메뉴 건너뛰기




Volumn 31, Issue , 2013, Pages 675-704

Signaling by the phosphoinositide 3-kinase family in immune cells

Author keywords

Akt; Autophagy; Foxo; MTOR; PI3K; Signaling

Indexed keywords

GUANOSINE TRIPHOSPHATASE; MYOTUBULARIN; PHOSPHATASE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PROTEIN; PROTEIN INPP4; PROTEIN KINASE B; PROTEIN P110; PROTEIN P110ALPHA; PROTEIN P110BETA; PROTEIN P110DELTA; PROTEIN SHIP; PROTEIN TYROSINE KINASE; TEC KINASE; TRANSCRIPTION FACTOR FOXO; UNCLASSIFIED DRUG;

EID: 84875528574     PISSN: 07320582     EISSN: 15453278     Source Type: Book Series    
DOI: 10.1146/annurev-immunol-032712-095946     Document Type: Article
Times cited : (343)

References (239)
  • 2
    • 33746257209 scopus 로고    scopus 로고
    • The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism
    • Engelman JA, Luo J, Cantley LC. 2006. The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism. Nat. Rev. Genet. 7:606-19
    • (2006) Nat. Rev. Genet. , vol.7 , pp. 606-619
    • Engelman, J.A.1    Luo, J.2    Cantley, L.C.3
  • 5
    • 39749141485 scopus 로고    scopus 로고
    • The regulation and function of class III PI3Ks: Novel roles for Vps34
    • Backer JM. 2008. The regulation and function of class III PI3Ks: novel roles for Vps34. Biochem. J. 410:1-17
    • (2008) Biochem. J. , vol.410 , pp. 1-17
    • Backer, J.M.1
  • 6
    • 50249084987 scopus 로고    scopus 로고
    • Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum
    • Axe EL, Walker SA, ManifavaM, Chandra P, Roderick HL, et al. 2008. Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum. J. Cell Biol. 182:685-701
    • (2008) J. Cell Biol. , vol.182 , pp. 685-701
    • Axe, E.L.1    Walker, S.A.2    Manifava, M.3    Chandra, P.4    Roderick, H.L.5
  • 7
    • 0035899869 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-phosphate is generated in phagosomal membranes
    • Ellson CD, AndersonKE, Morgan G, Chilvers ER, Lipp P, et al. 2001. Phosphatidylinositol 3-phosphate is generated in phagosomal membranes. Curr. Biol. 11:1631-35
    • (2001) Curr. Biol. , vol.11 , pp. 1631-1635
    • Ellson, C.D.1    Anderson, K.E.2    Morgan, G.3    Chilvers, E.R.4    Lipp, P.5
  • 8
    • 0035494493 scopus 로고    scopus 로고
    • Distinct roles of class i and class III phosphatidylinositol 3-kinases in phagosome formation and maturation
    • Vieira O, Botelho R, Rameh L, Brachmann S, Matsuo T, et al. 2001. Distinct roles of class I and class III phosphatidylinositol 3-kinases in phagosome formation and maturation. J. Cell Biol. 155:19-25
    • (2001) J. Cell Biol. , vol.155 , pp. 19-25
    • Vieira, O.1    Botelho, R.2    Rameh, L.3    Brachmann, S.4    Matsuo, T.5
  • 10
    • 0027905021 scopus 로고
    • Phosphatidylinositol 3-kinase encoded by yeast VPS34 gene essential for protein sorting
    • Schu PV, Takegawa K, Fry MJ, Stack JH, Waterfield MD, et al. 1993. Phosphatidylinositol 3-kinase encoded by yeast VPS34 gene essential for protein sorting. Science 260:88-91
    • (1993) Science , vol.260 , pp. 88-91
    • Schu, P.V.1    Takegawa, K.2    Fry, M.J.3    Stack, J.H.4    Waterfield, M.D.5
  • 12
    • 0035809160 scopus 로고    scopus 로고
    • Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase y sorting in Saccharomyces cerevisiae
    • Kihara A, Noda T, Ishihara N, Ohsumi Y. 2001. Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase Y sorting in Saccharomyces cerevisiae. J. Cell Biol. 152:519-30
    • (2001) J. Cell Biol. , vol.152 , pp. 519-530
    • Kihara, A.1    Noda, T.2    Ishihara, N.3    Ohsumi, Y.4
  • 13
    • 0027256130 scopus 로고
    • A membrane-associated complex containing the Vps15 protein kinase and the Vps34 PI 3-kinase is essential for protein sorting to the yeast lysosome-like vacuole
    • Stack JH, Herman PK, Schu PV, Emr SD. 1993. A membrane-associated complex containing the Vps15 protein kinase and the Vps34 PI 3-kinase is essential for protein sorting to the yeast lysosome-like vacuole. EMBO J. 12:2195-204
    • (1993) EMBO J. , vol.12 , pp. 2195-2204
    • Stack, J.H.1    Herman, P.K.2    Schu, P.V.3    Emr, S.D.4
  • 14
    • 84856275868 scopus 로고    scopus 로고
    • PtdIns 3-kinase orchestrates autophagosome formation in yeast
    • Obara K, Ohsumi Y. 2011. PtdIns 3-kinase orchestrates autophagosome formation in yeast. J. Lipids 2011:498768
    • (2011) J. Lipids , vol.2011 , pp. 498768
    • Obara, K.1    Ohsumi, Y.2
  • 15
    • 26444575415 scopus 로고    scopus 로고
    • Amino acids mediate mTOR/raptor signaling through activation of class 3 phosphatidylinositol 3OH-kinase
    • Nobukuni T, JoaquinM, Roccio M, Dann SG, Kim SY, et al. 2005. Amino acids mediate mTOR/raptor signaling through activation of class 3 phosphatidylinositol 3OH-kinase. Proc. Natl. Acad. Sci. USA 102:14238-43
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 14238-14243
    • Nobukuni, T.1    Joaquin, M.2    Roccio, M.3    Dann, S.G.4    Kim, S.Y.5
  • 16
    • 84863116629 scopus 로고    scopus 로고
    • Class III PI3K Vps34 plays an essential role in autophagy and in heart and liver function
    • Jaber N, Dou Z, Chen JS, Catanzaro J, Jiang YP, et al. 2012. Class III PI3K Vps34 plays an essential role in autophagy and in heart and liver function. Proc. Natl. Acad. Sci. USA 109:2003-8
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 2003-2008
    • Jaber, N.1    Dou, Z.2    Chen, J.S.3    Catanzaro, J.4    Jiang, Y.P.5
  • 17
    • 77950212231 scopus 로고    scopus 로고
    • Shaping development of autophagy inhibitors with the structure of the lipid kinase Vps34
    • Miller S, Tavshanjian B, Oleksy A, Perisic O, Houseman BT, et al. 2010. Shaping development of autophagy inhibitors with the structure of the lipid kinase Vps34. Science 327:1638-42
    • (2010) Science , vol.327 , pp. 1638-1642
    • Miller, S.1    Tavshanjian, B.2    Oleksy, A.3    Perisic, O.4    Houseman, B.T.5
  • 18
    • 79551528853 scopus 로고    scopus 로고
    • The mammalian class 3 PI3K (PIK3C3) is required for early embryogenesis and cell proliferation
    • Zhou X, Takatoh J, Wang F. 2011. The mammalian class 3 PI3K (PIK3C3) is required for early embryogenesis and cell proliferation. PLoS ONE 6:e16358
    • (2011) PLoS ONE , vol.6
    • Zhou, X.1    Takatoh, J.2    Wang, F.3
  • 19
    • 84861889657 scopus 로고    scopus 로고
    • Canonical autophagy dependent on the class III phosphoinositide-3 kinase Vps34 is required for naive T-cell homeostasis
    • Willinger T, Flavell RA. 2012. Canonical autophagy dependent on the class III phosphoinositide-3 kinase Vps34 is required for naive T-cell homeostasis. Proc. Natl. Acad. Sci. USA 109:8670-75
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 8670-8675
    • Willinger, T.1    Flavell, R.A.2
  • 20
    • 81455154986 scopus 로고    scopus 로고
    • The class III kinase Vps34 promotes T lymphocyte survival through regulating IL-7Rαsurface expression
    • McLeod IX, Zhou X, LiQJ, Wang F, He YW. 2011. The class III kinase Vps34 promotes T lymphocyte survival through regulating IL-7Rαsurface expression. J. Immunol. 187:5051-61
    • (2011) J. Immunol. , vol.187 , pp. 5051-5061
    • McLeod, I.X.1    Zhou, X.2    Liqj Wang, F.3    He, Y.W.4
  • 21
    • 78649757606 scopus 로고    scopus 로고
    • PtdIns3P and Rac direct the assembly of the NADPH oxidase on a novel, pre-phagosomal compartment during FcR-mediated phagocytosis in primary mouse neutrophils
    • Anderson KE, Chessa TA, Davidson K, Henderson RB, Walker S, et al. 2010. PtdIns3P and Rac direct the assembly of the NADPH oxidase on a novel, pre-phagosomal compartment during FcR-mediated phagocytosis in primary mouse neutrophils. Blood 116:4978-89
    • (2010) Blood , vol.116 , pp. 4978-4989
    • Anderson, K.E.1    Chessa, T.A.2    Davidson, K.3    Henderson, R.B.4    Walker, S.5
  • 22
    • 0034946472 scopus 로고    scopus 로고
    • The PX domains of p47phox and p40phox bind to lipid products of PI(3)K
    • Kanai F, Liu H, Field SJ, Akbary H, Matsuo T, et al. 2001. The PX domains of p47phox and p40phox bind to lipid products of PI(3)K. Nat. Cell Biol. 3:675-78
    • (2001) Nat. Cell Biol. , vol.3 , pp. 675-678
    • Kanai, F.1    Liu, H.2    Field, S.J.3    Akbary, H.4    Matsuo, T.5
  • 24
    • 33749317192 scopus 로고    scopus 로고
    • PtdIns3P binding to the PX domain of p40phox is a physiological signal in NADPH oxidase activation
    • Ellson C, Davidson K, Anderson K, Stephens LR, Hawkins PT. 2006. PtdIns3P binding to the PX domain of p40phox is a physiological signal in NADPH oxidase activation. EMBO J. 25:4468-78
    • (2006) EMBO J. , vol.25 , pp. 4468-4478
    • Ellson, C.1    Davidson, K.2    Anderson, K.3    Stephens, L.R.4    Hawkins, P.T.5
  • 25
    • 77956958415 scopus 로고    scopus 로고
    • SLAM is a microbial sensor that regulates bacterial phagosome functions in macrophages
    • Berger SB, Romero X, Ma C, Wang G, Faubion WA, et al. 2010. SLAM is a microbial sensor that regulates bacterial phagosome functions in macrophages. Nat. Immunol. 11:920-27
    • (2010) Nat. Immunol. , vol.11 , pp. 920-927
    • Berger, S.B.1    Romero, X.2    Ma, C.3    Wang, G.4    Faubion, W.A.5
  • 26
    • 84861550705 scopus 로고    scopus 로고
    • Receptor signaling lymphocyte-activation molecule family 1 (Slamf1) regulates membrane fusion and NADPH oxidase 2 (NOX2) activity by recruiting a Beclin-1/Vps34/ultraviolet radiation resistance-associated gene (UVRAG) complex
    • Ma C, Wang N, Detre C, Wang G, O'Keeffe M, et al. 2012. Receptor signaling lymphocyte-activation molecule family 1 (Slamf1) regulates membrane fusion and NADPH oxidase 2 (NOX2) activity by recruiting a Beclin-1/Vps34/ ultraviolet radiation resistance-associated gene (UVRAG) complex. J. Biol. Chem. 287:18359-65
    • (2012) J. Biol. Chem. , vol.287 , pp. 18359-18365
    • Ma, C.1    Wang, N.2    Detre, C.3    Wang, G.4    O'Keeffe, M.5
  • 27
    • 84856249448 scopus 로고    scopus 로고
    • How phosphoinositide 3-phosphate controls growth downstream of amino acids and autophagy downstream of amino acid withdrawal
    • Ktistakis NT, Manifava M, Schoenfelder P, Rotondo S. 2012. How phosphoinositide 3-phosphate controls growth downstream of amino acids and autophagy downstream of amino acid withdrawal. Biochem. Soc. Trans. 40:37-43
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 37-43
