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Gene Review

Pi3K92E  -  CG4141 gene product from transcript CG4141-RB

Drosophila melanogaster

Synonyms: CG4141, DP110, Dmel\CG4141, Dmp110, Dp110, ...
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Disease relevance of Pi3K92E


High impact information on Pi3K92E

  • This involves TSC/TOR signaling in the fat body, and a remote inhibition of organismal growth via local repression of PI3-kinase signaling in peripheral tissues [6].
  • Here, we present evidence indicating that Ras(V12) promotes cell growth and G(1)/S progression by increasing dMyc protein levels and activating dPI3K signaling, and that it does so via separate effector pathways [7].
  • These results suggest that Ras may only affect PI3K signaling when mutationally activated, such as in Ras(V12)-transformed cells, and provide a basis for understanding the synergy between Ras and other growth-promoting oncogenes in cancer [7].
  • We demonstrate that DPTEN modulates tissue mass by acting antagonistically to the Drosophila Class I phosphatidylinositol 3-kinase, Dp110, and its upstream activator Chico, an insulin receptor substrate homolog [8].
  • It acts in opposition to Dp110 to control cell number and growth, while coordinately influencing events at the cell periphery via its effects on the actin cytoskeleton [8].

Biological context of Pi3K92E

  • The inhibition of Dp110 activity reduces the rate of increase in cell number in the imaginal discs, suggesting that Dp110 normally promotes cell division and/or cell survival [9].
  • In addition, modulating Dp110 activity increases or reduces cell size in the developing imaginal disc, and does so throughout the cell cycle [9].
  • Unlike direct manipulation of cell-cycle progression, manipulation of Dp110 activity in one compartment of the disc influences the size of that compartment and the size of the disc as a whole [9].
  • RESULTS: Null mutations in Dp110 and p60 were generated and used to demonstrate that they are essential genes that are autonomously required for imaginal disc cells to achieve their normal adult size [9].
  • In mammalian cells, insulin-induced PI3K (phosphoinositide 3-kinase) activation, generates the lipid second messenger PtdIns(3,4,5) P (3), which is thought to play a key role in triggering the activation of S6K [10].

Anatomical context of Pi3K92E

  • We report here the cloning of a novel PI 3-kinase, p170, from cDNA of insulin-sensitive mouse 3T3-L1 adipocytes [11].
  • In this study, we show that elevated signaling through PI3K and Akt can prevent developmentally controlled death in the salivary glands of the fruit fly [12].
  • The P3k oncoprotein [homolog of the catalytic subunit p110alpha of class 1A phosphoinositide 3-kinase (PI3K)] and its downstream effector Akt induce oncogenic transformation in cultures of chicken embryo fibroblasts (CEF) [13].
  • Furthermore, co-purification of the catalytic subunit of PI3K (p110) was achieved from lysates of co-transfected S2 cells as well as RBL-2H3 mast cells stably expressing isc-p85alpha [14].
  • Together, these data suggest that p120 is an important positive modulator of adhesion but that it is not an essential core component of adherens junctions [15].

Associations of Pi3K92E with chemical compounds

  • The insulin-induced activations of dERK and dAKT were blocked by LY294002, dPTEN, and by an AKT inhibitor, indicating involvement of dPI3K and dAKT in the insulin-induced dERK and dAKT activations [16].
  • Thus, Dp110 integrates inputs from its phosphotyrosine-binding adaptor and Ras to achieve maximal PI(3)K signalling in specific biological situations [17].
  • PI3K inhibitors or the proteasome inhibitor lactacystin interfere with this process [13].
  • We also observed impairment of PI3K/Akt signaling in the fly parkin model of PD, hinting at a common molecular event in the pathogenesis of PD [18].
  • Sequence analysis suggests that HsC2-PI3K is a second distinct mammalian member of the C2 domain-containing PI 3-kinase family [19].

Other interactions of Pi3K92E

  • Our results indicate that Dp110 and p60 signalling can affect growth in multiple ways, which has important implications for the function of signalling through class I(A) PI 3-kinases [9].
  • Studies in Drosophila have identified an evolutionarily conserved signaling pathway that regulates organismal size and that includes the Drosophila insulin receptor substrate homolog Chico, the lipid kinase PI(3)K (Dp110), DAkt1/dPKB, and dS6K [20].

