Inhibition of the Jun N-Terminal Protein Kinase Pathway by SHIP-1, a Lipid Phosphatase That Interacts with the Adaptor Molecule Dok-3

REFERENCE

• Abraham, N., Miceli M. C., Parnes J. R., and Veillette A.. 1991. Enhancement of T-cell responsiveness by the lymphocyte-specific tyrosine protein kinase p56lck. Nature 350:62–66.
   PubMedGoogle Scholar
• Aman, M. J., Lamkin T. D., Okada H., Kurosaki T., and Ravichandran K. S.. 1998. The inositol phosphatase SHIP inhibits Akt/PKB activation in B cells. J. Biol. Chem. 273:33922–33928.
   PubMed Web of Science ®Google Scholar
• Benschop, R. J., and Cambier J. C.. 1999. B cell development: signal transduction by antigen receptors and their surrogates. Curr. Opin. Immunol. 11:143–151.
   PubMed Web of Science ®Google Scholar
• Bolland, S., Pearse R. N., Kurosaki T., and Ravetch J. V.. 1998. SHIP modulates immune receptor responses by regulating membrane association of Btk. Immunity 8:509–516.
   PubMed Web of Science ®Google Scholar
• Brauweiler, A., Tamir I., Dal Porto J., Benschop R. J., Helgason C. D., Humphries R. K., Freed J. H., and Cambier J. C.. 2000. Differential regulation of B cell development, activation, and death by the src homology 2 domain-containing 5′ inositol phosphatase (SHIP). J. Exp. Med. 191:1545–1554.
   PubMed Web of Science ®Google Scholar
• Brauweiler, A. M., Tamir I., and Cambier J. C.. 2000. Bilevel control of B-cell activation by the inositol 5-phosphatase SHIP. Immunol. Rev. 176:69–74.
   PubMedGoogle Scholar
• Cambier, J. C. 1995. Antigen and Fc receptor signaling. The awesome power of the immunoreceptor tyrosine-based activation motif (ITAM). J. Immunol. 155:3281–3285.
   PubMed Web of Science ®Google Scholar
• Cambier, J. C., Pleiman C. M., and Clark M. R.. 1994. Signal transduction by the B cell antigen receptor and its coreceptors. Annu. Rev. Immunol. 12:457–486.
   PubMed Web of Science ®Google Scholar
• Chow, L. M., Fournel M., Davidson D., and Veillette A.. 1993. Negative regulation of T-cell receptor signalling by tyrosine protein kinase p50csk. Nature 365:156–160.
   PubMed Web of Science ®Google Scholar
• Cong, F., Yuan B., and Goff S. P.. 1999. Characterization of a novel member of the DOK family that binds and modulates Abl signaling. Mol. Cell. Biol. 19:8314–8325.
   PubMedGoogle Scholar
• Coso, O. A., Chiariello M., Yu J. C., Teramoto H., Crespo P., Xu N., Miki T., and Gutkind J. S.. 1995. The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway. Cell 81:1137–1146.
   PubMed Web of Science ®Google Scholar
• Cox, D., Dale B. M., Kashiwada M., Helgason C. D., and Greenberg S.. 2000. A regulatory role for Src homology 2 domain-containing inositol 5′-phosphatase (SHIP) in phagocytosis mediated by Fc γ receptors and complement receptor 3 (αMβ2; CD11b/CD18). J. Exp. Med. 193:61–72.
   Google Scholar
• Damen, J. E., Liu L., Rosten P., Humphries R. K., Jefferson A. B., Majerus P. W., and Krystal G.. 1996. The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-triphosphate 5-phosphatase. Proc. Natl. Acad. Sci. USA 93:1689–1693.
   PubMed Web of Science ®Google Scholar
• Davidson, D., Chow L. M., Fournel M., and Veillette A.. 1992. Differential regulation of T cell antigen responsiveness by isoforms of the src-related tyrosine protein kinase p59fyn. J. Exp. Med. 175:1483–1492.
   PubMedGoogle Scholar
• Davis, R. J. 2000. Signal transduction by the JNK group of MAP kinases. Cell 103:239–252.
   PubMed Web of Science ®Google Scholar
• Fournel, M., Davidson D., Weil R., and Veillette A.. 1996. Association of tyrosine protein kinase Zap-70 with the protooncogene product p120c-cbl in T lymphocytes. J. Exp. Med. 183:301–306.