    • Ktistakis, N.T.1    Manifava, M.2    Schoenfelder, P.3    Rotondo, S.4
  • 28
    • 84862295360 scopus 로고    scopus 로고
    • Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes
    • Klionsky DJ, Abeliovich H, Agostinis P, Agrawal DK, Aliev G, et al. 2012. Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes. Autophagy 8:445-544
    • (2012) Autophagy , vol.8 , pp. 445-544
    • Klionsky, D.J.1    Abeliovich, H.2    Agostinis, P.3    Agrawal, D.K.4    Aliev, G.5
  • 29
    • 78751672975 scopus 로고    scopus 로고
    • Autophagy in immunity and inflammation
    • Levine B, MizushimaN, VirginHW. 2011. Autophagy in immunity and inflammation. Nature 469:323-35
    • (2011) Nature , vol.469 , pp. 323-335
    • Levine, B.1    Mizushima, N.2    Virgin, H.W.3
  • 30
    • 80052251448 scopus 로고    scopus 로고
    • Autophagy in the control and pathogenesis of viral infection
    • Yordy B, Iwasaki A. 2011. Autophagy in the control and pathogenesis of viral infection. Curr. Opin. Virol. 1:196-203
    • (2011) Curr. Opin. Virol. , vol.1 , pp. 196-203
    • Yordy, B.1    Iwasaki, A.2
  • 31
    • 33947134377 scopus 로고    scopus 로고
    • Autophagy-dependent viral recognition by plasmacytoid dendritic cells
    • Lee HK, Lund JM, Ramanathan B, Mizushima N, Iwasaki A. 2007. Autophagy-dependent viral recognition by plasmacytoid dendritic cells. Science 315:1398-401
    • (2007) Science , vol.315 , pp. 1398-1401
    • Lee, H.K.1    Lund, J.M.2    Ramanathan, B.3    Mizushima, N.4    Iwasaki, A.5
  • 32
    • 12844275079 scopus 로고    scopus 로고
    • Endogenous MHC class II processing of a viral nuclear antigen after autophagy
    • Paludan C, Schmid D, Landthaler M, Vockerodt M, Kube D, et al. 2005. Endogenous MHC class II processing of a viral nuclear antigen after autophagy. Science 307:593-96
    • (2005) Science , vol.307 , pp. 593-596
    • Paludan, C.1    Schmid, D.2    Landthaler, M.3    Vockerodt, M.4    Kube, D.5
  • 33
    • 76949091325 scopus 로고    scopus 로고
    • In vivo requirement for Atg5 in antigen presentation by dendritic cells
    • Lee HK, Mattei LM, Steinberg BE, Alberts P, Lee YH, et al. 2010. In vivo requirement for Atg5 in antigen presentation by dendritic cells. Immunity 32:227-39
    • (2010) Immunity , vol.32 , pp. 227-239
    • Lee, H.K.1    Mattei, L.M.2    Steinberg, B.E.3    Alberts, P.4    Lee, Y.H.5
  • 34
    • 84872348186 scopus 로고    scopus 로고
    • Macroautophagy inTlymphocyte development and function
    • He MX, McLeod IX, JiaW, He YW.2012. Macroautophagy inTlymphocyte development and function. Front. Immunol. 3:22
    • (2012) Front. Immunol. , vol.3 , pp. 22
    • He, M.X.1    McLeod, I.X.2    Jia, W.3    He, Y.W.4
  • 35
    • 77953726483 scopus 로고    scopus 로고
    • Mammalian Atg18 (WIPI2) localizes to omegasome-anchored phagophores and positively regulates LC3 lipidation
    • PolsonHE, deLartigue J, Rigden DJ, ReedijkM, Urbe S, et al. 2010. Mammalian Atg18 (WIPI2) localizes to omegasome-anchored phagophores and positively regulates LC3 lipidation. Autophagy 6:506-22
    • (2010) Autophagy , vol.6 , pp. 506-522
    • Polson, H.E.1    De Lartigue, J.2    Rigden, D.J.3    Reedijk, M.4    Urbe, S.5
  • 36
    • 84860206692 scopus 로고    scopus 로고
    • Regulation and cellular functions of class II phosphoinositide 3-kinases
    • Falasca M, Maffucci T. 2012. Regulation and cellular functions of class II phosphoinositide 3-kinases. Biochem. J. 443:587-601
    • (2012) Biochem. J. , vol.443 , pp. 587-601
    • Falasca, M.1    Maffucci, T.2
  • 37
    • 78751679539 scopus 로고    scopus 로고
    • Requirement for class II phosphoinositide 3-kinase C2αin maintenance of glomerular structure and function
    • Harris DP, Vogel P, Wims M, Moberg K, Humphries J, et al. 2011. Requirement for class II phosphoinositide 3-kinase C2αin maintenance of glomerular structure and function. Mol. Cell. Biol. 31:63-80
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 63-80
    • Harris, D.P.1    Vogel, P.2    Wims, M.3    Moberg, K.4    Humphries, J.5
  • 38
    • 28544448230 scopus 로고    scopus 로고
    • The class II phosphoinositide 3-kinase C2β is not essential for epidermal differentiation
    • Harada K, Truong AB, Cai T, Khavari PA. 2005. The class II phosphoinositide 3-kinase C2β is not essential for epidermal differentiation. Mol. Cell. Biol. 25:11122-30
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 11122-11130
    • Harada, K.1    Truong, A.B.2    Cai, T.3    Khavari, P.A.4
  • 39
    • 58149402411 scopus 로고    scopus 로고
    • CD18-dependent activation of the neutrophilNADPHoxidase during phagocytosis of Escherichia coli or Staphylococcus aureus is regulated by class III but not class i or II PI3Ks
    • Anderson KE, Boyle KB, DavidsonK, Chessa TA, Kulkarni S, et al. 2008. CD18-dependent activation of the neutrophilNADPHoxidase during phagocytosis of Escherichia coli or Staphylococcus aureus is regulated by class III but not class I or II PI3Ks. Blood 112:5202-11
    • (2008) Blood , vol.112 , pp. 5202-5211
    • Anderson, K.E.1    Boyle, K.B.2    Davidson, K.3    Chessa, T.A.4    Kulkarni, S.5
  • 41
    • 30044440424 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-phosphate indirectly activates KCa3.1 via 14 amino acids in the carboxy terminus of KCa3.1
    • Srivastava S, Choudhury P, Li Z, Liu G, Nadkarni V, et al. 2006. Phosphatidylinositol 3-phosphate indirectly activates KCa3.1 via 14 amino acids in the carboxy terminus of KCa3.1. Mol. Biol. Cell 17:146-54
    • (2006) Mol. Biol. Cell , vol.17 , pp. 146-154
    • Srivastava, S.1    Choudhury, P.2    Li, Z.3    Liu, G.4    Nadkarni, V.5
  • 42
    • 33746547806 scopus 로고    scopus 로고
    • Phosphatidylinositol-3 phosphatase myotubularin-related protein 6 negatively regulates CD4 T cells
    • Srivastava S, Ko K, Choudhury P, Li Z, Johnson AK, et al. 2006. Phosphatidylinositol-3 phosphatase myotubularin-related protein 6 negatively regulates CD4 T cells. Mol. Cell. Biol. 26:5595-602
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 5595-5602
    • Srivastava, S.1    Ko, K.2    Choudhury, P.3    Li, Z.4    Johnson, A.K.5
  • 44
    • 84862861740 scopus 로고    scopus 로고
    • Ion channels and transporters in lymphocyte function and immunity
    • Feske S, Skolnik EY, Prakriya M. 2012. Ion channels and transporters in lymphocyte function and immunity. Nat. Rev. Immunol. 12:532-47
    • (2012) Nat. Rev. Immunol. , vol.12 , pp. 532-547
    • Feske, S.1    Skolnik, E.Y.2    Prakriya, M.3
  • 45
    • 0030669546 scopus 로고    scopus 로고
    • Osmotic stress activates phosphatidylinositol-3, 5-bisphosphate synthesis
    • Dove SK, Cooke FT, Douglas MR, Sayers LG, Parker PJ, et al. 1997. Osmotic stress activates phosphatidylinositol-3, 5-bisphosphate synthesis. Nature 390:187-92
    • (1997) Nature , vol.390 , pp. 187-192
    • Dove, S.K.1    Cooke, F.T.2    Douglas, M.R.3    Sayers, L.G.4    Parker, P.J.5
  • 46
    • 62749090535 scopus 로고    scopus 로고
    • Phosphatidylinositol 3, 5-bisphosphate and Fab1p/PIKfyve underPPIn endo-lysosome function
    • Dove SK, DongK, KobayashiT, Williams FK, Michell RH. 2009. Phosphatidylinositol 3, 5-bisphosphate and Fab1p/PIKfyve underPPIn endo-lysosome function. Biochem. J. 419:1-13
    • (2009) Biochem. J. , vol.419 , pp. 1-13
    • Dove, S.K.1    Dong, K.2    Kobayashi, T.3    Williams, F.K.4    Michell, R.H.5
  • 48
    • 77951460389 scopus 로고    scopus 로고
    • Inhibition of the PtdIns(5) kinase PIKfyve disrupts intracellular replication of Salmonella
    • Kerr MC, Wang JT, Castro NA, Hamilton NA, Town L, et al. 2010. Inhibition of the PtdIns(5) kinase PIKfyve disrupts intracellular replication of Salmonella. EMBO J. 29:1331-47
    • (2010) EMBO J. , vol.29 , pp. 1331-1347
    • Kerr, M.C.1    Wang, J.T.2    Castro, N.A.3    Hamilton, N.A.4    Town, L.5
  • 49
    • 84861901908 scopus 로고    scopus 로고
    • Myotubularin phosphoinositide phosphatases: Cellular functions and disease pathophysiology
    • Hnia K, Vaccari I, Bolino A, Laporte J. 2012. Myotubularin phosphoinositide phosphatases: cellular functions and disease pathophysiology. Trends Mol. Med. 18:317-27
    • (2012) Trends Mol. Med. , vol.18 , pp. 317-327
    • Hnia, K.1    Vaccari, I.2    Bolino, A.3    Laporte, J.4
  • 50
    • 33746729798 scopus 로고    scopus 로고
    • Myotubularin phosphatases: Policing 3-phosphoinositides
    • Robinson FL, Dixon JE. 2006. Myotubularin phosphatases: policing 3-phosphoinositides. Trends Cell Biol. 16:403-12
    • (2006) Trends Cell Biol. , vol.16 , pp. 403-412
    • Robinson, F.L.1    Dixon, J.E.2
  • 51
    • 77955458776 scopus 로고    scopus 로고
    • Drosophila Mtm and class II PI3K coregulate a PI(3)P pool with cortical and endolysosomal functions
    • Velichkova M, Juan J, Kadandale P, Jean S, Ribeiro I, et al. 2010. Drosophila Mtm and class II PI3K coregulate a PI(3)P pool with cortical and endolysosomal functions. J. Cell Biol. 190:407-25
    • (2010) J. Cell Biol. , vol.190 , pp. 407-425
    • Velichkova, M.1    Juan, J.2    Kadandale, P.3    Jean, S.4    Ribeiro, I.5
  • 52
    • 79952112367 scopus 로고    scopus 로고
    • Regulatory subunits of class IA PI3K
    • Fruman DA. 2010. Regulatory subunits of class IA PI3K. Curr. Top. Microbiol. Immunol. 346:225-44
    • (2010) Curr. Top. Microbiol. Immunol. , vol.346 , pp. 225-244
    • Fruman, D.A.1
  • 53
    • 79960055459 scopus 로고    scopus 로고
    • RAS interaction with PI3K: More than just another effector pathway
    • Castellano E, Downward J. 2011. RAS interaction with PI3K: more than just another effector pathway. Genes Cancer 2:261-74
    • (2011) Genes Cancer , vol.2 , pp. 261-274
    • Castellano, E.1    Downward, J.2
  • 54
    • 0037047590 scopus 로고    scopus 로고
    • Impaired B and T cell antigen receptor signaling in p110∞ PI 3-kinase mutant mice
    • Okkenhaug K, Bilancio A, Farjot G, Priddle H, Sancho S, et al. 2002. Impaired B and T cell antigen receptor signaling in p110∞ PI 3-kinase mutant mice. Science 297:1031-34
    • (2002) Science , vol.297 , pp. 1031-1034
    • Okkenhaug, K.1    Bilancio, A.2    Farjot, G.3    Priddle, H.4    Sancho, S.5
  • 55
    • 77956636063 scopus 로고    scopus 로고
    • The PI3K isoforms p110α and p110∞ are essential for pre-B cell receptor signaling and B cell development
