Identification of the Mitogen-Activated Protein Kinase Phosphorylation Sites on Human Sosl That Regulate Interaction with Grb2

REFERENCES

• Aronheim, A., D. Engelberg, N. Li, N. al-Alawi, J. Schlessinger, and M. Karin. 1994. Membrane targeting of the nucleotide exchange factor Sos is sufficient for activating the Ras signaling pathway. Cell 78:949–961.
   PubMed Web of Science ®Google Scholar
• Baltensperger, K., L. M. Kozma, A. D. Cherniack, J. K. Klarlund, A. Chawla, U. Barnerjee, and M. P. Czech. 1993. Binding of the ras activator son of sevenless to insulin receptor substrate-1 signaling complexes. Science 260:1950–1952.
   PubMedGoogle Scholar
• Blattler, D. P., F. Garner, K. Van Slyke, and A. Bradley. 1972. Quantitative electrophoresis in polyacrylamide of 2-40%. J. Chromatogr. 64:147–155.
   Web of Science ®Google Scholar
• Boyle, N. J., P. Van der Geer, and T. Hunter. 1991. Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer plates. Methods Enzymol. 201:110–149.
   PubMed Web of Science ®Google Scholar
• Buday, L., and J. Downward. 1993. Epidermal growth factor regulates p21ras through the formation of a complex receptor, Grb2 adaptor protein, and Sos nucleotide exchange factor. Cell 48:611–620.
   Google Scholar
• Buday, L., P. H. Warne, and J. Downward. 1995. Downregulation of the Ras activation pathway by MAP kinase phosphorylation of Sos. Oncogene 11:1327–1331.
   PubMed Web of Science ®Google Scholar
• Burgering, B. M. T., G. J. Pronk, P. C. van Weeren, P. Chardin, and J. L. Bos. 1993. cAMP antagonizes p21 ras-directed activation of extracellular signal-regulated kinase 2 and phosphorylation of mSos nucleotide exchange factor. EMBO J. 12:4211–4220.
   PubMedGoogle Scholar
• Chardin, P., J. H. Camonis, N. W. Gale, L. Van Aelst, J. Schlessinger, M. H. Wigler, and D. Bar-Sagi. 1993. Human Sosl: a guanine nucleotide exchange factor for Ras that binds to Grb2. Science 260:1338–1343.
   PubMed Web of Science ®Google Scholar
• Chen, D., S. B. Waters, K. H. Holt, and J. E. Pessin. 1996. Sos phosphorylation and disassociation of the Grb2-Sos complex by ERK and JNK signaling pathways. J. Biol. Chem. 271:6328–6332.
   PubMed Web of Science ®Google Scholar
• Cherniack, A. D., J. K. Klarlund, B. R. Conway, and M. P. Czech. 1995. Disassembly of Son-of-sevenless proteins from Grb2 during p21ras desensitization by insulin. J. Biol. Chem. 270:1485–1488.
   PubMedGoogle Scholar
• Cherniack, A. D., J. K. Klarlund, and M. P. Czech. 1994. Phosphorylation of the Ras nucleotide exchange factor son of sevenless by mitogen-activated protein kinase. J. Biol. Chem. 269:4717–4720.
   PubMedGoogle Scholar
• Clark-Lewis, I., J. S. Sanghera, and S. L. Pelech. 1991. Definition of a consensus sequence for peptide substrate recognition by p44mpk, the meiosis-activated myelin basic protein kinase. J. Biol. Chem. 266:15180–15184.
   PubMedGoogle Scholar
• Corbalan-Garcia, S., K. R. Degenhardt, and D. Bar-Sagi. 1996. Insulin-induced dissociation of Sos from Grb2 does not contribute to the down regulation of Ras activation. Oncogene 12:1063–1068.
   PubMedGoogle Scholar
• Corbalan-Garcia, S., A. Whitmarsh, R. J. Davis, and D. Bar-Sagi. Unpublished observations.
   Google Scholar
• Egan, S. E., B. W. Giddings, M. W. Brooks, L. Buday, A. M. Sizeland, and R. Weinberg. 1993. Association of Sos ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation. Nature (London) 363:45–51.
   PubMed Web of Science ®Google Scholar
• Gonzalez, F. A., D. L. Raden, and R. J. Davis. 1991. Identification of substrate recognition determinants for human ERK1 and ERK2 protein kinases. J. Biol. Chem. 266:22159–22163.
   PubMed Web of Science ®Google Scholar
• Haycock, J. W., N. G. Ahn, M. H. Cobb, and E. G. Krebs. 1992. ERK1 and ERK2, two microtubule-associated protein 2 kinases, mediate the phosphorylation of tyrosine hydroxylase at serine-31 in situ. Proc. Natl. Acad. Sci. USA 89:2365–2369.
   PubMed Web of Science ®Google Scholar
• Holt, K. H., B. G. Kasson, and J. E. Pessin. 1996. Insulin stimulation of a MEK-dependent but ERK-independent Sos protein kinase. Mol. Cell. Biol. 16:577–583.
   PubMed Web of Science ®Google Scholar
• Karlovich, C. A., L. Bonfini, L. McCollam, R. D. Rogge, A. Daga, M. P. Czech, and U. Banerjee. 1995. In vivo functional analysis of the Ras exchange factor Son of Sevenless. Science 268:576–579.
   PubMed Web of Science ®Google Scholar
• Li, N., A. Batzer, R. Daly, V. Yajnik, E. Skolnik, P. Chardin, D. Bar-Sagi, B. Margolis, and J. Schlessinger. 1993. Guanine-nucleotide-releasing factor hSosl binds to Grb2 and links receptor tyrosine kinases to ras signaling. Nature (London) 363:85–88.
