1997;1647-1655.
8. Tzahar E., Waterman H., Chen X., Levkowitz G., Karunagaran D., Lavi S., Ratzkin B.J., Yarden Y. A hierarchical network of interreceptor interactions determines signal transduction by Neu differentiation factor/neuregulin and epidermal growth factor. Mol Cell Biol. 16:1996;5276-5287.
9. Beerli R.R., Graus-Porta D., Woods-Cook K., Chen X., Yarden Y., Hynes N.E. Neu differentiation factor activation of ErbB-3 and ErbB-4 is cell specific and displays a differential requirement for ErbB-2. Mol Cell Biol. 15:1995;6496-6505.
10. Graus-Porta D., Beerli R.R., Hynes N.E. Single-chain antibody-mediated intracellular retention of ErbB-2 impairs Neu differentiation factor and epidermal growth factor signaling. Mol Cell Biol. 15:1995;1182-1191.
11. Olayioye M.A., Graus-Porta D., Beerli R.R., Rohrer J., Gay B., Hynes N.E. ErbB-1 and ErbB-2 acquire distinct signaling properties dependent upon their dimerization partner. Mol Cell Biol. 18:1998;5042-5051. This work demonstrates that the specific pattern of tyrosyl phosphorylation of an ErbB family member is dependent on the nature of the heterodimerizing partner, as well as the ligand. In addition, it is shown that different ligand-receptor combinations result in qualitative, quantitative, and kinetic differences in effector molecule recruitment.
12. Sweeney Crovello C., Lai C., Cantley L.C., Carraway K.L. Jr. Differential signaling by the epidermal growth factor-like growth factors Neuregulin-1 and Neuregulin-2. J Biol Chem. 273:1998;26954-26961.
13. Pinkas-Kramarski R., Shelly M., Guarino B.C., Wang L.M., Lyass L., Alroy I., Alamandi M., Kuo A., Moyer J.D., Lavi S.et al. ErbB tyrosine kinases and the two neuregulin families constitute a ligand-receptor network. Mol Cell Biol. 18:1998;6090-6101.
14. Schnepp B., Donaldson T., Grumbling G., Ostrowski S., Schweitzer R., Shilo B-Z., Simcox A. EGF domain swap converts a Drosophila EGF receptor activator into an inhibitor. Genes Dev. 12:1998;908-913.
15. Howes R., Wasserman J.D., Freeman M. In vivo analysis of Argos structure-function. J Biol Chem. 273:1998;4275-4281.
16. van de Poll M.L., van Vugt M.J., Lenferink A.E., van Zoelen E.J. Insertion of Argos sequences into the B-loop of epidermal growth factor results in a low-affinity ligand with strong agonistic activity. Biochemistry. 36:1997;7425-7431.
17. Moscatello D.K., Santra M., Mann D.M., McQuillan D.J., Wong A.J., Iozzo R.V. Decorin suppresses tumor cell growth by activating the epidermal growth factor receptor. J Clin Invest. 101:1998;406-412.
18. 2+ in A431 carcinoma cells. J Biol Chem. 273:1998;3121-3124.
19. Vieira A.V., Lamaze C., Schmid S.L. Control of EGF receptor signaling by clathrin-mediated endocytosis. Science. 274:1996;2086-2089.
20. Lenferink A.E.G., Pinkas-Kramarski R., van de Poll M.L.M., van Vugt M.J.H., Klapper L.N., Tzahar E., Waterman H., Sela M., van Zoelen E.J.J., Yarden Y. Differential endocytic routing of homo- and hetero-dimeric ErbB tyrosine kinases confers signaling superiority to receptor heterodimers. EMBO J. 17:1998;3385-3397.
21. Ferguson E., Horvitz H.R. Identification and characterization of 22 genes that affect the vulval cell lineages of Caenorhabditis elegans. Genetics. 110:1985;17-72.
22. Kaech S.M., Whitfield C.W., Kim S.K. The LIN-2/LIN-7/LIN-10 complex mediates basolateral membrane localization of the C. elegans EGF receptor LET-23 in vulval epithelial cells. Cell. 94:1998;761-771. An elegant demonstration by a combination of in vivo and in vitro studies that a new complex of PDZ-domain-containing proteins acts in vivo to localize LET-23 to basolateral membranes. Compensating mutations in LIN-7 and LET-23 define the interaction site in vivo.
23. Butz S., Okamoto M., Südhof T.C. A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Cell. 94:1998;773-782.
24. Rongo C., Whitfield C.W., Rodal A., Kim S.K., Kaplan J.M. LIN-10 is a shared component of the polarized protein localization pathways in neurons and epithelia. Cell. 94:1998;751-759.
25. Rommel C., Hafen E. Ras - a versatile cellular switch. Curr Opin Genet Dev. 8:1998;412-418.
26. Sternberg P.W., Alberola-Ila J. Conspiracy Theory: Ras and Raf do not act alone. Cell. 95:1998;447-450.
27. Ji G.S., Ermini S., Baulida J., Sun F.L., Carpenter G. Epidermal growth factor signaling and mitogenesis in PLCγ1 null mouse embryonic fibroblasts. Mol Biol Cell. 9:1998;749-757. Analysis of mouse cells genetically defective in PLCγ1 fail to find a role for this major EGFR effector in fibroblasts.