    • Ramadani F, Bolland DJ, Garcon F, Emery JL, Vanhaesebroeck B, et al. 2010. The PI3K isoforms p110α and p110∞ are essential for pre-B cell receptor signaling and B cell development. Sci. Signal. 3:ra60
    • (2010) Sci. Signal. , vol.3
    • Ramadani, F.1    Bolland, D.J.2    Garcon, F.3    Emery, J.L.4    Vanhaesebroeck, B.5
  • 58
    • 0034635452 scopus 로고    scopus 로고
    • Central role forGprotein-coupled phosphoinositide 3-kinase γin inflammation
    • Hirsch E, Katanaev VL, Garlanda C, AzzolinoO, PirolaL, et al. 2000. Central role forGprotein-coupled phosphoinositide 3-kinase γin inflammation. Science 287:1049-53
    • (2000) Science , vol.287 , pp. 1049-1053
    • Hirsch, E.1    Katanaev, V.L.2    Garlanda, C.3    Azzolino Pirola, O.L.4
  • 59
    • 0034635264 scopus 로고    scopus 로고
    • Function of PI3Kγ in thymocyte development, T cell activation, and neutrophil migration
    • Sasaki T, Irie-Sasaki J, Jones RG, Oliveira-dos-Santos AJ, Stanford WL, et al. 2000. Function of PI3Kγ in thymocyte development, T cell activation, and neutrophil migration. Science 287:1040-46
    • (2000) Science , vol.287 , pp. 1040-1046
    • Sasaki, T.1    Irie-Sasaki, J.2    Jones, R.G.3    Oliveira-Dos-Santos, A.J.4    Stanford, W.L.5
  • 60
    • 0034635221 scopus 로고    scopus 로고
    • Roles of PLC-β2 and -β3 and PI3Kγ in chemoattractant- mediated signal transduction
    • Li Z, Jiang H, Xie W, Zhang Z, Smrcka AV, et al. 2000. Roles of PLC-β2 and -β3 and PI3Kγ in chemoattractant-mediated signal transduction. Science 287:1046-49
    • (2000) Science , vol.287 , pp. 1046-1049
    • Li, Z.1    Jiang, H.2    Xie, W.3    Zhang, Z.4    Smrcka, A.V.5
  • 61
    • 0037695593 scopus 로고    scopus 로고
    • Essential, nonredundant role for the phosphoinositide 3-kinase p110∞in signaling by the B-cell receptor complex
    • Jou ST, Carpino N, Takahashi Y, Piekorz R, Chao JR, et al. 2002. Essential, nonredundant role for the phosphoinositide 3-kinase p110∞in signaling by the B-cell receptor complex. Mol. Cell. Biol. 22:8580-91
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8580-8591
    • Jou, S.T.1    Carpino, N.2    Takahashi, Y.3    Piekorz, R.4    Chao, J.R.5
  • 62
    • 0037119630 scopus 로고    scopus 로고
    • A crucial role for the p110∞ subunit of phosphatidylinositol 3-kinase in B cell development and activation
    • Clayton E, Bardi G, Bell SE, Chantry D, Downes CP, et al. 2002. A crucial role for the p110∞ subunit of phosphatidylinositol 3-kinase in B cell development and activation. J. Exp. Med. 196:753-63
    • (2002) J. Exp. Med. , vol.196 , pp. 753-763
    • Clayton, E.1    Bardi, G.2    Bell, S.E.3    Chantry, D.4    Downes, C.P.5
  • 63
    • 0037369696 scopus 로고    scopus 로고
    • Essential role of phosphoinositide 3-kinase ∞ in neutrophil directional movement
    • Sadhu C, Masinovsky B, Dick K, Sowell CG, Staunton DE. 2003. Essential role of phosphoinositide 3-kinase ∞ in neutrophil directional movement. J. Immunol. 170:2647-54
    • (2003) J. Immunol. , vol.170 , pp. 2647-2654
    • Sadhu, C.1    Masinovsky, B.2    Dick, K.3    Sowell, C.G.4    Staunton, D.E.5
  • 64
    • 24744435115 scopus 로고    scopus 로고
    • Blockade of PI3Kγ suppresses joint inflammation and damage in mouse models of rheumatoid arthritis
    • Camps M, Ruckle T, Ji H, Ardissone V, Rintelen F, et al. 2005. Blockade of PI3Kγ suppresses joint inflammation and damage in mouse models of rheumatoid arthritis. Nat. Med. 11:936-43
    • (2005) Nat. Med. , vol.11 , pp. 936-943
    • Camps, M.1    Ruckle, T.2    Ji, H.3    Ardissone, V.4    Rintelen, F.5
  • 66
    • 46149106818 scopus 로고    scopus 로고
    • The p110βisoform of phosphoinositide 3-kinase signals downstream of G protein-coupled receptors and is functionally redundant with p110γ
    • Guillermet-Guibert J, Bjorklof K, Salpekar A, Gonella C, Ramadani F, et al. 2008. The p110βisoform of phosphoinositide 3-kinase signals downstream of G protein-coupled receptors and is functionally redundant with p110γ. Proc. Natl. Acad. Sci. USA. 105:8292-97
    • (2008) Proc. Natl. Acad. Sci. USA. , vol.105 , pp. 8292-8297
    • Guillermet-Guibert, J.1    Bjorklof, K.2    Salpekar, A.3    Gonella, C.4    Ramadani, F.5
  • 67
    • 55649084906 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase p110β activity: Key role in metabolism and mammary gland cancer but not development
    • Ciraolo E, Iezzi M, Marone R, Marengo S, Curcio C, et al. 2008. Phosphoinositide 3-kinase p110β activity: key role in metabolism and mammary gland cancer but not development. Sci. Signal. 1:ra3
    • (2008) Sci. Signal. , vol.1
    • Ciraolo, E.1    Iezzi, M.2    Marone, R.3    Marengo, S.4    Curcio, C.5
  • 68
    • 49649087385 scopus 로고    scopus 로고
    • Essential roles of PI(3)K-p110β in cell growth, metabolism and tumorigenesis
    • Jia S, Liu Z, Zhang S, Liu P, Zhang L, et al. 2008. Essential roles of PI(3)K-p110β in cell growth, metabolism and tumorigenesis. Nature 454:776-79
    • (2008) Nature , vol.454 , pp. 776-779
    • Jia, S.1    Liu, Z.2    Zhang, S.3    Liu, P.4    Zhang, L.5
  • 69
    • 84870750816 scopus 로고    scopus 로고
    • G protein-coupled receptormediated activation of p110βbyGβ γis required for cellular transformation and invasiveness
    • Dbouk HA, Vadas O, Shymanets A, Burke JE, Salamon RS, et al. 2012. G protein-coupled receptormediated activation of p110βbyGβγis required for cellular transformation and invasiveness. Sci. Signal. 5:ra89
    • (2012) Sci. Signal. , vol.5
    • Dbouk, H.A.1    Vadas, O.2    Shymanets, A.3    Burke, J.E.4    Salamon, R.S.5
  • 70
    • 65249191411 scopus 로고    scopus 로고
    • P110γ and p110∞ isoforms of phosphoinositide 3-kinase differentially regulate natural killer cell migration in health and disease
    • Saudemont A, Garcon F, Yadi H, Roche-Molina M, Kim N, et al. 2009. p110γ and p110∞ isoforms of phosphoinositide 3-kinase differentially regulate natural killer cell migration in health and disease. Proc. Natl. Acad. Sci. USA 106:5795-800
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 5795-5800
    • Saudemont, A.1    Garcon, F.2    Yadi, H.3    Roche-Molina, M.4    Kim, N.5
  • 71
    • 4043082729 scopus 로고    scopus 로고
    • Cutting edge: Differential roles for phosphoinositide 3-kinases, p110γ and p110∞, in lymphocyte chemotaxis and homing
    • Reif K, Okkenhaug K, Sasaki T, Penninger JM, Vanhaesebroeck B, et al. 2004. Cutting edge: differential roles for phosphoinositide 3-kinases, p110γ and p110∞, in lymphocyte chemotaxis and homing. J. Immunol. 173:2236-40
    • (2004) J. Immunol. , vol.173 , pp. 2236-2240
    • Reif, K.1    Okkenhaug, K.2    Sasaki, T.3    Penninger, J.M.4    Vanhaesebroeck, B.5
  • 73
    • 11144358645 scopus 로고    scopus 로고
    • High frequency of mutations of the PIK3CA gene in human cancers
    • Samuels Y, Wang Z, Bardelli A, Silliman N, Ptak J, et al. 2004. High frequency of mutations of the PIK3CA gene in human cancers. Science 304:554
    • (2004) Science , vol.304 , pp. 554
    • Samuels, Y.1    Wang, Z.2    Bardelli, A.3    Silliman, N.4    Ptak, J.5
  • 74
    • 80054736907 scopus 로고    scopus 로고
    • Structural basis for activation and inhibition of class i phosphoinositide 3-kinases
    • Vadas O, Burke JE, Zhang X, Berndt A, Williams RL. 2011. Structural basis for activation and inhibition of class I phosphoinositide 3-kinases. Sci. Signal. 4:re2
    • (2011) Sci. Signal. , vol.4
    • Vadas, O.1    Burke, J.E.2    Zhang, X.3    Berndt, A.4    Williams, R.L.5
  • 75
    • 78651330430 scopus 로고    scopus 로고
    • COSMIC: Mining complete cancer genomes in the Catalogue of Somatic Mutations in Cancer
    • Forbes SA, Bindal N, Bamford S, Cole C, Kok CY, et al. 2011. COSMIC: mining complete cancer genomes in the Catalogue of Somatic Mutations in Cancer. Nucleic Acids Res. 39:D945-50. http://www.sanger.ac.uk/cosmic
    • (2011) Nucleic Acids Res. , vol.39
    • Forbes, S.A.1    Bindal, N.2    Bamford, S.3    Cole, C.4    Kok, C.Y.5
  • 77
    • 37249056471 scopus 로고    scopus 로고
    • The structure of a human p110α/p85αcomplex elucidates the effects of oncogenic PI3Kαmutations
    • Huang CH, Mandelker D, Schmidt-Kittler O, Samuels Y, Velculescu VE, et al. 2007. The structure of a human p110α/p85αcomplex elucidates the effects of oncogenic PI3Kαmutations. Science 318:1744-48
    • (2007) Science , vol.318 , pp. 1744-1748
    • Huang, C.H.1    Mandelker, D.2    Schmidt-Kittler, O.3    Samuels, Y.4    Velculescu, V.E.5
  • 78
    • 34447503808 scopus 로고    scopus 로고
    • Mechanism of two classes of cancer mutations in the phosphoinositide 3-kinase catalytic subunit
    • Miled N, Yan Y, Hon WC, Perisic O, Zvelebil M, et al. 2007. Mechanism of two classes of cancer mutations in the phosphoinositide 3-kinase catalytic subunit. Science 317:239-42
    • (2007) Science , vol.317 , pp. 239-242
    • Miled, N.1    Yan, Y.2    Hon, W.C.3    Perisic, O.4    Zvelebil, M.5
  • 79
    • 0032514801 scopus 로고    scopus 로고
    • Regulation of the p85/p110αphosphatidylinositol 3-kinase. Distinct roles for the N-terminal and C-terminal SH2 domains
    • Yu J, Wjasow C, Backer JM. 1998. Regulation of the p85/ p110αphosphatidylinositol 3-kinase. Distinct roles for the N-terminal and C-terminal SH2 domains. J. Biol. Chem. 273:30199-203
    • (1998) J. Biol. Chem. , vol.273 , pp. 30199-30203
    • Yu, J.1    Wjasow, C.2    Backer, J.M.3
  • 80
    • 0031887249 scopus 로고    scopus 로고
    • Regulation of the p85/p110 phosphatidylinositol 3-kinase: Stabilization and inhibition of the p110αcatalytic subunit by the p85 regulatory subunit
    • Yu J, Zhang Y, McIlroy J, Rordorf-Nikolic T, Orr GA, et al. 1998. Regulation of the p85/p110 phosphatidylinositol 3-kinase: stabilization and inhibition of the p110αcatalytic subunit by the p85 regulatory subunit. Mol. Cell. Biol. 18:1379-87
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1379-1387
    • Yu, J.1    Zhang, Y.2    McIlroy, J.3    Rordorf-Nikolic, T.4    Orr, G.A.5
  • 81
    • 80051488597 scopus 로고    scopus 로고
    • Dynamics of the phosphoinositide 3-kinase p110∞interaction with p85αand membranes reveals aspects of regulation distinct from p110α
    • Burke JE, Vadas O, Berndt A, Finegan T, Perisic O, et al. 2011. Dynamics of the phosphoinositide 3-kinase p110∞interaction with p85αand membranes reveals aspects of regulation distinct from p110α. Structure 19:1127-37
    • (2011) Structure , vol.19 , pp. 1127-1137