   PubMed Web of Science ®Google Scholar
• Li, N., J. Schlessinger, and B. Margolis. 1994. Autophosphorylation mutants of the EGF-receptor signal through auxiliary mechanisms involving SH2 domain proteins. Oncogene 9:3457–3465.
   PubMedGoogle Scholar
• Lowenstein, E. R., R. J. Daly, A. G. Batzer, W. Li, B. Margolis, R. Lammers, A. Ullrich, E. Y. Skolnik, D. Bar-Sagi, and J. Schlessinger. 1992. The SH2 and SH3 domain-containing protein Grb2 links receptor tyrosine kinases to ras signaling. Cell 70:431–442.
   PubMed Web of Science ®Google Scholar
• Mayer, B. J., and D. Baltimore. 1993. Signaling through SH2 and SH3 domains. Trends Cell Biol. 3:8–13.
   PubMedGoogle Scholar
• McCollam, L., L. Bonfini, C. A. Karlovich, B. R. Conway, L. M. Kozma, U. Banerjee, and M. P. Czech. 1995. Functional roles for the pleckstrin and Dbl homology regions in the Ras exchange factor Son of sevenless. J. Biol. Chem. 270:15954–15957.
   PubMedGoogle Scholar
• Porfiri, E., and F. McCormick. 1996. Regulation of epidermal growth factor receptor signaling by phosphorylation of the ras exchange factor hSosl. J. Biol. Chem. 271:5871–5877.
   PubMed Web of Science ®Google Scholar
• Rozakis-Adcock, M., R. Fernley, J. Wade, T. Pawson, and D. Bowtell. 1993. The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSosl. Nature (London) 363:83–85.
   PubMed Web of Science ®Google Scholar
• Rozakis-Adcock, M., J. McGlade, G. Mbamalu, G. Pelicci, R. Daly, W. Li, A. Batzer, S. Thomas, J. Brugge, P. G. Pelicci, J. Schlessinger, and T. Pawson. 1992. Association of the Shc and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases. Nature (London) 360:689–692.
   PubMed Web of Science ®Google Scholar
• Rozakis-Adcock, M., P. van der Geer, G. Mbamalu, and T. Pawson. 1995. MAP kinase phosphorylation of mSosl promotes dissociation of mSosl-Shc and mSosl-EGF receptor complexes. Oncogene 11:1417–1426.
   PubMed Web of Science ®Google Scholar
• Russo, G. L., M. T. Vandernberg, I. J. Yu, Y.-S. Bae, B. R. Franza, and D. R. Marshak. 1992. Caseine kinase II phosphorylates p34cdc2 kinase in G1 phase of the HeLa cell division cycle. J. Biol. Chem. 267:20317–20325.
   PubMed Web of Science ®Google Scholar
• Schlessinger, J., and D. Bar-Sagi. 1994. Activation of Ras and other signaling pathways by receptor tyrosine kinases. Cold Spring Harbor Symp. Quant. Biol. 59:173–179.
   PubMedGoogle Scholar
• Shibuya, E. K., A. J. Polverino, E. Chang, M. Wigler, and J. V. Ruderman. 1992. Oncogenic Ras triggers the activation of 42-kDa mitogen-activated protein kinase in extracts of quiescent Xenopus oocytes. Proc. Natl. Acad. Sci. USA 89:9831–9835.
   PubMed Web of Science ®Google Scholar
• Skolnik, E. Y., C. H. Lee, A. Batzer, L. M. Vicentini, M. Zhou, R. Daly, M. J. Myers, J. M. Backer, A. Ullrich, M. F. White, and J. Schlessinger. 1993. The SH2/SH3 domain containing protein Grb2 interacts with tyrosine phosphorylated IRS-1 and Shc: implications for insulin control of Ras signaling. EMBO J. 12:1929–1936.
   PubMed Web of Science ®Google Scholar
• Songyang, Z., S. Blechner, N. Hoagland, M. F. Hoekstra, H. Piwnica-Worms, and L. C. Cantley. 1994. Use of an oriented peptide library to determine the optimal substrates of protein kinases. Curr. Biol. 4:973–982.
   PubMed Web of Science ®Google Scholar
• Wang, W., E. M. C. Fisher, Q. Jia, J. M. Dum, E. Porfiri, J. Downward, and S. E. Egan. 1995. The Grb2 binding domain of mSosl is not required for downstream signal transduction. Nat. Genet. 10:294–300.
   PubMedGoogle Scholar
• Waters, S. B., K. H. Holt, S. E. Ross, L.-J. Syu, K.-L. Guan, A. R. Saltiel, G. A. Koretzky, and J. E. Pessin. 1995. Desensitization of Ras activation by a feedback dissociation of the Sos-Grb2 complex. J. Biol. Chem. 270:20883–20886.
   PubMed Web of Science ®Google Scholar
• Waters, S. B., K. Yamauchi, and J. E. Pessin. 1995. Insulin-stimulated disassociation of the Sos-Grb2 complex. Mol. Cell. Biol. 15:2791–2799.
   PubMedGoogle Scholar
• Wigler, M., S. Silverstein, L. S. Lee, A. Pellicer, Y. C. Cheng, and R. Axel. 1977. Transfer of purified herpes virus thymidine kinase gene to cultured mouse cells. Cell 11:223–227.
   PubMed Web of Science ®Google Scholar
• Yang, S. S., L. Van Aelst, and D. Bar-Sagi. 1995. Differential interactions of human Sosl and Sos2 with Grb2. J. Biol. Chem. 270:18212–18215.
   PubMedGoogle Scholar
• Zhao, L.-J., Q. X. Zhang, and R. Padmanabhan. 1993. Polymerase chain reaction-based point mutagenesis protocol. Methods Enzymol. 217:218–227.
   PubMedGoogle Scholar