28. Hollenberg M.D. Tyrosine kinase pathways and the regulation of smooth muscle contractility. Trends Pharm Sci. 15:1994;108-114.
29. Lesa G.M., Sternberg P.W. Positive and negative tissue-specific signaling by a nematode epidermal growth factor receptor. Mol Biol Cell. 8:1997;779-793. Systematic site-directed mutagenesis of LET-23 indicates distinct positive and negative functions of the receptor, and that six tyrosine sites function in vivo.
30. Clandinin T.R., DeModena J.A., Sternberg P.W. Inositol trisphosphate mediates a RAS-independent response to LET-23 receptor kinase activation in C. elegans. Cell. 92:1998;523-533. Genetic suppressor analysis reveals a striking example of the cell-type specific utilization of different signaling pathways by one receptor. In addition to the previously known RAS-RAF pathway, C. elegans LET-23 signals via inositol trisphosphate to stimulate ovulation. A role for inositol trisphosphate 3 kinase in down regulating signaling in vivo is demonstrated.
31. Habib A.A., Högnason T., Ren J., Stefánsson K., Ratan R.R. The epidermal growth factor receptor associates with and recruits phosphatidylinositol 3-kinase to the platelet-derived growth factor β receptor. J Biol Chem. 273:1998;6885-6891.
32. Habib T., Hejna J.A., Moses R.E., Decker S.J. Growth factors and insulin stimulate tyrosine phosphorylation of the 51C/SHIP2 protein. J Biol Chem. 273:1998;18605-18609.
33. 3 at the 3′ position on the inositol ring in vitro.
34. +/-(heterozygous) cells.
35. Bennett A.M., Hausdorff S.F., O'Reilly A.M., Freeman R.M. Jr., Neel B.G. Multiple requirements for SHPTP2 in epidermal growth factor-mediated cell cycle progression. Mol Cell Biol. 16:1996;1189-1202.
36. Perkins L.A., Larsen I., Perrimon N. corkscrew encodes a putative protein tyrosine phosphatase that functions to transduce the terminal signal from the receptor tyrosine kinase torso. Cell. 70:1992;225-236.
37. Gutch M.J., Flint A.J., Keller J., Tonks N.K., Hengartner M.O. The Caenorhabditis elegans SH2 domain-containing protein tyrosine phosphatase PTP-2 participates in signal transduction during oogenesis and vulval development. Genes Dev. 12:1998;571-585.
38. Holgado-Madruga M., Emlet D.R., Moscatello D.K., Godwin A.K., Wong A.J. A Grb2-associated docking protein in EGF- and insulin-receptor signalling. Nature. 379:1996;560-564.
39. Herbst R., Carroll P.M., Allard J.D., Schilling J., Raabe T., Simon M.A. Daughter of Sevenless is a substrate of the phosphotyrosine phosphatase corkscrew and functions during Sevenless signaling. Cell. 85:1996;899-909.
40. Hajnal A., Whitfield C.W., Kim S.K. Inhibition of Caenorhabditis elegans vulval induction by gap-1 and by let-23 receptor tyrosine kinase. Genes Dev. 11:1997;2715-2728.
41. Jongeward G.D., Clandinin T.R., Sternberg P.W. sli-1, a negative regulator of let-23-mediated signaling in C. elegans. Genetics. 139:1995;1553-1566.
42. Hayashizaki S., Iino Y., Yamamoto M. Characterization of the C. elegans gap-2 gene encoding a novel Ras-GTPase activating protein and its possible role in larval development. Genes Cells. 3:1998;189-202.
43. Yoon C.H., Lee J., Jongeward G.D., Sternberg P.W. Similarity of sli-1, a regulator of vulval development in Caenorhabditis elegans, to the mammalian proto-oncogene, c-cbl. Science. 269:1995;1102-1105.
44. Smit L., Borst J. The Cbl family of signal transduction molecules. Crit Rev Oncogen. 8:1997;359-379.
45. 292 negative regulatory phosphorylation site of ZAP-70. J Biol Chem. 272:1997;33140-33144.
46. Hime G.R., Dhungat M.P., Ng A., Bowtell D.D. D-Cbl, the Drosophila homologue of the c-Cbl proto-oncogene, interacts with the Drosophila EGF receptor in vivo, despite lacking C-terminal adaptor binding sites. Oncogene. 14:1997;2709-2719.
47. Meisner H., Daga A., Buxton J., Fernandez B., Chawla A., Banerjee U., Czech M.P. Interactions of Drosophila Cbl with epidermal growth factor receptors, role of Cbl in R7 photoreceptor. Mol Cell Biol. 17:1997;2217-2225.