    • Burke, J.E.1    Vadas, O.2    Berndt, A.3    Finegan, T.4    Perisic, O.5
  • 82
    • 40649096375 scopus 로고    scopus 로고
    • Helical domain and kinase domain mutations in p110αof phosphatidylinositol 3-kinase induce gain of function by different mechanisms
    • Zhao L, Vogt PK. 2008. Helical domain and kinase domain mutations in p110αof phosphatidylinositol 3-kinase induce gain of function by different mechanisms. Proc. Natl. Acad. Sci. USA 105:2652-57
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 2652-2657
    • Zhao, L.1    Vogt, P.K.2
  • 83
    • 77957258073 scopus 로고    scopus 로고
    • Cancer-derived mutations in the regulatory subunit p85αof phosphoinositide 3-kinase function through the catalytic subunit p110α
    • SunM, Hillmann P, Hofmann BT, Hart JR, Vogt PK. 2010. Cancer-derived mutations in the regulatory subunit p85αof phosphoinositide 3-kinase function through the catalytic subunit p110α. Proc.Natl. Acad. Sci. USA. 107:15547-52
    • (2010) Proc.Natl. Acad. Sci. USA. , vol.107 , pp. 15547-15552
    • Sun, M.1    Hillmann, P.2    Hofmann, B.T.3    Hart, J.R.4    Vogt, P.K.5
  • 84
    • 73949084778 scopus 로고    scopus 로고
    • Regulation of class IA PI 3-kinases: C2 domain-iSH2 domain contacts inhibit p85/p110αand are disrupted in oncogenic p85 mutants
    • Wu H, Shekar SC, Flinn RJ, El-Sibai M, Jaiswal BS, et al. 2009. Regulation of class IA PI 3-kinases: C2 domain-iSH2 domain contacts inhibit p85/p110αand are disrupted in oncogenic p85 mutants. Proc. Natl. Acad. Sci. USA 106:20258-63
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 20258-20263
    • Wu, H.1    Shekar, S.C.2    Flinn, R.J.3    El-Sibai, M.4    Jaiswal, B.S.5
  • 85
    • 34249026448 scopus 로고    scopus 로고
    • Binding of Ras to phosphoinositide 3-kinase p110αis required for Ras-driven tumorigenesis in mice
    • Gupta S, Ramjaun AR, Haiko P, Wang Y, Warne PH, et al. 2007. Binding of Ras to phosphoinositide 3-kinase p110αis required for Ras-driven tumorigenesis in mice. Cell 129:957-68
    • (2007) Cell , vol.129 , pp. 957-968
    • Gupta, S.1    Ramjaun, A.R.2    Haiko, P.3    Wang, Y.4    Warne, P.H.5
  • 86
    • 31944448780 scopus 로고    scopus 로고
    • Oncogenic transformation induced by the p110β, -γ, and -∞ Isoforms of class i phosphoinositide 3-kinase
    • Kang S, Denley A, Vanhaesebroeck B, Vogt PK. 2006. Oncogenic transformation induced by the p110β, -γ, and -∞ isoforms of class I phosphoinositide 3-kinase. Proc. Natl. Acad. Sci. USA 103:1289-94
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 1289-1294
    • Kang, S.1    Denley, A.2    Vanhaesebroeck, B.3    Vogt, P.K.4
  • 88
    • 2442689239 scopus 로고    scopus 로고
    • Signaling specificity by Ras family GTPases is determined by the full spectrum of effectors they regulate
    • Rodriguez-Viciana P, Sabatier C, McCormick F. 2004. Signaling specificity by Ras family GTPases is determined by the full spectrum of effectors they regulate. Mol. Cell. Biol. 24:4943-54
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4943-4954
    • Rodriguez-Viciana, P.1    Sabatier, C.2    McCormick, F.3
  • 89
    • 67651151038 scopus 로고    scopus 로고
    • Essential function for the GTPase TC21 in homeostatic antigen receptor signaling
    • Delgado P, Cubelos B, Calleja E, Martinez-Martin N, Cipres A, et al. 2009. Essential function for the GTPase TC21 in homeostatic antigen receptor signaling. Nat. Immunol. 10:880-88
    • (2009) Nat. Immunol. , vol.10 , pp. 880-888
    • Delgado, P.1    Cubelos, B.2    Calleja, E.3    Martinez-Martin, N.4    Cipres, A.5
  • 90
    • 79951993684 scopus 로고    scopus 로고
    • Structure of lipid kinase p110β/p85β elucidates an unusual SH2-domain-mediated inhibitory mechanism
    • Zhang X, Vadas O, Perisic O, Anderson KE, Clark J, et al. 2011. Structure of lipid kinase p110β/p85β elucidates an unusual SH2-domain-mediated inhibitory mechanism. Mol. Cell 41:567-78
    • (2011) Mol. Cell , vol.41 , pp. 567-578
    • Zhang, X.1    Vadas, O.2    Perisic, O.3    Anderson, K.E.4    Clark, J.5
  • 91
    • 33744990592 scopus 로고    scopus 로고
    • Critical role for the p110α phosphoinositide-3-OH kinase in growth and metabolic regulation
    • Foukas LC, Claret M, Pearce W, Okkenhaug K, Meek S, et al. 2006. Critical role for the p110α phosphoinositide-3-OH kinase in growth and metabolic regulation. Nature 441:366-70
    • (2006) Nature , vol.441 , pp. 366-370
    • Foukas, L.C.1    Claret, M.2    Pearce, W.3    Okkenhaug, K.4    Meek, S.5
  • 92
    • 33646383684 scopus 로고    scopus 로고
    • A pharmacological map of the PI3-K family defines a role for p110αin insulin signaling
    • Knight ZA, Gonzalez B, Feldman ME, Zunder ER, Goldenberg DD, et al. 2006. A pharmacological map of the PI3-K family defines a role for p110αin insulin signaling. Cell 125:733-47
    • (2006) Cell , vol.125 , pp. 733-747
    • Knight, Z.A.1    Gonzalez, B.2    Feldman, M.E.3    Zunder, E.R.4    Goldenberg, D.D.5
  • 93
    • 44349119736 scopus 로고    scopus 로고
    • Angiogenesis selectively requires the p110αisoform of PI3K to control endothelial cell migration
    • Graupera M, Guillermet-Guibert J, Foukas LC, Phng LK, Cain RJ, et al. 2008. Angiogenesis selectively requires the p110αisoform of PI3K to control endothelial cell migration. Nature 453:662-66
    • (2008) Nature , vol.453 , pp. 662-666
    • Graupera, M.1    Guillermet-Guibert, J.2    Foukas, L.C.3    Phng, L.K.4    Cain, R.J.5
  • 94
    • 33750826279 scopus 로고    scopus 로고
    • The p110αisoform of PI3K is essential for proper growth factor signaling and oncogenic transformation
    • Zhao JJ, Cheng H, Jia S, Wang L, Gjoerup OV, et al. 2006. The p110αisoform of PI3K is essential for proper growth factor signaling and oncogenic transformation. Proc. Natl. Acad. Sci. USA 103:16296-300
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 16296-16300
    • Zhao, J.J.1    Cheng, H.2    Jia, S.3    Wang, L.4    Gjoerup, O.V.5
  • 95
    • 40449110080 scopus 로고    scopus 로고
    • The effect of deleting p110∞ on the phenotype and function of PTEN-deficient B cells
    • Janas ML, Hodson D, Stamataki Z, Hill S, Welch K, et al. 2008. The effect of deleting p110∞ on the phenotype and function of PTEN-deficient B cells. J. Immunol. 180:739-46
    • (2008) J. Immunol. , vol.180 , pp. 739-746
    • Janas, M.L.1    Hodson, D.2    Stamataki, Z.3    Hill, S.4    Welch, K.5
  • 96
    • 30444439101 scopus 로고    scopus 로고
    • Key role of the p110∞isoform of PI3K in B-cell antigen and IL-4 receptor signaling: Comparative analysis of genetic and pharmacologic interference with p110∞ function in B cells
    • Bilancio A, Okkenhaug K, CampsM, Emery JL, Ruckle T, et al. 2006. Key role of the p110∞isoform of PI3K in B-cell antigen and IL-4 receptor signaling: comparative analysis of genetic and pharmacologic interference with p110∞ function in B cells. Blood 107:642-50
    • (2006) Blood , vol.107 , pp. 642-650
    • Bilancio, A.1    Okkenhaug, K.2    Camps, M.3    Emery, J.L.4    Ruckle, T.5
  • 97
    • 33846621025 scopus 로고    scopus 로고
    • Antigen receptor signalling: A distinctive role for the p110∞ isoform of PI3K
    • Okkenhaug K, Ali K, Vanhaesebroeck B. 2007. Antigen receptor signalling: a distinctive role for the p110∞ isoform of PI3K. Trends Immunol. 28:80-87
    • (2007) Trends Immunol. , vol.28 , pp. 80-87
    • Okkenhaug, K.1    Ali, K.2    Vanhaesebroeck, B.3
  • 99
    • 75349106113 scopus 로고    scopus 로고
    • The p110∞ structure: Mechanisms for selectivity and potency of new PI(3)K inhibitors
    • Berndt A, Miller S, Williams O, Le DD, Houseman BT, et al. 2010. The p110∞ structure: mechanisms for selectivity and potency of new PI(3)K inhibitors. Nat. Chem. Biol. 6:117-24
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 117-124
    • Berndt, A.1    Miller, S.2    Williams, O.3    Le, D.D.4    Houseman, B.T.5
  • 100
    • 0027169534 scopus 로고
    • CD19 of B cells as a surrogate kinase insert region to bind phosphatidylinositol 3-kinase
    • Tuveson DA, Carter RH, Soltoff SP, Fearon DT. 1993. CD19 of B cells as a surrogate kinase insert region to bind phosphatidylinositol 3-kinase. Science 260:986-89
    • (1993) Science , vol.260 , pp. 986-989
    • Tuveson, D.A.1    Carter, R.H.2    Soltoff, S.P.3    Fearon, D.T.4
  • 102
    • 84874219783 scopus 로고    scopus 로고
    • Pharmacological targeting of phosphoinositide lipid kinases and phosphatases in the immune system: Success, disappointment and new opportunities
    • Ward SG, Blunt MD. 2012. Pharmacological targeting of phosphoinositide lipid kinases and phosphatases in the immune system: success, disappointment and new opportunities. Front. Immunol. 3:226
    • (2012) Front. Immunol. , vol.3 , pp. 226
    • Ward, S.G.1    Blunt, M.D.2
  • 103
    • 0030820924 scopus 로고    scopus 로고
    • Acomparative analysis of the phosphoinositide binding specificity of pleckstrin homology domains
    • Rameh LE, ArvidssonA, CarrawayKL3rd, Couvillon AD, Rathbun G, et al. 1997.Acomparative analysis of the phosphoinositide binding specificity of pleckstrin homology domains. J. Biol. Chem. 272:22059-66
    • (1997) J. Biol. Chem. , vol.272 , pp. 22059-22066
    • Rameh, L.E.1    Arvidsson, A.2    Carraway Iii, K.L.3    Couvillon, A.D.4    Rathbun, G.5
  • 104
    • 0031039024 scopus 로고    scopus 로고
    • Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3, 4-bisphosphate
    • Franke TF, Kaplan DR, Cantley LC, Toker A. 1997. Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3, 4-bisphosphate. Science 275:665-68
    • (1997) Science , vol.275 , pp. 665-668
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3    Toker, A.4
  • 105
    • 0034663568 scopus 로고    scopus 로고
    • Signal-dependentmembrane targeting by pleckstrin homology (PH) domains
    • LemmonMA, Ferguson KM. 2000. Signal-dependentmembrane targeting by pleckstrin homology (PH) domains. Biochem. J. 350(Pt. 1):1-18
    • (2000) Biochem. J. , vol.350 , Issue.PART 1 , pp. 1-18
    • Ma, L.1    Ferguson, K.M.2
  • 106
    • 84874196138 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase signalling pathway in normal and malignant B cells: Activation mechanisms, regulation and impact on cellular functions