   PubMedGoogle Scholar
• Gugasyan, R., Quilici C., I S. T., Grail D., Verhagen A. M., Roberts A., Kitamura T., Dunn A. R., and Lock P.. 2002. Dok-related protein negatively regulates T cell development via its RasGTPase-activating protein and Nck docking sites. J. Cell Biol. 158:115–125.
   PubMed Web of Science ®Google Scholar
• Hashimoto, A., Okada H., Jiang A., Kurosaki M., Greenberg S., Clark E. A., and Kurosaki T.. 1998. Involvement of guanosine triphosphatases and phospholipase C-γ2 in extracellular signal-regulated kinase, c-Jun NH2-terminal kinase, and p38 mitogen-activated protein kinase activation by the B cell antigen receptor. J. Exp. Med. 188:1287–1295.
   PubMed Web of Science ®Google Scholar
• Healy, J. I., Dolmetsch R. E., Timmerman L. A., Cyster J. G., Thomas M. L., Crabtree G. R., Lewis R. S., and Goodnow C. C.. 1997. Different nuclear signals are activated by the B cell receptor during positive versus negative signaling. Immunity 6:419–428.
   PubMed Web of Science ®Google Scholar
• Helgason, C. D., Kalberer C. P., Damen J. E., Chappel S. M., Pineault N., Krystal G., and Humphries R. K.. 2000. A dual role for Src homology 2 domain-containing inositol-5-phosphatase (SHIP) in immunity: aberrant development and enhanced function of B lymphocytes in SHIP−/− mice. J. Exp. Med. 191:781–794.
   PubMedGoogle Scholar
• Ishiai, M., Kurosaki M., Pappu R., Okawa K., Ronko I., Fu C., Shibata M., Iwamatsu A., Chan A. C., and Kurosaki T.. 1999. BLNK required for coupling Syk to PLCγ2 and Rac1-JNK in B cells. Immunity 10:117–125.
   PubMed Web of Science ®Google Scholar
• Jacob, A., Cooney D., Tridandapani S., Kelley T., and Coggeshall K. M.. 1999. FcγRIIb modulation of surface immunoglobulin-induced Akt activation in murine B cells. J. Biol. Chem. 274:13704–13710.
   PubMed Web of Science ®Google Scholar
• Johnson, G. L., and Lapadat R.. 2002. Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases. Science 298:1911–1912.
   PubMed Web of Science ®Google Scholar
• Krystal, G. 2000. Lipid phosphatases in the immune system. Semin. Immunol. 12:397–403.
   PubMed Web of Science ®Google Scholar
• Kurosaki, T. 2000. Functional dissection of BCR signaling pathways. Curr. Opin. Immunol. 12:276–281.
   PubMedGoogle Scholar
• Lemay, S., Davidson D., Latour S., and Veillette A.. 2000. Dok-3, a novel adapter molecule involved in the negative regulation of immunoreceptor signaling. Mol. Cell. Biol. 20:2743–2754.
   PubMed Web of Science ®Google Scholar
• Liu, Q., Oliveira-Dos Santos A. J., Mariathasan S., Bouchard D., Jones J., Sarao R., Kozieradzki I., Ohashi P. S., Penninger J. M., and Dumont D. J.. 1998. The inositol polyphosphate 5-phosphatase Ship is a crucial negative regulator of B cell antigen receptor signaling. J. Exp. Med. 188:1333–1342.
   PubMed Web of Science ®Google Scholar
• Livingstone, C., Patel G., and Jones N.. 1995. ATF-2 contains a phosphorylation-dependent transcriptional activation domain. EMBO J. 14:1785–1797.
   PubMed Web of Science ®Google Scholar
• Muta, T., Kurosaki T., Misulovin Z., Sanchez M., Nussenzweig M. C., and Ravetch J. V.. 1994. A 13-amino-acid motif in the cytoplasmic domain of FcγRIIB modulates B-cell receptor signalling. Nature 368:70–73.
   PubMed Web of Science ®Google Scholar
• Nemorin, J. G., Laporte P., Berube G., and Duplay P.. 2001. p62dok negatively regulates CD2 signaling in Jurkat cells. J. Immunol. 166:4408–4415.
   PubMedGoogle Scholar
• Ono, M., Bolland S., Tempst P., and Ravetch J. V.. 1996. Role of the inositol phosphatase SHIP in negative regulation of the immune system by the receptor FcγRIIB. Nature 383:263–266.
   PubMed Web of Science ®Google Scholar
• Ono, M., Okada H., Bolland S., Yanagi S., Kurosaki T., and Ravetch J. V.. 1997. Deletion of SHIP or SHP-1 reveals two distinct pathways for inhibitory signaling. Cell 90:293–301.