48. Murphy M.A., Schnall R.G., Venter D.J., Barnett L., Bertoncello I., Thien C.B.F., Langdon W.Y., Bowtell D.D.L. Tissue hyperplasia and enhanced T-cell signalling via ZAP-70 in c-CBl-deficient mice. Mol Cell Biol. 18:1998;4872-4882. By a targeted gene knockout, Cbl is shown to regulate TCR signaling in murine T cells. This study should provide the means to evaluate more critically the role of Cbl in EGFR signaling.
49. Levkowitz G., Waterman H., Zamir E., Kam Z., Oved S., Langdon W.Y., Beguinot L., Geiger B., Yarden Y. c-Cbl/Sli-1 regulates endocytic sorting and ubiquitination of the epidermal growth factor receptor. Genes Dev. 12:1998;3663-3674. Provides strong evidence that Cbl acts to affect degradation and sorting of EGFR. Parallel experiments with ErbB3 indicate that it is not regulated by Cbl.
50. Miyake S., Lupher M.L. Jr., Druker B., Band H. The tyrosine kinase regulator Cbl enhances the ubiquitination and degradation of the platelet-derived growth factor receptor α Proc Natl Acad Sci USA. 95:1998;7927-7932. Demonstrates that overexpression of Cbl affects degradation of an RTK.
51. Daub H., Wallasch C., Lankenau A., Herrlich A., Ullrich A. Signal characteristics of G-protein-transactivated EGF receptor. EMBO J. 16:1997;7032-7044.
52. Daub H., Weiss F.U., Wallasch C., Ullrich A. Role of transactivation of the EGF receptor in signalling by G-protein-coupled receptors. Nature. 379:1996;557-560.
53. Luttrell L.M., Della Rocca G.J., van Biesen T., Luttrell D.K., Lefkowitz R.J. Gβγ subunits mediate Src-dependent phosphorylation of the epidermal growth factor receptor. J Biol Chem. 272:1997;4637-4644.
54. Dikic I., Tokiwa G., Lev S., Courtneidge S.A., Schlessinger J. A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation. Nature. 383:1996;547-550.
55. Yamauchi T., Ueki K., Tobe K., Tamemoto H., Sekine N., Wada M., Honjo M., Takahashi M., Takahashi T., Hirai H.et al. Tyrosine phosphorylation of the EGF receptor by the kinase Jak2 is induced by growth hormone. Nature. 390:1997;91-96. This work demonstrates that a tyrosine kinase, JAK2, belonging to a signaling pathway that is distinct from EGFR, can phosphorylate specific sites on the cytoplasmic tail of the EGFR and hence activate the RAS/MAPK pathway in the absence of EGFR catalytic activity.
56. Johnson J.L., Fenton S., Sheffield L.G. Prolactin inhibits epidermal growth factor-induced Ras-MAPK signaling in mammary epithelial cells. J Biol Chem. 271:1996;21574-21578.
57. Fenton S.E., Sheffield L.G. Prolactin inhibits EGF-induced DNA synthesis in mammary epithelium via early signaling mechanisms: possible involvement of protein kinase C. Exp Cell Res. 236:1997;285-293.
58. Rosen L.B., Greenberg M.E. Stimulation of growth factor receptor signal transduction by activation of voltage-sensitive calcium channels. Proc Natl Acad Sci USA. 93:1996;1113-1118.
59. Zwick E., Daub H., Aoki N., Yamaguchi-Aoki Y., Tinhofer I., Maly K., Ullrich A. Critical role of calcium-dependent epidermal growth factor receptor transactivation in PC12 cell membrane depolarization and bradykinin signaling. J Biol Chem. 272:1997;24767-24770.
60. 2+-induced regulation of ion channel and MAP kinase functions. Nature. 376:1995;737-745.
61. Fujioka Y., Matozaki T., Noguchi T., Iwamatsu A., Yamao T., Takahashi N., Tsuda M., Takada T., Kasuga M. A novel membrane glycoprotein, SHPS-1, that binds SH2-domain-containing protein tyrosine phosphatase SHP-2 in response to mitogens and cell adhesion. Mol Cell Biol. 16:1996;6887-6899.
62. Kharitonenkov A., Chen Z., Sures I., Wang H., Schilling J., Ullrich A. A family of proteins that inhibit signalling through tyrosine kinase receptors. Nature. 386:1997;181-186.
63. Schneller M., Vuori K., Ruoslahti E. αvβ3 integrin associates with activated insulin, PDGFβ receptors and potentiates the biological activity of PDGF. EMBO J. 16:1997;5600-5607. This work demonstrates a growth-factor-dependent physical association between an RTK and integrin molecules; furthermore, it is shown that this association is likely to be significant for fibroblasts and since activation of the integrin enhances RTK-dependent MAPK activation and proliferation.
64. Moghal N., Neel B.G. Integration of growth factor, extracellular matrix, and retinoid signals during bronchial epithelial cell differentiation. Mol Cell Biol. 18:1998;6666-6678. This work demonstrates that some ECM molecules can promote normal cellular responses such as differentiation by restricting the amount of growth factor dependent MAPK activation. Evidence also is provided that molecules distinct from the RTK itself may be targets for ECM-derived signaling pathways.