    • Pauls SD, Lafarge ST, Landego I, Zhang T-t, Marshall AJ. 2012. The phosphoinositide 3-kinase signalling pathway in normal and malignant B cells: activation mechanisms, regulation and impact on cellular functions. Front. Immunol. 3:224
    • (2012) Front. Immunol. , vol.3 , pp. 224
    • Pauls, S.D.1    Lafarge, S.T.2    Landego, I.3    Zhang, T.-T.4    Marshall, A.J.5
  • 107
    • 84872319862 scopus 로고    scopus 로고
    • Regulation of T cell homeostasis and responses by Pten
    • Newton RH, Turka LA. 2012. Regulation of T cell homeostasis and responses by Pten. Front. Immunol. 3:151
    • (2012) Front. Immunol. , vol.3 , pp. 151
    • Newton, R.H.1    Turka, L.A.2
  • 108
    • 0034995242 scopus 로고    scopus 로고
    • T cell-specific loss of Pten leads to defects in central and peripheral tolerance
    • Suzuki A, Yamaguchi MT, Ohteki T, Sasaki T, Kaisho T, et al. 2001. T cell-specific loss of Pten leads to defects in central and peripheral tolerance. Immunity 14:523-34
    • (2001) Immunity , vol.14 , pp. 523-534
    • Suzuki, A.1    Yamaguchi, M.T.2    Ohteki, T.3    Sasaki, T.4    Kaisho, T.5
  • 109
    • 33749132566 scopus 로고    scopus 로고
    • Cutting edge: T cell requirement for CD28 costimulation is due to negative regulation of TCR signals by PTEN
    • Buckler JL, Walsh PT, Porrett PM, Choi Y, Turka LA. 2006. Cutting edge: T cell requirement for CD28 costimulation is due to negative regulation of TCR signals by PTEN. J. Immunol. 177:4262-66
    • (2006) J. Immunol. , vol.177 , pp. 4262-4266
    • Buckler, J.L.1    Walsh, P.T.2    Porrett, P.M.3    Choi, Y.4    Turka, L.A.5
  • 110
    • 84862589113 scopus 로고    scopus 로고
    • Pten loss in CD4 T cells enhances their helper function but does not lead to autoimmunity or lymphoma
    • Soond DR, Garcon F, Patton DT, Rolf J, Turner M, et al. 2012. Pten loss in CD4 T cells enhances their helper function but does not lead to autoimmunity or lymphoma. J. Immunol. 188:5935-43
    • (2012) J. Immunol. , vol.188 , pp. 5935-5943
    • Soond, D.R.1    Garcon, F.2    Patton, D.T.3    Rolf, J.4    Turner, M.5
  • 111
    • 33749685322 scopus 로고    scopus 로고
    • Regulation of classswitch recombination and plasma cell differentiation by phosphatidylinositol 3-kinase signaling
    • Omori SA, Cato MH, Anzelon-Mills A, Puri KD, Shapiro-Shelef M, et al. 2006. Regulation of classswitch recombination and plasma cell differentiation by phosphatidylinositol 3-kinase signaling. Immunity 25:245-57
    • (2006) Immunity , vol.25 , pp. 245-257
    • Omori, S.A.1    Cato, M.H.2    Anzelon-Mills, A.3    Puri, K.D.4    Shapiro-Shelef, M.5
  • 112
    • 70449701417 scopus 로고    scopus 로고
    • Suppression of phosphatidylinositol 3, 4, 5-trisphosphate production is a key determinant of B cell anergy
    • Browne CD, Del Nagro CJ, Cato MH, Dengler HS, Rickert RC. 2009. Suppression of phosphatidylinositol 3, 4, 5-trisphosphate production is a key determinant of B cell anergy. Immunity 31:749-60
    • (2009) Immunity , vol.31 , pp. 749-760
    • Browne, C.D.1    Del Nagro, C.J.2    Cato, M.H.3    Dengler, H.S.4    Rickert, R.C.5
  • 113
    • 0037416216 scopus 로고    scopus 로고
    • Critical roles of Pten in B cell homeostasis and immunoglobulin class switch recombination
    • Suzuki A, Kaisho T, Ohishi M, Tsukio-Yamaguchi M, Tsubata T, et al. 2003. Critical roles of Pten in B cell homeostasis and immunoglobulin class switch recombination. J. Exp. Med. 197:657-67
    • (2003) J. Exp. Med. , vol.197 , pp. 657-667
    • Suzuki, A.1    Kaisho, T.2    Ohishi, M.3    Tsukio-Yamaguchi, M.4    Tsubata, T.5
  • 114
    • 79251553448 scopus 로고    scopus 로고
    • Inhibitor and activator: Dual functions for SHIP in immunity and cancer
    • Kerr WG. 2011. Inhibitor and activator: dual functions for SHIP in immunity and cancer. Ann. N. Y. Acad. Sci. 1217:1-17
    • (2011) Ann. N. Y. Acad. Sci. , vol.1217 , pp. 1-17
    • Kerr, W.G.1
  • 116
    • 78650675585 scopus 로고    scopus 로고
    • Inositol polyphosphate 4-phosphatase II regulates PI3K/Akt signaling and is lost in human basal-like breast cancers
    • Fedele CG, Ooms LM, Ho M, Vieusseux J, O'Toole SA, et al. 2010. Inositol polyphosphate 4-phosphatase II regulates PI3K/Akt signaling and is lost in human basal-like breast cancers. Proc. Natl. Acad. Sci. USA 107:22231-36
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 22231-22236
    • Fedele, C.G.1    Ooms, L.M.2    Ho, M.3    Vieusseux, J.4    O'Toole, S.A.5
  • 117
    • 67651148274 scopus 로고    scopus 로고
    • Evidence that inositol polyphosphate 4-phosphatase type II is a tumor suppressor that inhibits PI3K signaling
    • Gewinner C, Wang ZC, Richardson A, Teruya-Feldstein J, Etemadmoghadam D, et al. 2009. Evidence that inositol polyphosphate 4-phosphatase type II is a tumor suppressor that inhibits PI3K signaling. Cancer Cell 16:115-25
    • (2009) Cancer Cell , vol.16 , pp. 115-125
    • Gewinner, C.1    Wang, Z.C.2    Richardson, A.3    Teruya-Feldstein, J.4    Etemadmoghadam, D.5
  • 118
    • 38549092474 scopus 로고    scopus 로고
    • Membrane recognition by phospholipid-binding domains
    • Lemmon MA. 2008. Membrane recognition by phospholipid-binding domains. Nat. Rev. Mol. Cell Biol. 9:99-111
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 99-111
    • Lemmon, M.A.1
  • 120
    • 46449113353 scopus 로고    scopus 로고
    • Crucial structural role for the PH and C1 domains of the Vav1 exchange factor
    • Rapley J, Tybulewicz VL, Rittinger K. 2008. Crucial structural role for the PH and C1 domains of the Vav1 exchange factor. EMBO Rep. 9:655-61
    • (2008) EMBO Rep. , vol.9 , pp. 655-661
    • Rapley, J.1    Tybulewicz, V.L.2    Rittinger, K.3
  • 121
    • 42949124488 scopus 로고    scopus 로고
    • Comprehensive identification of PIP3-regulated PH domains from C. elegans to H. sapiens by model prediction and live imaging
    • Park WS, Heo WD, Whalen JH, O'Rourke NA, Bryan HM, et al. 2008. Comprehensive identification of PIP3-regulated PH domains from C. elegans to H. sapiens by model prediction and live imaging. Mol. Cell 30:381-92
    • (2008) Mol. Cell , vol.30 , pp. 381-392
    • Park, W.S.1    Heo, W.D.2    Whalen, J.H.3    O'Rourke, N.A.4    Bryan, H.M.5
  • 122
    • 18244392475 scopus 로고    scopus 로고
    • Identification of ARAP3, a novel PI3K effector regulating both Arf and Rho GTPases, by selective capture on phosphoinositide affinity matrices
    • Krugmann S, Anderson KE, Ridley SH, Risso N, McGregor A, et al. 2002. Identification of ARAP3, a novel PI3K effector regulating both Arf and Rho GTPases, by selective capture on phosphoinositide affinity matrices. Mol. Cell 9:95-108.
    • (2002) Mol. Cell , vol.9 , pp. 95-95
    • Krugmann, S.1    Anderson, K.E.2    Ridley, S.H.3    Risso, N.4    McGregor, A.5
  • 123
    • 70349469577 scopus 로고    scopus 로고
    • The cunning little vixen: Foxo and the cycle of life and death
    • Hedrick SM. 2009. The cunning little vixen: Foxo and the cycle of life and death. Nat. Immunol. 10:1057-63
    • (2009) Nat. Immunol. , vol.10 , pp. 1057-1063
    • Hedrick, S.M.1
  • 125
    • 79151486083 scopus 로고    scopus 로고
    • Metabolism, migration and memory in cytotoxicTcells
    • Finlay D, Cantrell DA. 2011. Metabolism, migration and memory in cytotoxicTcells. Nat. Rev. Immunol. 11:109-17
    • (2011) Nat. Rev. Immunol. , vol.11 , pp. 109-117
    • Finlay, D.1    Cantrell, D.A.2
  • 126
    • 84873702448 scopus 로고    scopus 로고
    • Akt and mTOR in B cell activation and differentiation
    • Fruman DA, Limon JJ. 2012. Akt and mTOR in B cell activation and differentiation. Front. Immunol. 3:228
    • (2012) Front. Immunol. , vol.3 , pp. 228
    • Fruman, D.A.1    Limon, J.J.2
  • 127
    • 34250788809 scopus 로고    scopus 로고
    • AKT/PKB signaling: Navigating downstream
    • Manning BD, Cantley LC. 2007. AKT/PKB signaling: navigating downstream. Cell 129:1261-74
    • (2007) Cell , vol.129 , pp. 1261-1274
    • Manning, B.D.1    Cantley, L.C.2
  • 128
    • 84555191987 scopus 로고    scopus 로고
    • Akt isoform-specific signaling in breast cancer: Uncovering an anti-migratory role for palladin
    • Chin YR, Toker A. 2011. Akt isoform-specific signaling in breast cancer: uncovering an anti-migratory role for palladin. Cell Adhes. Migr. 5:211-14
    • (2011) Cell Adhes. Migr. , vol.5 , pp. 211-214
    • Chin, Y.R.1    Toker, A.2
  • 129
    • 77953247731 scopus 로고    scopus 로고
    • Akt1 and Akt2 promote peripheral B-cell maturation and survival
    • Calamito M, Juntilla MM, Thomas M, Northrup DL, Rathmell J, et al. 2010. Akt1 and Akt2 promote peripheral B-cell maturation and survival. Blood 115:4043-50
    • (2010) Blood , vol.115 , pp. 4043-4050
    • Calamito, M.1    Juntilla, M.M.2    Thomas, M.3    Northrup, D.L.4    Rathmell, J.5
  • 130
    • 77953283847 scopus 로고    scopus 로고
    • AKT1 and AKT2 maintain hematopoietic stem cell function by regulating reactive oxygen species
    • Juntilla MM, Patil VD, Calamito M, Joshi RP, Birnbaum MJ, et al. 2010. AKT1 and AKT2 maintain hematopoietic stem cell function by regulating reactive oxygen species. Blood 115:4030-38
    • (2010) Blood , vol.115 , pp. 4030-4038
    • Juntilla, M.M.1    Patil, V.D.2    Calamito, M.3    Joshi, R.P.4    Birnbaum, M.J.5
  • 133
    • 34247627902 scopus 로고    scopus 로고
    • Unequal contribution of Akt isoforms in the double-negative to double-positive thymocyte transition
    • Mao C, Tili EG, Dose M, Haks MC, Bear SE, et al. 2007. Unequal contribution of Akt isoforms in the double-negative to double-positive thymocyte transition. J. Immunol. 178:5443-53
    • (2007) J. Immunol. , vol.178 , pp. 5443-5453
    • Mao, C.1    Tili, E.G.2    Dose, M.3    Haks, M.C.4    Bear, S.E.5
  • 134
    • 79951745387 scopus 로고    scopus 로고
    • Protein kinase B controls transcriptional programs that direct cytotoxic T cell fate but is dispensable for T cell metabolism
    • Macintyre AN, Finlay D, PrestonG, Sinclair LV, Waugh CM, et al. 2011. Protein kinase B controls transcriptional programs that direct cytotoxic T cell fate but is dispensable for T cell metabolism. Immunity 34:224-36
    • (2011) Immunity , vol.34 , pp. 224-236
    • Macintyre, A.N.1    Finlay, D.2    Preston, G.3    Sinclair, L.V.4    Waugh, C.M.5
  • 135
    • 44049091757 scopus 로고    scopus 로고
    • Foxo1 directly regulates the transcription of recombination-activating genes during B cell development
