Model analysis of difference between EGF pathway and FGF pathway

Biochemical and Biophysical Research Communications

Volumn 314, Issue 4, 2004, Pages 1113-1120

  Yamada, Satoshi ^a   Taketomi, Takaharu ^b   Yoshimura, Akihiko ^b  

^a MITSUBISHI ELECTRIC CORPORATION   (Japan)

^b KYUSHU UNIVERSITY   (Japan)

Author keywords

Epidermal growth factor; Fibroblast growth factor; Fibroblast growth factor receptor substrate 2; Nerve growth factor

Indexed keywords

EPIDERMAL GROWTH FACTOR; EPIDERMAL GROWTH FACTOR RECEPTOR; FIBROBLAST GROWTH FACTOR; FIBROBLAST GROWTH FACTOR RECEPTOR 2; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2; MITOGEN ACTIVATED PROTEIN KINASE; SOS PROTEIN;

ANALYTIC METHOD; ANIMAL CELL; ARTICLE; CELL MEMBRANE; CELL STRAIN; COMPUTER SIMULATION; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; ENZYME ACTIVATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FUNCTION; RAT;

EID: 0942300661     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.01.009     Document Type: Article

References (24)

1. Lowy D.R., Willumsen B.M. Function and regulation of ras. Annu. Rev. Biochem. 62:1993;851-891.
2. Robinson M.J., Cobb M.H. Mitogen-activated protein kinase pathways. Curr. Opin. Cell Biol. 9:1997;180-186.
3. Morrison D.K., Cuthler R.E. The complexity of Raf-1 regulation. Curr. Opin. Cell Biol. 9:1997;174-179.
4. Sternberg P.W., Alberola-Ila J. Conspiracy theory: RAS and RAF do not act alone. Cell. 95:1998;447-450.
5. Kerkhoff E., Rapp U.R. The Ras-Raf relationship: an unfinished puzzle. Adv. Enzyme Regul. 41:2001;261-267.
6. Wakioka T., Sasaki A., Kato R., Shouda T., Matsumoto A., Miyoshi K., Tsuneoka M., Komiya S., Baron R., Yoshimura A. Spred is a Sprouty-related suppressor of Ras signalling. Nature. 412:2001;647-651.
7. Hacohen N., Kramer S., Sutherland D., Hiromi Y., Krasnow M.A. Sprouty encodes a novel antagonist of FGF signaling that patterns apical branching of the Drosophila airways. Cell. 92:1998;253-263.
8. Sasaki A., Taketomi T., Wakioka T., Kato R., Yoshimura A. Identification of a dominant negative mutant of Sprouty that potentiates fibroblast growth factor- but not epidermal growth factor-induced ERK activation. J. Biol. Chem. 276:2001;36804-36808.
9. deMaximy A.A., Nakatake Y., Moncada S., Itoh N., Thiery J.P., Bellusci S. Cloning and expression pattern of a mouse homologue of Drosophila sprouty in the mouse embryo. Mech. Dev. 81:1999;213-216.
10. Tefft J.D., Lee M., Smith S., Leinwand M., Zhao J., Bringas P. Jr., Crowe D.L., Warburton D. Conserved function of mSpry-2, a murine homolog of Drosophila sprouty, which negatively modulates respiratory organogenesis. Curr. Biol. 9:1999;219-222.
11. Sasaki A., Taketomi T., Kato R., Saeki K., Nonami A., Sasaki M., Kuriyama M., Saito N., Shibuya M., Yoshimura A. Mammalian Sproty4 suppresses Ras-independent ERK activation by binding to Raf1. Nat. Cell Biol. 5:2003;427-432.
12. Marshall C.J. Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation. Cell. 80:1995;179-185.
13. Traverse S., Seedorf K., Paterson H., Marshall C.J., Cohen P., Ullrich A. EGF triggers neuronal differentiation of PC12 cells that overexpress the EGF receptor. Curr. Biol. 4:1994;694-701.
14. Huang C.Y., Ferrell J.E. Jr. Ultrasensitivity in the mitogen-activated protein kinase cascade. Proc. Natl. Acad. Sci. USA. 93:1996;10078-10083.
15. Brightman F.A., Fell D.A. Differential feedback regulation of the MAPK cascade underlies the quantitative differences in EGF and NGF signalling in PC12 cells. FEBS Lett. 482:2000;169-174.
16. Kholodenko B.N., Demin O.V., Moehren G., Hoek J.B. Quantification of short term signaling by the epidermal growth factor receptor. J. Biol. Chem. 274:1999;30169-30181.
17. Ferrell J.E. Jr., Machleder E.M. The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes. Science. 280:1998;895-898.
18. Schoeberl B., Eichler-Jonsson C., Gilles E.D., Muller G. Computational modeling of the dynamics of the MAP kinase cascade activated by surface and internalized EGF receptors. Nat. Biotechnol. 20:2002;370-375.
19. Chen D., Waters S.B., Holt K.H., Pessin J.E. SOS phosphorylation and disassociation of the Grb2-SOS complex by the ERK and JNK signaling pathways. J. Biol. Chem. 271:1996;6328-6332.
20. Kouhara H., Hadari Y.R., Spival-Kroizman T., Schilling J., Bar-Sagi D., Lax I., Schlessinger J. A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway. Cell. 89:1997;693-702.
21. Hadari Y.R., Gotoh N., Kouhara H., Lax I., Schlessinger J. Critical role for the docking-protein FRS2 alpha in FGF receptor-mediated signal transduction pathways. Proc. Natl. Acad. Sci. USA. 98:2001;8578-8583.
22. Ong S.H., Guy G.R., Hadari Y.R., Laks S., Gotoh N., Schlessinger J., Lax I. FRS2 proteins recruit intracellular signaling pathways by binding to diverse targets on fibroblast growth factor and nerve growth factor receptors. Mol. Cell. Biol. 20:2000;979-989.
23. Goldberg D.E. Genetic Algorithms in Search, Optimization and Machine Learning. 1989;Addison-Wesley, Boston.
24. Yamada S., Shiono S., Joo A., Yoshimura A. Control mechanism of JAK/STAT signal transduction pathway. FEBS Lett. 534:2003;190-196.