p66SHC Promotes Apoptosis and Antagonizes Mitogenic Signaling in T Cells

REFERENCES

• Baldari, C. T., and Telford J. L.. 1999. Lymphocyte antigen receptor signal integration and regulation by the SHC adaptor. Biol. Chem. 380:129–134.
   PubMedGoogle Scholar
• Bonfini, L., Migliaccio E., Pelicci G., Lanfrancone L., and Pelicci P. G.. 1996. Not all Shc's roads lead to Ras. Trends Biochem. Sci. 21:257–261.
   PubMed Web of Science ®Google Scholar
• Carrel, S., Moretta A., Pantaleo G., Tambussi G., Isler P., Perussia B., and Cerottini J. C.. 1988. Stimulation and proliferation of CD4+ peripheral blood T lymphocytes induced by an anti-CD4 monoclonal antibody. Eur. J. Immunol. 18:333–339.
   PubMedGoogle Scholar
• D'Ambrosio, D., Cantrell D. A., Frati L., Santoni A., and Testi R.. 1994. Involvement of p21ras activation in T cell CD69 expression. Eur. J. Immunol. 24:616–620.
   PubMed Web of Science ®Google Scholar
• el-Deiry, W. S. 1998. Regulation of p53 downstream genes. Semin. Cancer Biol. 8:345–357.
   PubMed Web of Science ®Google Scholar
• Friedmann, M. C., Migone T. S., Russell S. M., and Leonard W. J.. 1996. Different interleukin 2 receptor beta-chain tyrosines couple to at least two signaling pathways and synergistically mediate interleukin 2-induced proliferation. Proc. Natl. Acad. Sci. USA 93:2077–2082.
   PubMed Web of Science ®Google Scholar
• Gorczyca, W., Gong J., and Darzynkiewicz Z.. 1993. Detection of DNA strand breaks in individual apoptotic cells by the in situ terminal deoxynucleotidyl transferase and nick translation assays. Cancer Res. 53:1945–1951.
   PubMed Web of Science ®Google Scholar
• Gotoh, N., Tojo A., and Shibuya M.. 1996. A novel pathway from phosphorylation of tyrosine residues 239/240 of Shc, contributing to suppress apoptosis by IL-3. EMBO J. 15:6197–6204.
   PubMedGoogle Scholar
• Iwashima, M., Takamatsu M., Yamagishi H., Hatanaka Y., Huang Y. Y., McGinty C., Yamasaki S., and Koike T.. 2002. Genetic evidence for Shc requirement in TCR-induced c-Rel nuclear translocation and IL-2 expression. Proc. Natl. Acad. Sci. USA 99:4544–4549.
   PubMedGoogle Scholar
• Kamata, H., and Hirata H.. 1999. Redox regulation of cellular signalling. Cell Signal. 11:1–14.
   PubMed Web of Science ®Google Scholar
• Koopman, G., Reutelingsperger C. P., Kuijten G. A., Keehnen R. M., Pals S. T., and van Oers M. H.. 1994. Annexin V for flow cytometric detection of phosphatidylserine expression on B cells undergoing apoptosis. Blood 84:1415–1420.
   PubMed Web of Science ®Google Scholar
• Kops, G. J. P. L., Dansen T. B., Polderman P. E., Saarloos I., Wirtz K. W., Coffer P. J., Huang T.-T., Bos J. L., Medema R. H., and Burgering B. M. T.. 2002. Forkhead transcription factor FOXO3a protects quiescent cells from oxidative stress. Nature 419:316–321.
   PubMed Web of Science ®Google Scholar
• Langlet, C., Bernard A. M., Drevot P., and He H. T.. 2000. Membrane rafts and signaling by the multichain immune recognition receptors. Curr. Opin. Immunol. 12:250–255.
   PubMed Web of Science ®Google Scholar
• Latinis, K. M., Carr L. L., Peterson E. J., Norian L. A., Eliason S. L., and Koretzky G. A.. 1997. Regulation of CD95 (Fas) ligand expression by TCR-mediated signaling events. J. Immunol. 158:4602–4611.
   PubMedGoogle Scholar
• Lord, J. D., McIntosh B. C., Greenberg P. D., and Nelson B. H.. 1998. The IL-2 receptor promotes proliferation, bcl-2 and bcl-x induction, but not cell viability through the adapter molecule Shc. J. Immunol. 161:4627–4633.
   PubMed Web of Science ®Google Scholar
• Luzi, L., Confalonieri S., Di Fiore P. P., and Pelicci P. G.. 2000. Evolution of Shc functions from nematode to human. Curr. Opin. Genet. Dev. 10:668–674.
   PubMed Web of Science ®Google Scholar
• Migliaccio, E., Giorgio M., Mele S., Pelicci G., Reboldi P., Pandolfi P. P., Lanfrancone L., and Pelicci P. G.. 1999. The p66shc adaptor protein controls oxidative stress response and life span in mammals. Nature 402:309–313.
   PubMed Web of Science ®Google Scholar
• Migliaccio, E., Mele S., Salcini A. E., Pelicci G., Lai K. M., Superti-Furga G., Pawson T., Di Fiore P. P., Lanfrancone L., and Pelicci P. G.. 1997. Opposite effects of the p52shc/p46shc and p66shc splicing isoforms on the EGF receptor-MAP kinase-fos signalling pathway. EMBO J. 6:706–716.
   Google Scholar
• Milia, E., Di Somma M. M., Baldoni F., Chiari R., Lanfrancone L., Pelicci P. G., Telford J. L., and Baldari C. T.. 1996. The amino-terminal phosphotyrosine binding domain of Shc associates with ZAP-70 and mediates TCR dependent gene activation. Oncogene 13:767–775.