    • Amin RH, Schlissel MS. 2008. Foxo1 directly regulates the transcription of recombination-activating genes during B cell development. Nat. Immunol. 9:613-22
    • (2008) Nat. Immunol. , vol.9 , pp. 613-622
    • Amin, R.H.1    Schlissel, M.S.2
  • 136
    • 56349127778 scopus 로고    scopus 로고
    • Distinct functions for the transcription factor Foxo1 at various stages of B cell differentiation
    • Dengler HS, Baracho GV, Omori SA, Bruckner S, Arden KC, et al. 2008. Distinct functions for the transcription factor Foxo1 at various stages of B cell differentiation. Nat. Immunol. 9:1388-98
    • (2008) Nat. Immunol. , vol.9 , pp. 1388-1398
    • Dengler, H.S.1    Baracho, G.V.2    Omori, S.A.3    Bruckner, S.4    Arden, K.C.5
  • 137
    • 51549111249 scopus 로고    scopus 로고
    • FOXO1 regulates L-selectin and a network of human T cell homing molecules downstream of phosphatidylinositol 3-kinase
    • Fabre S, Carrette F, Chen J, Lang V, Semichon M, et al. 2008. FOXO1 regulates L-selectin and a network of human T cell homing molecules downstream of phosphatidylinositol 3-kinase. J. Immunol. 181:2980-89
    • (2008) J. Immunol. , vol.181 , pp. 2980-2989
    • Fabre, S.1    Carrette, F.2    Chen, J.3    Lang, V.4    Semichon, M.5
  • 139
    • 65249155463 scopus 로고    scopus 로고
    • Transcription factor Foxo3 controls the magnitude of T cell immune responses by modulating the function of dendritic cells
    • Dejean AS, Beisner DR, Ch'en IL, Kerdiles YM, Babour A, et al. 2009. Transcription factor Foxo3 controls the magnitude of T cell immune responses by modulating the function of dendritic cells. Nat. Immunol. 10:504-13
    • (2009) Nat. Immunol. , vol.10 , pp. 504-513
    • Dejean, A.S.1    Beisner, D.R.2    Ch'En, I.L.3    Kerdiles, Y.M.4    Babour, A.5
  • 140
    • 58449102260 scopus 로고    scopus 로고
    • Foxo1 links homing and survival of naive T cells by regulating L-selectin, CCR7 and interleukin 7 receptor
    • Kerdiles YM, Beisner DR, Tinoco R, Dejean AS, Castrillon DH, et al. 2009. Foxo1 links homing and survival of naive T cells by regulating L-selectin, CCR7 and interleukin 7 receptor. Nat. Immunol. 10:176-84
    • (2009) Nat. Immunol. , vol.10 , pp. 176-184
    • Kerdiles, Y.M.1    Beisner, D.R.2    Tinoco, R.3    Dejean, A.S.4    Castrillon, D.H.5
  • 141
    • 62049086102 scopus 로고    scopus 로고
    • An essential role of the Forkhead-box transcription factor Foxo1 in control of T cell homeostasis and tolerance
    • Ouyang W, Beckett O, Flavell RA, Li MO. 2009. An essential role of the Forkhead-box transcription factor Foxo1 in control of T cell homeostasis and tolerance. Immunity 30:358-71
    • (2009) Immunity , vol.30 , pp. 358-371
    • Ouyang, W.1    Beckett, O.2    Flavell, R.A.3    Li, M.O.4
  • 142
    • 77954417145 scopus 로고    scopus 로고
    • PI3 kinase signalling blocks Foxp3 expression by sequestering Foxo factors
    • Merkenschlager M, von Boehmer H. 2010. PI3 kinase signalling blocks Foxp3 expression by sequestering Foxo factors. J. Exp. Med. 207:1347-50
    • (2010) J. Exp. Med. , vol.207 , pp. 1347-1350
    • Merkenschlager, M.1    Von Boehmer, H.2
  • 144
    • 77953161581 scopus 로고    scopus 로고
    • Activation of FOXO3a is sufficient to reverse mitogen-activated protein/extracellular signal-regulated kinase kinase inhibitor chemoresistance in human cancer
    • Yang JY, Chang CJ, Xia W, Wang Y, Wong KK, et al. 2010. Activation of FOXO3a is sufficient to reverse mitogen-activated protein/extracellular signal-regulated kinase kinase inhibitor chemoresistance in human cancer. Cancer Res. 70:4709-18
    • (2010) Cancer Res. , vol.70 , pp. 4709-4718
    • Yang, J.Y.1    Chang, C.J.2    Xia, W.3    Wang, Y.4    Wong, K.K.5
  • 145
    • 84856927632 scopus 로고    scopus 로고
    • FoxO1 induces Ikaros splicing to promote immunoglobulin gene recombination
    • Alkhatib A, Werner M, Hug E, Herzog S, Eschbach C, et al. 2012. FoxO1 induces Ikaros splicing to promote immunoglobulin gene recombination. J. Exp. Med. 209:395-406
    • (2012) J. Exp. Med. , vol.209 , pp. 395-406
    • Alkhatib, A.1    Werner, M.2    Hug, E.3    Herzog, S.4    Eschbach, C.5
  • 146
    • 78649558664 scopus 로고    scopus 로고
    • MRNA degradation plays a significant role in the program of gene expression regulated by phosphatidylinositol 3-kinase signaling
    • Graham JR, Hendershott MC, Terragni J, Cooper GM. 2010. mRNA degradation plays a significant role in the program of gene expression regulated by phosphatidylinositol 3-kinase signaling. Mol. Cell. Biol. 30:5295-305
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 5295-5305
    • Graham, J.R.1    Hendershott, M.C.2    Terragni, J.3    Cooper, G.M.4
  • 147
    • 84859126410 scopus 로고    scopus 로고
    • Regulation of lymphocyte development and function by RNA-binding proteins
    • Turner M, Hodson D. 2012. Regulation of lymphocyte development and function by RNA-binding proteins. Curr. Opin. Immunol. 24:160-65
    • (2012) Curr. Opin. Immunol. , vol.24 , pp. 160-165
    • Turner, M.1    Hodson, D.2
  • 148
    • 84859778293 scopus 로고    scopus 로고
    • MTOR signaling in growth control and disease
    • Laplante M, Sabatini DM. 2012. mTOR signaling in growth control and disease. Cell 149:274-93
    • (2012) Cell , vol.149 , pp. 274-293
    • Laplante, M.1    Sabatini, D.M.2
  • 149
    • 33745307617 scopus 로고    scopus 로고
    • Ras, PI(3)K and mTOR signalling controls tumour cell growth
    • Shaw RJ, Cantley LC. 2006. Ras, PI(3)K and mTOR signalling controls tumour cell growth. Nature 441:424-30
    • (2006) Nature , vol.441 , pp. 424-430
    • Shaw, R.J.1    Cantley, L.C.2
  • 150
    • 73349119966 scopus 로고    scopus 로고
    • MAPK, phosphatidylinositol 3-kinase, and mammalian target of rapamycin pathways converge at the level of ribosomal protein S6 phosphorylation to control metabolic signaling in CD8 T cells
    • Salmond RJ, Emery J, Okkenhaug K, Zamoyska R. 2009. MAPK, phosphatidylinositol 3-kinase, and mammalian target of rapamycin pathways converge at the level of ribosomal protein S6 phosphorylation to control metabolic signaling in CD8 T cells. J. Immunol. 183:7388-97
    • (2009) J. Immunol. , vol.183 , pp. 7388-7397
    • Salmond, R.J.1    Emery, J.2    Okkenhaug, K.3    Zamoyska, R.4
  • 152
    • 77951768486 scopus 로고    scopus 로고
    • Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids
    • Sancak Y, Bar-Peled L, Zoncu R, Markhard AL, Nada S, et al. 2010. Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids. Cell 141:290-303
    • (2010) Cell , vol.141 , pp. 290-303
    • Sancak, Y.1    Bar-Peled, L.2    Zoncu, R.3    Markhard, A.L.4    Nada, S.5
  • 153
    • 45849105156 scopus 로고    scopus 로고
    • The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1
    • Sancak Y, Peterson TR, Shaul YD, Lindquist RA, Thoreen CC, et al. 2008. The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1. Science 320:1496-501
    • (2008) Science , vol.320 , pp. 1496-1501
    • Sancak, Y.1    Peterson, T.R.2    Shaul, Y.D.3    Lindquist, R.A.4    Thoreen, C.C.5
  • 154
    • 79958696694 scopus 로고    scopus 로고
    • The mTOR-regulated phosphoproteome reveals a mechanism of mTORC1-mediated inhibition of growth factor signaling
    • Hsu PP, Kang SA, Rameseder J, Zhang Y, Ottina KA, et al. 2011. The mTOR-regulated phosphoproteome reveals a mechanism of mTORC1-mediated inhibition of growth factor signaling. Science 332:1317-22
    • (2011) Science , vol.332 , pp. 1317-1322
    • Hsu, P.P.1    Kang, S.A.2    Rameseder, J.3    Zhang, Y.4    Ottina, K.A.5
  • 155
    • 79958696336 scopus 로고    scopus 로고
    • Phosphoproteomic analysis identifies Grb10 as an mTORC1 substrate that negatively regulates insulin signaling
    • Yu Y, Yoon SO, Poulogiannis G, Yang Q, Ma XM, et al. 2011. Phosphoproteomic analysis identifies Grb10 as an mTORC1 substrate that negatively regulates insulin signaling. Science 332:1322-26
    • (2011) Science , vol.332 , pp. 1322-1326
    • Yu, Y.1    Yoon, S.O.2    Poulogiannis, G.3    Yang, Q.4    Ma, X.M.5
  • 156
    • 79960369458 scopus 로고    scopus 로고
    • HIF1α-dependent glycolytic pathway orchestrates a metabolic checkpoint for the differentiation of TH17 and Treg cells
    • Shi LZ, Wang R, HuangG, Vogel P, Neale G, et al. 2011. HIF1α-dependent glycolytic pathway orchestrates a metabolic checkpoint for the differentiation of TH17 and Treg cells. J. Exp. Med. 208:1367-76
    • (2011) J. Exp. Med. , vol.208 , pp. 1367-1376
    • Shi, L.Z.1    Wang, R.2    Huang, G.3    Vogel, P.4    Neale, G.5
  • 157
    • 80052277906 scopus 로고    scopus 로고
    • Control of TH17/Treg balance by hypoxiainducible factor 1
    • Dang EV, Barbi J, Yang HY, Jinasena D, Yu H, et al. 2011. Control of TH17/Treg balance by hypoxiainducible factor 1. Cell 146:772-84
    • (2011) Cell , vol.146 , pp. 772-784
    • Dang, E.V.1    Barbi, J.2    Yang, H.Y.3    Jinasena, D.4    Yu, H.5
  • 158
    • 33646023695 scopus 로고    scopus 로고
    • Prolonged rapamycin treatment inhibits mTORC2 assembly and Akt/PKB
    • Sarbassov DD, Ali SM, Sengupta S, Sheen JH, Hsu PP, et al. 2006. Prolonged rapamycin treatment inhibits mTORC2 assembly and Akt/PKB. Mol. Cell 22:159-68
    • (2006) Mol. Cell , vol.22 , pp. 159-168
    • Sarbassov, D.D.1    Ali, S.M.2    Sengupta, S.3    Sheen, J.H.4    Hsu, P.P.5
  • 161
    • 0031471231 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase-γ activates Bruton's tyrosine kinase in concert with Src family kinases
    • Li Z, Wahl MI, Eguinoa A, Stephens LR, Hawkins PT, et al. 1997. Phosphatidylinositol 3-kinase-γ activates Bruton's tyrosine kinase in concert with Src family kinases. Proc. Natl. Acad. Sci. USA 94:13820-25
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13820-13825
    • Li, Z.1    Wahl, M.I.2    Eguinoa, A.3    Stephens, L.R.4    Hawkins, P.T.5
  • 162
    • 0037341617 scopus 로고    scopus 로고
    • PI3K and Btk differentially regulate B cell antigen receptor-mediated signal transduction
    • Suzuki H, Matsuda S, Terauchi Y, Fujiwara M, Ohteki T, et al. 2003. PI3K and Btk differentially regulate B cell antigen receptor-mediated signal transduction. Nat. Immunol. 4:280-86
    • (2003) Nat. Immunol. , vol.4 , pp. 280-286
    • Suzuki, H.1    Matsuda, S.2    Terauchi, Y.3    Fujiwara, M.4    Ohteki, T.5
  • 163
