The T-Cell Receptor Regulates Akt (Protein Kinase B) via a Pathway Involving Rac1 and Phosphatidylinositide 3-Kinase

REFERENCES

• Ahmed, N. N., Grimes, H. L., Bellacosa, A., Chan, T. O., and Tsichlis, P. N.. 1997. Transduction of interleukin-2 antiapoptotic and proliferative signals via Akt protein kinase. Proc. Natl. Acad. Sci. USA 94:3627–3632
   PubMed Web of Science ®Google Scholar
• Alessi, D. R., Andjelkovic, M., Caudwell, B., Cron, P., Morrice, N., Cohen, P., and Hemmings, B. A.. 1996. Mechanism of activation of protein kinase B by insulin and IGF-1. EMBO J. 15:6541–6551
   PubMed Web of Science ®Google Scholar
• Arrieumerlou, C., Donnadieu, E., Brennan, P., Keryer, G., Bismuth, G., Cantrell, D. A., and Trautmann, A.. 1998. Involvement of phosphoinositides 3-kinase and rac in membrane ruffling induced by IL2 in T cells. Eur. J. Immunol. 28:1877–1885
   PubMed Web of Science ®Google Scholar
• Arudchandran, R., Brown, M. J., Peirce, M. J., Song, J. S., Zhang, J., Siraganian, R. P., Blank, U., and Rivera, J.. 2000. The src homology 2 domain of vav is required for its compartmentation to the plasma membrane and activation of c-Jun NH(2)-terminal kinase 1. J. Exp. Med. 191:47–60
   PubMedGoogle Scholar
• Bellacosa, A., Chan, T. O., Ahmed, N. N., Datta, K., Malstrom, S., Stokoe, D., McCormick, F., Feng, J., and Tsichlis, P.. 1998. Akt activation by growth factors is a multiple-step process: the role of the PH domain. Oncogene 17:313–325
   PubMed Web of Science ®Google Scholar
• Bokoch, G. M., Vlahos, C. J., Wang, Y., Knaus, U. G., and Traylor-Kaplan, A. E.. 1996. Rac GTPase interacts specifically with phosphatidylinositol 3-kinase. Biochem. J. 315:775–779
   PubMedGoogle Scholar
• Brennan, P., Babbage, J. W., Burgering, B. M. T., Groner, B., Reif, K., and Cantrell, D. A.. 1997. Phosphatidylinositol 3-kinase couples the interleukin-2 receptor to the cell cycle regulator E2F. Immunity 7:679–689
   PubMed Web of Science ®Google Scholar
• Burgering, B. M., and Coffer, P. J.. 1995. Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction. Nature 376:599–602
   PubMed Web of Science ®Google Scholar
• Cantrell, D. A.. 1996. T cell antigen receptor signal transduction pathways. Annu. Rev. Immunol. 14:259–274
   PubMed Web of Science ®Google Scholar
• Coffer, P. J., Jin, J., and Woodgett, J. R.. 1998. Protein kinase B (c-Akt): a multifunctional mediator of phosphatidylinositol 3-kinase activation. Biochem. J. 335:1–13
   PubMed Web of Science ®Google Scholar
• De Aos, I. M., Metzger, H., Exley, M., Dahl, C. E., Misra, S., Zheng, D., Varticovski, L., Terhorst, C., and Sancho, J.. 1997. Tyrosine phosphorylation of the CD3-epsilon subunit of the T cell antigen receptor mediates enhanced association with phosphatidylinositol 3-kinase in Jurkat T cells. J. Biol. Chem. 272:25310–25318
   PubMedGoogle Scholar
• Downward, J., Graves, J. D., Warne, P. H., Rayter, S., and Cantrell, D. A.. 1990. Stimulation of p21ras upon T-cell activation. Nature 346:719–723
   PubMed Web of Science ®Google Scholar
• D'souza-schorey, C., Boettner, B., and Van Aelst, L.. 1998. Rac regulates integrin-mediated spreading and increased adhesion of T lymphocytes. Mol. Cell. Biol. 18:3936–3946
   PubMed Web of Science ®Google Scholar
• Filippa, N., Sable, C. L., Filloux, C., Hemmings, B., and Van Obberghen, E.. 1999. Mechanism of protein kinase B activation by cyclic AMP-dependent protein kinase. Mol. Cell. Biol. 19:4989–5000
   PubMed Web of Science ®Google Scholar
• Génot, E., Reif, K., Beach, S., Kramer, I. M., and Cantrell, D. A.. 1998. p21ras initiates Rac-1 but not phosphatidylinositol 3-kinase/PKB mediated signaling pathways in T lymphocytes. Oncogene 17:1731–1738
   PubMedGoogle Scholar
