Mutations in the inter-SH2 domain of the regulatory subunit of phosphoinositide 3-kinase: effects on catalytic subunit binding and holoenzyme function

References

Agius, E., Oelgeschlager, M., Wessely, O., Kemp, C., and De Robertis, E.M. (2000). Endodermal nodal-related signals and mesoderm induction in Xenopus. Development127, 1173–1183.10.1242/dev.127.6.1173Search in Google Scholar

Cantley, L.C. (2002). The phosphoinositide 3-kinase pathway. Science296, 1655–1657.10.1126/science.296.5573.1655Search in Google Scholar

Carballada, R., Yasuo, H., and Lemaire, P. (2001). Phosphatidylinositol-3 kinase acts in parallel to the ERK MAP kinase in the FGF pathway during Xenopus mesoderm induction. Development128, 35–44.10.1242/dev.128.1.35Search in Google Scholar

Chan, T.O., Rodeck, U., Chan, A.M., Kimmelman, A.C., Rittenhouse, S.E., Panayotou, G., and Tsichlis, P.N. (2002). Small GTPases and tyrosine kinases coregulate a molecular switch in the phosphoinositide 3-kinase regulatory subunit. Cancer Cell1, 181–191.10.1016/S1535-6108(02)00033-8Search in Google Scholar

Dhand, R., Hara, K., Hiles, I., Bax, B., Gout, I., Panayotou, G., Fry, M.J., Yonezawa, K., Kasuga, M., and Waterfield, M.D. (1994). PI 3-kinase: structural and functional analysis of intersubunit interactions. EMBO J.13, 511–521.10.1002/j.1460-2075.1994.tb06289.xSearch in Google Scholar PubMed PubMed Central

Elis, W., Reth, M., and Huber, M. (2004). Functional folding of a cytoplasmic single-chain variable fragment and its use as elutable protein purification tag. Immunol. Lett.92, 185–192.10.1016/j.imlet.2003.11.027Search in Google Scholar PubMed

Fu, Z., Aronoff-Spencer, E., Wu, H., Gerfen, G.J., and Backer, J.M. (2004). The iSH2 domain of PI 3-kinase is a rigid tether for p110 and not a conformational switch. Arch. Biochem. Biophys.432, 244–251.10.1016/j.abb.2004.09.032Search in Google Scholar PubMed PubMed Central

Fukazawa, T., Miyake, S., Band, V., and Band, H. (1996). Tyrosine phosphorylation of Cbl upon epidermal growth factor (EGF) stimulation and its association with EGF receptor and downstream signaling proteins. J. Biol. Chem.271, 14554–14559.10.1074/jbc.271.24.14554Search in Google Scholar PubMed

Hill, K.M., Huang, Y., Yip, S.C., Yu, J., Segall, J.E., and Backer, J.M. (2001). N-terminal domains of the class Ia phosphoinositide 3-kinase regulatory subunit play a role in cyto-skeletal but not mitogenic signaling. J. Biol. Chem.276, 16374–16378.10.1074/jbc.M006985200Search in Google Scholar PubMed

Holt, K.H., Olson, L., Moye-Rowley, W.S., and Pessin, J.E. (1994). Phosphatidylinositol 3-kinase activation is mediated by high-affinity interactions between distinct domains within the p110 and p85 subunits. Mol. Cell. Biol.14, 42–49.Search in Google Scholar

Hu, P., Mondino, A., Skolnik, E.Y., and Schlessinger, J. (1993). Cloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p85. Mol. Cell. Biol.13, 7677–7688.Search in Google Scholar

Jimenez, C., Portela, R.A., Mellado, M., Rodriguez-Frade, J.M., Collard, J., Serrano, A., Martinez, A.C., Avila, J., and Carrera, A.C. (2000). Role of the PI3K regulatory subunit in the control of actin organization and cell migration. J. Cell. Biol.151, 249–262.10.1083/jcb.151.2.249Search in Google Scholar PubMed PubMed Central

Kang, H., Schneider, H., and Rudd, C.E. (2002). Phosphatidylinositol 3-kinase p85 adaptor function in T-cells. Co-stimulation and regulation of cytokine transcription independent of associated p110. J. Biol. Chem.277, 912–921.10.1074/jbc.M107648200Search in Google Scholar