    • 60849117518 scopus 로고    scopus 로고
    • Critical role of class IA PI3K for c-Rel expression in B lymphocytes
    • Matsuda S, Mikami Y, Ohtani M, Fujiwara M, Hirata Y, et al. 2009. Critical role of class IA PI3K for c-Rel expression in B lymphocytes. Blood 113:1037-44
    • (2009) Blood , vol.113 , pp. 1037-1044
    • Matsuda, S.1    Mikami, Y.2    Ohtani, M.3    Fujiwara, M.4    Hirata, Y.5
  • 165
    • 0037155727 scopus 로고    scopus 로고
    • P-Rex1, a PtdIns(3, 4, 5)P3-and Gβγ-regulated guanine-nucleotide exchange factor for Rac
    • Welch HC, CoadwellWJ, Ellson CD, Ferguson GJ, Andrews SR, et al. 2002. P-Rex1, a PtdIns(3, 4, 5)P3-and Gβγ-regulated guanine-nucleotide exchange factor for Rac. Cell 108:809-21
    • (2002) Cell , vol.108 , pp. 809-821
    • Welch, H.C.1    Coadwell, W.J.2    Ellson, C.D.3    Ferguson, G.J.4    Andrews, S.R.5
  • 166
    • 23744492188 scopus 로고    scopus 로고
    • Sequential activation of class IB and class IA PI3K is important for the primed respiratory burst of human but not murine neutrophils
    • Condliffe AM, Davidson K, Anderson KE, Ellson CD, Crabbe T, et al. 2005. Sequential activation of class IB and class IA PI3K is important for the primed respiratory burst of human but not murine neutrophils. Blood 106:1432-40
    • (2005) Blood , vol.106 , pp. 1432-1440
    • Condliffe, A.M.1    Davidson, K.2    Anderson, K.E.3    Ellson, C.D.4    Crabbe, T.5
  • 167
    • 79251573248 scopus 로고    scopus 로고
    • P-Rex1 and Vav1 cooperate in the regulation of formyl-methionyl-leucyl- phenylalanine-dependent neutrophil responses
    • Lawson CD, Donald S, Anderson KE, Patton DT, Welch HC. 2011. P-Rex1 and Vav1 cooperate in the regulation of formyl-methionyl-leucyl-phenylalanine- dependent neutrophil responses. J. Immunol. 186:1467-76
    • (2011) J. Immunol. , vol.186 , pp. 1467-1476
    • Lawson, C.D.1    Donald, S.2    Anderson, K.E.3    Patton, D.T.4    Welch, H.C.5
  • 168
    • 77649214306 scopus 로고    scopus 로고
    • Function of the nucleotide exchange activity of Vav1 in T cell development and activation
    • Saveliev A, Vanes L, Ksionda O, Rapley J, Smerdon SJ, et al. 2009. Function of the nucleotide exchange activity of Vav1 in T cell development and activation. Sci. Signal. 2:ra83
    • (2009) Sci. Signal. , vol.2
    • Saveliev, A.1    Vanes, L.2    Ksionda, O.3    Rapley, J.4    Smerdon, S.J.5
  • 169
    • 35448938870 scopus 로고    scopus 로고
    • Negative feedback regulation of Rac in leukocytes from mice expressing a constitutively active phosphatidylinositol 3-kinase γ
    • Costa C, Barberis L, Ambrogio C, Manazza AD, Patrucco E, et al. 2007. Negative feedback regulation of Rac in leukocytes from mice expressing a constitutively active phosphatidylinositol 3-kinase γ. Proc. Natl. Acad. Sci. USA 104:14354-59
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 14354-14359
    • Costa, C.1    Barberis, L.2    Ambrogio, C.3    Manazza, A.D.4    Patrucco, E.5
  • 170
    • 79961006795 scopus 로고    scopus 로고
    • The RacGAP ArhGAP15 is a master negative regulator of neutrophil functions
    • Costa C, Germena G, Martin-Conte EL, Molineris I, Bosco E, et al. 2011. The RacGAP ArhGAP15 is a master negative regulator of neutrophil functions. Blood 118:1099-108
    • (2011) Blood , vol.118 , pp. 1099-1108
    • Costa, C.1    Germena, G.2    Martin-Conte, E.L.3    Molineris, I.4    Bosco, E.5
  • 171
    • 70450237753 scopus 로고    scopus 로고
    • ARAP3 binding to phosphatidylinositol-(3, 4, 5)-trisphosphate depends on N-terminal tandemPHdomains and adjacent sequences
    • Craig HE, Coadwell J, Guillou H, Vermeren S. 2010. ARAP3 binding to phosphatidylinositol-(3, 4, 5)-trisphosphate depends on N-terminal tandemPHdomains and adjacent sequences. Cell Signal. 22:257-64
    • (2010) Cell Signal. , vol.22 , pp. 257-264
    • Craig, H.E.1    Coadwell, J.2    Guillou, H.3    Vermeren, S.4
  • 172
    • 79961010009 scopus 로고    scopus 로고
    • TheGTPaseactivating protein ARAP3 regulates chemotaxis and adhesion-dependent processes in neutrophils
    • Gambardella L, Anderson KE, NussbaumC, Segonds-Pichon A, MargaridoT, et al. 2011. TheGTPaseactivating protein ARAP3 regulates chemotaxis and adhesion-dependent processes in neutrophils. Blood 118:1087-98
    • (2011) Blood , vol.118 , pp. 1087-1098
    • Gambardella, L.1    Anderson, K.E.2    Nussbaum, C.3    Segonds-Pichon, A.4    Margarido, T.5
  • 173
    • 84857875585 scopus 로고    scopus 로고
    • PI3K signalling in B-and T-lymphocytes: New developments and therapeutic advances
    • So L, Fruman DA. 2012. PI3K signalling in B-and T-lymphocytes: new developments and therapeutic advances. Biochem. J. 442:465-81
    • (2012) Biochem. J. , vol.442 , pp. 465-481
    • So, L.1    Fruman, D.A.2
  • 175
    • 61849126233 scopus 로고    scopus 로고
    • Fine tuning the immune response with PI3K
    • Fruman DA, Bismuth G. 2009. Fine tuning the immune response with PI3K. Immunol. Rev. 228:253-72
    • (2009) Immunol. Rev. , vol.228 , pp. 253-272
    • Fruman, D.A.1    Bismuth, G.2
  • 176
    • 0038549067 scopus 로고    scopus 로고
    • PI3K in lymphocyte development, differentiation and activation
    • Okkenhaug K, VanhaesebroeckB. 2003. PI3K in lymphocyte development, differentiation and activation. Nat. Rev. Immunol. 3:317-30
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 317-330
    • Okkenhaug, K.1    Vanhaesebroeck, B.2
  • 177
    • 1342292522 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase: Diverse roles in immune cell activation
    • Deane JA, Fruman DA. 2004. Phosphoinositide 3-kinase: diverse roles in immune cell activation. Annu. Rev. Immunol. 22:563-98
    • (2004) Annu. Rev. Immunol. , vol.22 , pp. 563-598
    • Deane, J.A.1    Fruman, D.A.2
  • 178
    • 0037374815 scopus 로고    scopus 로고
    • The role of PI3K in immune cells
    • Koyasu S. 2003. The role of PI3K in immune cells. Nat. Immunol. 4:313-19
    • (2003) Nat. Immunol. , vol.4 , pp. 313-319
    • Koyasu, S.1
  • 179
    • 33646376411 scopus 로고    scopus 로고
    • Pten dependence distinguishes haematopoietic stem cells from leukaemia-initiating cells
    • Yilmaz OH, Valdez R, Theisen BK, GuoW, Ferguson DO, et al. 2006. Pten dependence distinguishes haematopoietic stem cells from leukaemia-initiating cells. Nature 441:475-82
    • (2006) Nature , vol.441 , pp. 475-482
    • Yilmaz, O.H.1    Valdez, R.2    Theisen, B.K.3    Guo, W.4    Ferguson, D.O.5
  • 180
    • 33646351002 scopus 로고    scopus 로고
    • PTEN maintains haematopoietic stem cells and acts in lineage choice and leukaemia prevention
    • Zhang J, Grindley JC, Yin T, Jayasinghe S, He XC, et al. 2006. PTEN maintains haematopoietic stem cells and acts in lineage choice and leukaemia prevention. Nature 441:518-22
    • (2006) Nature , vol.441 , pp. 518-522
    • Zhang, J.1    Grindley, J.C.2    Yin, T.3    Jayasinghe, S.4    He, X.C.5
  • 181
    • 33846419112 scopus 로고    scopus 로고
    • FoxOs are critical mediators of hematopoietic stem cell resistance to physiologic oxidative stress
    • Tothova Z, Kollipara R, Huntly BJ, Lee BH, Castrillon DH, et al. 2007. FoxOs are critical mediators of hematopoietic stem cell resistance to physiologic oxidative stress. Cell 128:325-39
    • (2007) Cell , vol.128 , pp. 325-339
    • Tothova, Z.1    Kollipara, R.2    Huntly, B.J.3    Lee, B.H.4    Castrillon, D.H.5
  • 182
    • 61349179407 scopus 로고    scopus 로고
    • Regulation of B-cell proliferation and differentiation by pre-B-cell receptor signalling
    • Herzog S, Reth M, Jumaa H. 2009. Regulation of B-cell proliferation and differentiation by pre-B-cell receptor signalling. Nat. Rev. Immunol. 9:195-205
    • (2009) Nat. Rev. Immunol. , vol.9 , pp. 195-205
    • Herzog, S.1    Reth, M.2    Jumaa, H.3
  • 183
    • 0029983731 scopus 로고    scopus 로고
    • The interleukin-7 receptor αchain transmits distinct signals for proliferation and differentiation during B lymphopoiesis
    • Corcoran AE, Smart FM, Cowling RJ, Crompton T, Owen MJ, et al. 1996. The interleukin-7 receptor αchain transmits distinct signals for proliferation and differentiation during B lymphopoiesis. EMBO J. 15:1924-32
    • (1996) EMBO J. , vol.15 , pp. 1924-1932
    • Corcoran, A.E.1    Smart, F.M.2    Cowling, R.J.3    Crompton, T.4    Owen, M.J.5
  • 184
    • 77954243830 scopus 로고    scopus 로고
    • Selective ablation of the YxxM motif of IL-7Rαsuppresses lymphomagenesis but maintains lymphocyte development
    • Osborne LC, DuthieKA, Seo JH, Gascoyne RD, Abraham N. 2010. Selective ablation of the YxxM motif of IL-7Rαsuppresses lymphomagenesis but maintains lymphocyte development. Oncogene 29:3854-64
    • (2010) Oncogene , vol.29 , pp. 3854-3864
    • Osborne, L.C.1    Duthie, K.A.2    Seo, J.H.3    Gascoyne, R.D.4    Abraham, N.5
  • 185
    • 0032402316 scopus 로고    scopus 로고
    • Modulation of the IL-7 dose-response threshold during pro-B cell differentiation is dependent on pre-B cell receptor expression
    • Marshall AJ, Fleming HE, Wu GE, Paige CJ. 1998. Modulation of the IL-7 dose-response threshold during pro-B cell differentiation is dependent on pre-B cell receptor expression. J. Immunol. 161:6038-45
    • (1998) J. Immunol. , vol.161 , pp. 6038-6045
    • Marshall, A.J.1    Fleming, H.E.2    Wu, G.E.3    Paige, C.J.4
  • 186
    • 44049101651 scopus 로고    scopus 로고
    • SLP-65 regulates immunoglobulin light chain gene recombination through the PI(3)K-PKB-Foxo pathway
    • Herzog S, Hug E, Meixlsperger S, Paik JH, DePinho RA, et al. 2008. SLP-65 regulates immunoglobulin light chain gene recombination through the PI(3)K-PKB-Foxo pathway. Nat. Immunol. 9:623-31
    • (2008) Nat. Immunol. , vol.9 , pp. 623-631
    • Herzog, S.1    Hug, E.2    Meixlsperger, S.3    Paik, J.H.4    De Pinho, R.A.5
  • 187
    • 77955876805 scopus 로고    scopus 로고
    • Role of PI3K in the generation and survival of B cells
    • Werner M, Hobeika E, Jumaa H. 2010. Role of PI3K in the generation and survival of B cells. Immunol. Rev. 237:55-71
    • (2010) Immunol. Rev. , vol.237 , pp. 55-71
    • Werner, M.1    Hobeika, E.2    Jumaa, H.3
  • 188
    • 33846895443 scopus 로고    scopus 로고
    • The PI3K p110∞ is required for down-regulation of RAG expression in immature B cells
    • Llorian M, Stamataki Z, Hill S, Turner M, Martensson IL. 2007. The PI3K p110∞ is required for down-regulation of RAG expression in immature B cells. J. Immunol. 178:1981-85