   PubMedGoogle Scholar
• Naldini, A., Carney D. H., Pucci A., and Carraro F.. 2002. Human alpha-thrombin stimulates proliferation of interferon-gamma differentiated, growth-arrested U937 cells, overcoming differentiation-related changes in expression of p21CIP1/WAF1 and cyclin D1. J. Cell. Physiol. 191:290–297.
   PubMedGoogle Scholar
• Nemoto, S., and Finkel T.. 2002. Redox regulation of forkhead proteins through a p66shc-dependent signaling pathway. Science 295:2450–2452.
   PubMed Web of Science ®Google Scholar
• Okada, S., Kao A. W., Ceresa B. P., Blaikie P., Margolis B., and Pessin J. E.. 1997. The 66-kDa Shc isoform is a negative regulator of the epidermal growth factor-stimulated mitogen-activated protein kinase pathway. J. Biol. Chem. 272:28042–28049.
   PubMed Web of Science ®Google Scholar
• Pacini, S., Ulivieri C., M Di Somma M., Isacchi A., Lanfrancone L., Pelicci P. G., Telford J. L., and Baldari C. T.. 1998. Tyrosine 474 of ZAP-70 is required for association with the Shc adaptor and for T-cell antigen receptor-dependent gene activation. J. Biol. Chem. 273:20487–20493.
   PubMedGoogle Scholar
• Pelicci, G., Lanfrancone L., Grignani F. McGlade J., Cavallo F., Forni G., Nicoletti I., Grignani F., Pawson T., and Pelicci P. G.. 1992. A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction. Cell 70:93–104.
   PubMed Web of Science ®Google Scholar
• Piette, J., Piret B., Bonizzi G., Schoonbroodt S., Merville M. P., Legrand-Poels S., and Bours V.. 1997. Multiple redox regulation in NF-κB transcription factor activation. Biol. Chem. 378:1237–1245.
   PubMed Web of Science ®Google Scholar
• Plyte, S., Majolini M. B., Pacini S., Scarpini F., Bianchini C., Lanfrancone L., Pelicci P. G., and Baldari C. T.. 2000. Constitutive activation of the Ras/MAP kinase pathway and enhanced TCR signaling by targeting the Shc adaptor to membrane rafts. Oncogene 19:1529–1537.
   PubMedGoogle Scholar
• Pratt, J. C., van den Brink M. R., Igras V. E., Walk S. F., Ravichandran K. S., and Burakoff S. J.. 1999. Requirement for Shc in TCR-mediated activation of a T cell hybridoma. J. Immunol. 163:2586–2591.
   PubMedGoogle Scholar
• Ravichandran, K. S., Lee K. K., Songyang Z., Cantley L. C., Burn P., and Burakoff S. J.. 1993. Interaction of Shc with the zeta chain of the T cell receptor upon T cell activation. Science 262:902–905.
   PubMedGoogle Scholar
• Ravichandran, K. S., Lorenz U., Shoelson E., and Burakoff S. J.. 1995. Interaction of Shc with Grb2 regulates association of Grb2 with mSOS. Mol. Cell. Biol. 15:593–600.
   PubMedGoogle Scholar
• Ravichandran, K. S. 2001. Signaling via Shc family adapter proteins. Oncogene 20:6322–6330.
   PubMed Web of Science ®Google Scholar
• Rozakis-Adcock, M., McGlade J., Mbamalu G., Pelicci G., Daly R., Li W., Batzer A., Thomas S., Brugge J., Pelicci P. G., Schlessinger J., and Pawson T.. 1992. Association of the Shc and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases. Nature 360:689–692.
   PubMed Web of Science ®Google Scholar
• Trinei, M., Giorgio M., Cicalese A., Barozzi S., Ventura A., Migliaccio E., E., Milia, Padura I. M., Raker V. A., Maccarana M., Petronilli V., Minucci S., Bernardi P., Lanfrancone L., and Pelicci P. G.. 2002. A p53-p66Shc signalling pathway controls intracellular redox status, levels of oxidation-damaged DNA and oxidative stress-induced apoptosis. Oncogene 21:3872–3878.
   PubMed Web of Science ®Google Scholar
• Valensin, S., Rossi Paccani S., Ulivieri U., Mercati D., Pacini S., Patrussi L., Hirst T., Lupetti P., and Baldari C. T.. 2002. F-actin dynamics control segregation of the TCR signaling cascade to clustered lipid rafts. Eur. J. Immunol. 32:435–446.
   PubMed Web of Science ®Google Scholar
• van der Geer, P., Wiley S., Gish G. D., and Pawson T.. 1996. The Shc adaptor protein is highly phosphorylated at conserved, twin tyrosine residues (Y239/240) that mediate protein-protein interactions. Curr. Biol. 6:1435–1444.
   PubMed Web of Science ®Google Scholar
• Ventura, A., Luzi L., Pacini S., Baldari C. T., and Pelicci P. G.. 2002. The p66Shc longevity gene is silenced through epigenetic modifications of an alternative promoter. J. Biol. Chem. 277:22370–22376.
   PubMed Web of Science ®Google Scholar
• Zhang, L., Camerini V., Bender T. P., and Ravichandran K. S.. 2002. A nonredundant role for the adapter protein Shc in thymic T cell development. Nat. Immunol. 3:749–755.
   PubMedGoogle Scholar
• Zhou, M. M., Ravichandran K. S., Olejniczak E. F., Petros A. M., Meadows R. P., Sattler M., Harlan J. E., Wade W. S., Burakoff S. J., and Fesik S. W.. 1995. 1995. Structure and ligand recognition of the phosphotyrosine binding domain of Shc. Nature 378:584–592.
   PubMedGoogle Scholar