• Génot, E., Cleverley, S., Henning, S., and Cantrell, D. A.. 1996. Multiple p21ras effector pathways regulate Nuclear Factor of Activated T cell, NFAT. EMBO J. 15:3923–3933
   PubMedGoogle Scholar
• Gold, M. R., Scheid, M. P., Santos, L., Dang-Lawson, M., Roth, R. A., Matsuuchi, L., Duronio, V., and Krebs, D. L.. 1999. The B cell antigen receptor activates the Akt (protein kinase B)/glycogen synthase kinase-3 signaling pathway via phosphatidylinositol 3-kinase. J. Immunol. 163:1894–1905
   PubMed Web of Science ®Google Scholar
• Goldsmith, M. A., Desai, D. M., Schultz, T., and Weiss, A.. 1989. Function of a heterologous muscarinic receptor in T cell antigen receptor signal transduction mutants. J. Biol. Chem. 264:17190–17197
   PubMedGoogle Scholar
• Keely, P. J., Westwick, J. K., Whitehead, I. P., Der, C. J., and Parise, L.. 1997. Cdc42 and Rac1 induce integrin-mediated cell motility and invasiveness through PI(3)K. Nature 390:632–636
   PubMed Web of Science ®Google Scholar
• Klippel, A., Kavanaugh, W. M., Pot, D., and Williams, L. T.. 1997. A specific product of phosphatidylinositol 3-kinase directly activates the protein kinase Akt through its pleckstrin homology domain. Mol. Cell. Biol. 17:338–344
   PubMed Web of Science ®Google Scholar
• Kuhne, M., Ku, G., and Weiss, A.. 1999. A guanine nucleotide exchange factor-independent function of Vav1 in transcriptional activation. J. Biol. Chem. 275:2185–2190
   Google Scholar
• Lamarche, N., Tapon, N., Stowers, L., Burbelo, P. D., Aspenstrom, P., Bridges, T., Chant, J., and Hall, A.. 1996. Rac and Cdc42 induce actin polymerization and G1 cell cycle progression independent of p65PAK and the JNK/SAPK MAPkinase cascade. Cell 87:519–529
   PubMed Web of Science ®Google Scholar
• Manser, E., Loo, T. H., Koh, C. G., Zhao, Z. S., Chen, X. Q., Tan, L., Leung, T., and Lim, L.. 1998. PAK kinases are directly coupled to the PIX family of nucleotide exchange factors. Mol. Cell 1:183–192
   PubMed Web of Science ®Google Scholar
• Nobes, C., and Hall, A.. 1995. Rho, Rac and Cdc42 GTPases regulate the assembly of multimolecular complexes associated with actin stress fibers lamellipodia and filopodia. Cell 81:53–62
   PubMed Web of Science ®Google Scholar
• Osman, N., Turner, H., Lucas, S., Reif, K., and Cantrell, D. A.. 1996. The protein interactions of the immunoglobulin receptor family tyrosine-based activation motifs present in the T cell receptor zeta subunits and the CD3 gamma, delta and epsilon chains. Eur. J. Immunol. 26:1063–1068
   PubMedGoogle Scholar
• Reif, K., Lucas, S., and Cantrell, D. A.. 1997. A negative role for phosphatidylinositol 3-kinase in T cell antigen receptor function. Curr. Biol. 7:285–293
   PubMedGoogle Scholar
• Reif, K., Nobes, K., Thomas, G., Hall, A., and Cantrell, D. A.. 1996. Phosphatidylinositol 3-kinase activates a selective subset of Rac/Rho-dependent effector pathways. Curr. Biol. 6:1445–1455
   PubMedGoogle Scholar
• Reif, K., Gout, I., Waterfield, M. D., and Cantrell, D. A.. 1993. Divergent regulation of phosphatidylinositol 3-kinase p85 alpha and p85 beta isoforms upon T cell activation. J. Biol. Chem. 268:10780–10788
   PubMedGoogle Scholar
• Ren, X. D., and Schwartz, M. A.. 1998. Regulation of inositol lipid kinases by Rho and Rac. Curr. Opin. Genet. Dev. 8:63–67
   PubMed Web of Science ®Google Scholar
• Ridley, A. J., Paterson, H. F., Johneson, C. L., Dieckman, D., and Hall, A.. 1992. The small GTP-binding protein Rac regulates growth factor induced membrane ruffling. Cell 70:401–410
   PubMed Web of Science ®Google Scholar
• Rodriguez-Viciana, P., Warne, P., Khwaja, A., Marte, M. M., Pappin, D., Das, P., Waterfield, P. M., Ridley, A., and Downward, J.. 1997. Role of phosphoinositide 3-OH kinase in cell transformation and control of the actin cytoskeleton. Cell 89:457–467