   PubMed Web of Science ®Google Scholar
• Peri, K. G., Gervais F. G., Weil R., Davidson D., Gish G. D., and Veillette A.. 1993. Interactions of the SH2 domain of lymphocyte-specific tyrosine protein kinase p56lck with phosphotyrosine-containing proteins. Oncogene 8:2765–2772.
   PubMedGoogle Scholar
• Ravetch, J. V., and Lanier L. L.. 2000. Immune inhibitory receptors. Science 290:84–89.
   PubMed Web of Science ®Google Scholar
• Reimold, A. M., Kim J., Finberg R., and Glimcher L. H.. 2001. Decreased immediate inflammatory gene induction in activating transcription factor-2 mutant mice. Int. Immunol. 13:241–248.
   PubMed Web of Science ®Google Scholar
• Reth, M., and Wienands J.. 1997. Initiation and processing of signals from the B cell antigen receptor. Annu. Rev. Immunol. 15:453–479.
   PubMed Web of Science ®Google Scholar
• Rohrschneider, L. R., Fuller J. F., Wolf I., Liu Y., and Lucas D. M.. 2000. Structure, function, and biology of SHIP proteins. Genes Dev. 14:505–520.
   PubMed Web of Science ®Google Scholar
• Sabapathy, K., Hu Y., Kallunki T., Schreiber M., David J. P., Jochum W., Wagner E. F., and Karin M.. 1999. JNK2 is required for efficient T-cell activation and apoptosis but not for normal lymphocyte development. Curr. Biol. 9:116–125.
   PubMed Web of Science ®Google Scholar
• Scharenberg, A. M., El-Hillal O., Fruman D. A., Beitz L. O., Li Z., Lin S., Gout I., Cantley L. C., Rawlings D. J., and Kinet J. P.. 1998. Phosphatidylinositol-3,4,5-trisphosphate (PtdIns-3,4,5-P3)/Tec kinase-dependent calcium signaling pathway: a target for SHIP-mediated inhibitory signals. EMBO J. 17:1961–1972.
   PubMedGoogle Scholar
• Suzu, S., Tanaka-Douzono M., Nomaguchi K., Yamada M., Hayasawa H., Kimura F., and Motoyoshi K.. 2000. p56(dok-2) as a cytokine-inducible inhibitor of cell proliferation and signal transduction. EMBO J. 19:5114–5122.
   PubMedGoogle Scholar
• Tamir, I., Stolpa J. C., Helgason C. D., Nakamura K., Bruhns P., Daeron M., and Cambier J. C.. 2000. The RasGAP-binding protein p62dok is a mediator of inhibitory FcγRIIB signals in B cells. Immunity 12:347–358.
   PubMed Web of Science ®Google Scholar
• Tsai, E. Y., Falvo J. V., Tsytsykova A. V., Barczak A. K., Reimold A. M., Glimcher L. H., Fenton M. J., Gordon D. C., Dunn I. F., and Goldfeld A. E.. 2000. A lipopolysaccharide-specific enhancer complex involving Ets, Elk-1, Sp1, and CREB binding protein and p300 is recruited to the tumor necrosis factor alpha promoter in vivo. Mol. Cell. Biol. 20:6084–6094.
   PubMed Web of Science ®Google Scholar
• Tsai, E. Y., Yie J., Thanos D., and Goldfeld A. E.. 1996. Cell-type-specific regulation of the human tumor necrosis factor alpha gene in B cells and T cells by NFATp and ATF-2/JUN. Mol. Cell. Biol. 16:5232–5244.
   PubMed Web of Science ®Google Scholar
• Veillette, A., Bookman M. A., Horak E. M., and Bolen J. B.. 1988. The CD4 and CD8 T cell surface antigens are associated with the internal membrane tyrosine-protein kinase p56lck. Cell 55:301–308.
   PubMed Web of Science ®Google Scholar
• Veillette, A., Latour S., and Davidson D.. 2002. Negative regulation of immunoreceptor signaling. Annu. Rev. Immunol. 20:669–707.
   PubMed Web of Science ®Google Scholar
• Yang, D. D., Conze D., Whitmarsh A. J., Barrett T., Davis R. J., Rincon M., and Flavell R. A.. 1998. Differentiation of CD4+ T cells to Th1 cells requires MAP kinase JNK2. Immunity 9:575–585.
   PubMed Web of Science ®Google Scholar