Analytical, diagnostic and therapeutic context of Pi3K92E


  1. Phosphatidylinositol 3-kinase and Akt nonautonomously promote perineurial glial growth in Drosophila peripheral nerves. Lavery, W., Hall, V., Yager, J.C., Rottgers, A., Wells, M.C., Stern, M. J. Neurosci. (2007) [Pubmed]
  2. The cytohesin Steppke is essential for insulin signalling in Drosophila. Fuss, B., Becker, T., Zinke, I., Hoch, M. Nature (2006) [Pubmed]
  3. Re-evaluating AKT regulation: role of TOR complex 2 in tissue growth. Hietakangas, V., Cohen, S.M. Genes Dev. (2007) [Pubmed]
  4. Control of growth and differentiation by Drosophila RasGAP, a homolog of p120 Ras-GTPase-activating protein. Feldmann, P., Eicher, E.N., Leevers, S.J., Hafen, E., Hughes, D.A. Mol. Cell. Biol. (1999) [Pubmed]
  5. TRB3 is a PI 3-kinase dependent indicator for nutrient starvation. Schwarzer, R., Dames, S., Tondera, D., Klippel, A., Kaufmann, J. Cell. Signal. (2006) [Pubmed]
  6. A nutrient sensor mechanism controls Drosophila growth. Colombani, J., Raisin, S., Pantalacci, S., Radimerski, T., Montagne, J., Léopold, P. Cell (2003) [Pubmed]
  7. Interactions between Ras1, dMyc, and dPI3K signaling in the developing Drosophila wing. Prober, D.A., Edgar, B.A. Genes Dev. (2002) [Pubmed]
  8. Drosophila tumor suppressor PTEN controls cell size and number by antagonizing the Chico/PI3-kinase signaling pathway. Goberdhan, D.C., Paricio, N., Goodman, E.C., Mlodzik, M., Wilson, C. Genes Dev. (1999) [Pubmed]
  9. Regulation of imaginal disc cell size, cell number and organ size by Drosophila class I(A) phosphoinositide 3-kinase and its adaptor. Weinkove, D., Neufeld, T.P., Twardzik, T., Waterfield, M.D., Leevers, S.J. Curr. Biol. (1999) [Pubmed]
  10. Insulin-induced Drosophila S6 kinase activation requires phosphoinositide 3-kinase and protein kinase B. Lizcano, J.M., Alrubaie, S., Kieloch, A., Deak, M., Leevers, S.J., Alessi, D.R. Biochem. J. (2003) [Pubmed]
  11. Mouse p170 is a novel phosphatidylinositol 3-kinase containing a C2 domain. Virbasius, J.V., Guilherme, A., Czech, M.P. J. Biol. Chem. (1996) [Pubmed]
  12. FOXO-independent suppression of programmed cell death by the PI3K/Akt signaling pathway in Drosophila. Liu, Y., Lehmann, M. Dev. Genes Evol. (2006) [Pubmed]
  13. Proteasomal degradation of the FoxO1 transcriptional regulator in cells transformed by the P3k and Akt oncoproteins. Aoki, M., Jiang, H., Vogt, P.K. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  14. Functional folding of a cytoplasmic single-chain variable fragment and its use as elutable protein purification tag. Elis, W., Reth, M., Huber, M. Immunol. Lett. (2004) [Pubmed]
  15. Drosophila p120catenin plays a supporting role in cell adhesion but is not an essential adherens junction component. Myster, S.H., Cavallo, R., Anderson, C.T., Fox, D.T., Peifer, M. J. Cell Biol. (2003) [Pubmed]
  16. Drosophila PI3 kinase and Akt involved in insulin-stimulated proliferation and ERK pathway activation in Schneider cells. Kim, S.E., Cho, J.Y., Kim, K.S., Lee, S.J., Lee, K.H., Choi, K.Y. Cell. Signal. (2004) [Pubmed]
  17. Input from Ras is required for maximal PI(3)K signalling in Drosophila. Orme, M.H., Alrubaie, S., Bradley, G.L., Walker, C.D., Leevers, S.J. Nat. Cell Biol. (2006) [Pubmed]
  18. Inactivation of Drosophila DJ-1 leads to impairments of oxidative stress response and phosphatidylinositol 3-kinase/Akt signaling. Yang, Y., Gehrke, S., Haque, M.E., Imai, Y., Kosek, J., Yang, L., Beal, M.F., Nishimura, I., Wakamatsu, K., Ito, S., Takahashi, R., Lu, B. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  19. Identification and cDNA cloning of a novel mammalian C2 domain-containing phosphoinositide 3-kinase, HsC2-PI3K. Brown, R.A., Ho, L.K., Weber-Hall, S.J., Shipley, J.M., Fry, M.J. Biochem. Biophys. Res. Commun. (1997) [Pubmed]
  20. An evolutionarily conserved function of the Drosophila insulin receptor and insulin-like peptides in growth control. Brogiolo, W., Stocker, H., Ikeya, T., Rintelen, F., Fernandez, R., Hafen, E. Curr. Biol. (2001) [Pubmed]
  21. Ras activity in the Drosophila prothoracic gland regulates body size and developmental rate via ecdysone release. Caldwell, P.E., Walkiewicz, M., Stern, M. Curr. Biol. (2005) [Pubmed]
  22. Effects of 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one on synaptic vesicle cycling at the frog neuromuscular junction. Rizzoli, S.O., Betz, W.J. J. Neurosci. (2002) [Pubmed]
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