   PubMed Web of Science ®Google Scholar
• Rodriguez-Viciana, P., Warne, P. H., Dhand, R., Vanhaesebroeck, B., Gout, I., Fry, M. J., Waterfield, M. D., and Downward, J.. 1994. Phosphatidylinositol-3-OH kinase as a direct target of Ras. Nature 370:527–532
   PubMed Web of Science ®Google Scholar
• Rodriguez-Viciana, P., Warne, P. H., Vanhaesebroeck, B., Waterfield, M. D., and Downward, J.. 1996. Activation of phosphoinositide 3-kinase by interaction with Ras and by point mutation. EMBO J. 15:2442–2451
   PubMed Web of Science ®Google Scholar
• Stokoe, D. L., Stephens, R., Copeland, T., Gaffney, P. R., Reese, C. B., Painter, G. F., Holmes, A. B., McCormick, F., and Hawkins, P. T.. 1997. Dual role of phosphatidylinositol-3,4,5-trisphosphate in the activation of protein kinase B. Science 277:567–570
   PubMed Web of Science ®Google Scholar
• Tolias, K. F., Cantley, L. C., and Carpenter, C. L.. 1995. Rho family GTPases bind to phosphoinositide kinases. J. Biol. Chem. 270:17656–17659
   PubMedGoogle Scholar
• Van Aelst, L., and D'souza-schorey, C.. 1997. Rho GTPases and signaling networks. Genes Dev. 11:2295–2322
   PubMed Web of Science ®Google Scholar
• Vanhaesebroeck, B., Jones, G., Alen, W. E., Zicha, D., Hooshmand-Rad, R., Sawyer, T., Wells, C., Waterfield, M., and Ridley, A.. 1999. Distinct PI3K mediate mitogenic signalling and cell migration in macrophages. Nat. Cell. Biol. 1:69–72
   PubMed Web of Science ®Google Scholar
• Van Weering, D. H., De Rooij, J., Marte, B. M., Downward, J., Bos, J. L., and Burgering, B. M.. 1998. Protein kinase B activation and lamellipodium formation are independent phosphoinositide 3-kinase-mediated events differentially regulated by endogenous Ras. Mol. Cell. Biol. 18:1802–1811
   PubMedGoogle Scholar
• Welch, H., Eguinoa, A., Stephens, L. R., and Hawkins, P. T.. 1998. Protein kinase B and Rac are activated in parallel within a phosphatidylinositide 3OH-kinase-controlled signaling pathway. J. Biol. Chem. 273:11248–11256
   PubMedGoogle Scholar
• Westwick, J. K., Lambert, Q. T., Clark, G. J., Symons, M., Van Aelst, L., Pestell, R. G., and Der, C. J.. 1997. Rac regulation of transformation, gene expression, and actin organization by multiple, PAK-independent pathways. Mol. Cell. Biol. 17:1324–1335
   PubMed Web of Science ®Google Scholar
• Whitehead, J. P., Clark, S. F., Urso, B., and James, D. E.. 2000. Signalling through the insulin receptor. Curr. Opin. Cell Biol. 12:222–228
   PubMed Web of Science ®Google Scholar
• Williams, M., Simon, J., Arthur, C., Balendran, A., Van der Kaay, J., Poli, A., Coher, P., and Alessi, D.. 2000. The role of 3-phosphoinositide-dependent protein kinase1 in activating AGC kinases defined in embryonic stem cells. Curr. Biol. 10:439–448
   PubMed Web of Science ®Google Scholar
• Wymann, M. P., and Pirola, L.. 1998. Structure and function of phosphoinositide 3-kinases. Biochim. Biophys. Acta 1436:127–150
   PubMed Web of Science ®Google Scholar
• Yablonski, D., Kane, L. P., Qian, D., and Weiss, A.. 1998. A Nck-Pak1 signalling module is required for T cell receptor mediated activation of NFAT, but not of JNK. EMBO J. 17:5647–5657
   PubMedGoogle Scholar
• Yano, S., Tokumitsu, H., and Soderling, T. R.. 1998. Calcium promotes cell survival through CaM-K kinase activation of the protein-kinase-B pathway. Nature 396:584–587
   PubMed Web of Science ®Google Scholar
• Zhang, W., Sloan-Lancaster, J., Kitchen, J., Trible, R. P., and Samelson, L. E.. 1998. LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation. Cell 92:83–92
   PubMed Web of Science ®Google Scholar
• Zheng, Y., Bagrodia, S., and Cerione, R. A.. 1994. Activation of phosphoinositide 3-kinase activity by Cdc42HS binding to p85. J. Biol. Chem. 269:18727–18730
   PubMed Web of Science ®Google Scholar