Klippel, A., Escobedo, J.A., Hirano, M., and Williams, L.T. (1994). The interaction of small domains between the subunits of phosphatidylinositol 3-kinase determines enzyme activity. Mol. Cell. Biol.14, 2675–2685.Search in Google Scholar

Luo, J., Field, S.J., Lee, J.Y., Engelman, J.A., and Cantley, L.C. (2005). The p85 regulatory subunit of phosphoinositide 3-kinase down-regulates IRS-1 signaling via the formation of a sequestration complex. J. Cell Biol.170, 455–464.10.1083/jcb.200503088Search in Google Scholar

Nieuwkoop, P. and Faber, J. (1994). Normal Table of Xenopus laevis (New York, USA: Garland Publishing Inc.).Search in Google Scholar

Okkenhaug, K. and Vanhaesebroeck, B. (2003). PI3K in lymphocyte development, differentiation and activation. Nat. Rev. Immunol.3, 317–330.10.1038/nri1056Search in Google Scholar

Rigaut, G., Shevchenko, A., Rutz, B., Wilm, M., Mann, M., and Seraphin, B. (1999). A generic protein purification method for protein complex characterization and proteome exploration. Nat. Biotechnol.17, 1030–1032.10.1038/13732Search in Google Scholar

Rordorf-Nikolic, T., Van Horn, D.J., Chen, D., White, M.F., and Backer, J.M. (1995). Regulation of phosphatidylinositol 3′-kinase by tyrosyl phosphoproteins. Full activation requires occupancy of both SH2 domains in the 85-kDa regulatory subunit. J. Biol. Chem.270, 3662–3666.10.1074/jbc.270.8.3662Search in Google Scholar

Sive, H.L., Grainger, R.M., and Harland, R.M. (2000). Early Development of Xenopus laevis: A Laboratory Manual (New York, USA: Cold Spring Harbor Laboratory Press).Search in Google Scholar

Smith, A.J., Surviladze, Z., Gaudet, E.A., Backer, J.M., Mitchell, C.A., and Wilson, B.S. (2001). p110β and p110δ phosphatidylinositol 3-kinases up-regulate FcεRI-activated Ca²⁺ influx by enhancing inositol 1,4,5-trisphosphate production. J. Biol. Chem.276, 17213–17220.10.1074/jbc.M100417200Search in Google Scholar

Smith, J.C., Price, B.M., Green, J.B., Weigel, D., and Herrmann, B.G. (1991). Expression of a Xenopus homolog of Brachyury (T) is an immediate-early response to mesoderm induction. Cell67, 79–87.10.1016/0092-8674(91)90573-HSearch in Google Scholar

Vanhaesebroeck, B., Leevers, S.J., Ahmadi, K., Timms, J., Katso, R., Driscoll, P.C., Woscholski, R., Parker, P.J., and Waterfield, M.D. (2001). Synthesis and function of 3-phosphorylated inositol lipids. Annu. Rev. Biochem.70, 535–602.10.1146/annurev.biochem.70.1.535Search in Google Scholar PubMed

Yu, J., Wjasow, C., and Backer, J.M. (1998a). Regulation of the p85/p110α phosphatidylinositol 3′-kinase. Distinct roles for the N-terminal and C-terminal SH2 domains. J. Biol. Chem.273, 30199–30203.10.1074/jbc.273.46.30199Search in Google Scholar PubMed

Yu, J., Zhang, Y., McIlroy, J., Rordorf-Nikolic, T., Orr, G.A., and Backer, J.M. (1998b). Regulation of the p85/p110 phosphatidylinositol 3′-kinase: stabilization and inhibition of the p110α catalytic subunit by the p85 regulatory subunit. Mol. Cell. Biol.18, 1379–1387.10.1128/MCB.18.3.1379Search in Google Scholar PubMed PubMed Central

Zieger, M., Oehrl, W., Wetzker, R., Henklein, P., Nowak, G., and Kaufmann, R. (2000). Different signaling pathways are involved in CCK(B) receptor-mediated MAP kinase activation in COS-7 cells. Biol. Chem.381, 763–768.10.1515/BC.2000.097Search in Google Scholar PubMed