    • (2007) J. Immunol. , vol.178 , pp. 1981-1985
    • Llorian, M.1    Stamataki, Z.2    Hill, S.3    Turner, M.4    Martensson, I.L.5
  • 189
    • 34248216554 scopus 로고    scopus 로고
    • Basal B cell receptor-directed phosphatidylinositol 3-kinase signaling turns off RAGs and promotes B cell-positive selection
    • Verkoczy L, Duong B, Skog P, Ait-AzzouzeneD, Puri K, et al. 2007. Basal B cell receptor-directed phosphatidylinositol 3-kinase signaling turns off RAGs and promotes B cell-positive selection. J. Immunol. 178:6332-41
    • (2007) J. Immunol. , vol.178 , pp. 6332-6341
    • Verkoczy, L.1    Duong, B.2    Skog, P.3    Ait-Azzouzene, D.4    Puri, K.5
  • 190
    • 20944435721 scopus 로고    scopus 로고
    • Basal immunoglobulin signaling actively maintains developmental stage in immature B cells
    • Tze LE, Schram BR, Lam KP, Hogquist KA, Hippen KL, et al. 2005. Basal immunoglobulin signaling actively maintains developmental stage in immature B cells. PLoS Biol. 3:e82
    • (2005) PLoS Biol. , vol.3
    • Tze, L.E.1    Schram, B.R.2    Lam, K.P.3    Hogquist, K.A.4    Hippen, K.L.5
  • 191
    • 0342711256 scopus 로고    scopus 로고
    • In vivo ablation of surface immunoglobulin on mature B cells by inducible gene targeting results in rapid cell death
    • Lam KP, Kuhn R, Rajewsky K. 1997. In vivo ablation of surface immunoglobulin on mature B cells by inducible gene targeting results in rapid cell death. Cell 90:1073-83
    • (1997) Cell , vol.90 , pp. 1073-1083
    • Lam, K.P.1    Kuhn, R.2    Rajewsky, K.3
  • 192
    • 2942582913 scopus 로고    scopus 로고
    • Survival of resting mature B lymphocytes depends on BCR signaling via the Igα/βheterodimer
    • Kraus M, Alimzhanov MB, Rajewsky N, Rajewsky K. 2004. Survival of resting mature B lymphocytes depends on BCR signaling via the Igα/ βheterodimer. Cell 117:787-800
    • (2004) Cell , vol.117 , pp. 787-800
    • Kraus, M.1    Alimzhanov, M.B.2    Rajewsky, N.3    Rajewsky, K.4
  • 193
    • 70350304558 scopus 로고    scopus 로고
    • PI3 kinase signals BCR-dependent mature B cell survival
    • Srinivasan L, Sasaki Y, Calado DP, Zhang B, Paik JH, et al. 2009. PI3 kinase signals BCR-dependent mature B cell survival. Cell 139:573-86
    • (2009) Cell , vol.139 , pp. 573-586
    • Srinivasan, L.1    Sasaki, Y.2    Calado, D.P.3    Zhang, B.4    Paik, J.H.5
  • 194
    • 38949150779 scopus 로고    scopus 로고
    • CD28 provides T-cell costimulation and enhances PI3K activity at the immune synapse independently of its capacity to interact with the p85/p110 heterodimer
    • Garcon F, Patton DT, Emery JL, Hirsch E, Rottapel R, et al. 2008. CD28 provides T-cell costimulation and enhances PI3K activity at the immune synapse independently of its capacity to interact with the p85/p110 heterodimer. Blood 111:1464-71
    • (2008) Blood , vol.111 , pp. 1464-1471
    • Garcon, F.1    Patton, D.T.2    Emery, J.L.3    Hirsch, E.4    Rottapel, R.5
  • 195
    • 76349098519 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase p110∞ regulates natural antibody production, marginal zone and B-1 B cell function, and autoantibody responses
    • Durand CA, Hartvigsen K, Fogelstrand L, Kim S, Iritani S, et al. 2009. Phosphoinositide 3-kinase p110∞ regulates natural antibody production, marginal zone and B-1 B cell function, and autoantibody responses. J. Immunol. 183:5673-84
    • (2009) J. Immunol. , vol.183 , pp. 5673-5684
    • Durand, C.A.1    Hartvigsen, K.2    Fogelstrand, L.3    Kim, S.4    Iritani, S.5
  • 196
    • 77958134778 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase activity in T cells regulates the magnitude of the germinal center reaction
    • Rolf J, Bell SE, Kovesdi D, Janas ML, Soond DR, et al. 2010. Phosphoinositide 3-kinase activity in T cells regulates the magnitude of the germinal center reaction. J. Immunol. 185:4042-52
    • (2010) J. Immunol. , vol.185 , pp. 4042-4052
    • Rolf, J.1    Bell, S.E.2    Kovesdi, D.3    Janas, M.L.4    Soond, D.R.5
  • 197
    • 84860330649 scopus 로고    scopus 로고
    • P110∞ phosphoinositide 3-kinase represses IgE switch by potentiating BCL6 expression
    • Zhang TT, Makondo KJ, Marshall AJ. 2012. p110∞ phosphoinositide 3-kinase represses IgE switch by potentiating BCL6 expression. J. Immunol. 188:3700-8
    • (2012) J. Immunol. , vol.188 , pp. 3700-3708
    • Zhang, T.T.1    Makondo, K.J.2    Marshall, A.J.3
  • 198
    • 53049098169 scopus 로고    scopus 로고
    • Genetic or pharmaceutical blockade of p110∞ phosphoinositide 3-kinase enhances IgE production
    • Zhang TT, Okkenhaug K, Nashed BF, Puri KD, Knight ZA, et al. 2008. Genetic or pharmaceutical blockade of p110∞ phosphoinositide 3-kinase enhances IgE production. J. Allergy Clin. Immunol. 122:811-19.e2
    • (2008) J. Allergy Clin. Immunol. , vol.122
    • Zhang, T.T.1    Okkenhaug, K.2    Nashed, B.F.3    Puri, K.D.4    Knight, Z.A.5
  • 199
    • 84861692916 scopus 로고    scopus 로고
    • B cell receptor signal transduction in the GC is shortcircuited by high phosphatase activity
    • Khalil AM, Cambier JC, Shlomchik MJ. 2012. B cell receptor signal transduction in the GC is shortcircuited by high phosphatase activity. Science 336:1178-81
    • (2012) Science , vol.336 , pp. 1178-1181
    • Khalil, A.M.1    Cambier, J.C.2    Shlomchik, M.J.3
  • 200
    • 33947595612 scopus 로고    scopus 로고
    • T-cell function is partially maintained in the absence of class IA phosphoinositide 3-kinase signaling
    • Deane JA, Kharas MG, Oak JS, Stiles LN, Luo J, et al. 2007. T-cell function is partially maintained in the absence of class IA phosphoinositide 3-kinase signaling. Blood 109:2894-902
    • (2007) Blood , vol.109 , pp. 2894-2902
    • Deane, J.A.1    Kharas, M.G.2    Oak, J.S.3    Stiles, L.N.4    Luo, J.5
  • 201
    • 77957264936 scopus 로고    scopus 로고
    • Stromal cell-derived factor 1α and CXCR4: Newly defined requirements for efficient thymic β-selection
    • Janas ML, Turner M. 2010. Stromal cell-derived factor 1α and CXCR4: newly defined requirements for efficient thymic β-selection. Trends Immunol. 31:370-76
    • (2010) Trends Immunol. , vol.31 , pp. 370-376
    • Janas, M.L.1    Turner, M.2
  • 202
    • 5444269438 scopus 로고    scopus 로고
    • The loss of PTEN allows TCR αβlineage thymocytes to bypass IL-7 and Pre-TCR-mediated signaling
    • Hagenbeek TJ, Naspetti M, Malergue F, Garcon F, Nunes JA, et al. 2004. The loss of PTEN allows TCR αβlineage thymocytes to bypass IL-7 and Pre-TCR-mediated signaling. J. Exp.Med. 200:883-94
    • (2004) J. Exp.Med. , vol.200 , pp. 883-894
    • Hagenbeek, T.J.1    Naspetti, M.2    Malergue, F.3    Garcon, F.4    Nunes, J.A.5
  • 203
    • 76149086153 scopus 로고    scopus 로고
    • Thymic development beyond β-selection requires phosphatidylinositol 3-kinase activation by CXCR4
    • JanasML, VaranoG, Gudmundsson K, Noda M, Nagasawa T, et al. 2010. Thymic development beyond β-selection requires phosphatidylinositol 3-kinase activation by CXCR4. J. Exp. Med. 207:247-61
    • (2010) J. Exp. Med. , vol.207 , pp. 247-261
    • Janas, M.L.1    Varano, G.2    Gudmundsson, K.3    Noda, M.4    Nagasawa, T.5
  • 204
    • 23844462453 scopus 로고    scopus 로고
    • Cutting edge: T cell development requires the combined activities of the p110γ and p110∞ catalytic isoforms of phosphatidylinositol 3-kinase
    • Webb LM, Vigorito E, Wymann MP, Hirsch E, Turner M. 2005. Cutting edge: T cell development requires the combined activities of the p110γ and p110∞ catalytic isoforms of phosphatidylinositol 3-kinase. J. Immunol. 175:2783-87
    • (2005) J. Immunol. , vol.175 , pp. 2783-2787
    • Webb, L.M.1    Vigorito, E.2    Wymann, M.P.3    Hirsch, E.4    Turner, M.5
  • 205
    • 35548996385 scopus 로고    scopus 로고
    • Inactivation of PI3Kγ and PI3K∞ distorts T-cell development and causes multiple organ inflammation
    • Ji H, Rintelen F, Waltzinger C, Bertschy Meier D, Bilancio A, et al. 2007. Inactivation of PI3Kγ and PI3K∞ distorts T-cell development and causes multiple organ inflammation. Blood 110:2940-47
    • (2007) Blood , vol.110 , pp. 2940-2947
    • Ji, H.1    Rintelen, F.2    Waltzinger, C.3    Bertschy Meier, D.4    Bilancio, A.5
  • 206
    • 33644765808 scopus 로고    scopus 로고
    • Essential role of PI3K∞ and PI3Kγin thymocyte survival
    • Swat W, Montgrain V, Doggett TA, Douangpanya J, Puri K, et al. 2006. Essential role of PI3K∞ and PI3Kγin thymocyte survival. Blood 107:2415-22
    • (2006) Blood , vol.107 , pp. 2415-2422
    • Swat, W.1    Montgrain, V.2    Doggett, T.A.3    Douangpanya, J.4    Puri, K.5
  • 207
    • 34547208593 scopus 로고    scopus 로고
    • Notch-induced T cell development requires phosphoinositide-dependent kinase 1
    • Kelly AP, Finlay DK, Hinton HJ, Clarke RG, Fiorini E, et al. 2007. Notch-induced T cell development requires phosphoinositide-dependent kinase 1. EMBO J. 26:3441-50
    • (2007) EMBO J. , vol.26 , pp. 3441-3450
    • Kelly, A.P.1    Finlay, D.K.2    Hinton, H.J.3    Clarke, R.G.4    Fiorini, E.5
  • 208
    • 24944444760 scopus 로고    scopus 로고
    • Notch promotes survival of pre-T cells at the β-selection checkpoint by regulating cellular metabolism
    • Ciofani M, Zuniga-Pflucker JC. 2005. Notch promotes survival of pre-T cells at the β-selection checkpoint by regulating cellular metabolism. Nat. Immunol. 6:881-88
    • (2005) Nat. Immunol. , vol.6 , pp. 881-888
    • Ciofani, M.1    Zuniga-Pflucker, J.C.2
  • 209
    • 84865160657 scopus 로고    scopus 로고
    • HES1 opposes a PTENdependent check on survival, differentiation and proliferation of TCRβ-selected mouse thymocytes
    • Wong GW, Knowles GC, Mak TW, Ferrando AA, Zuniga-Pflücker JC. 2012. HES1 opposes a PTENdependent check on survival, differentiation and proliferation of TCRβ-selected mouse thymocytes. Blood 120:1439-48
    • (2012) Blood , vol.120 , pp. 1439-1448
    • Wong, G.W.1    Knowles, G.C.2    Mak, T.W.3    Ferrando, A.A.4    Zuniga-Pflücker, J.C.5
  • 210
    • 84864401500 scopus 로고    scopus 로고
    • Distinct spatial andmolecular features of Notch pathway assembly in regulatory T cells
    • Perumalsamy LR, Marcel N, Kulkarni S, Radtke F, Sarin A. 2012. Distinct spatial andmolecular features of Notch pathway assembly in regulatory T cells. Sci. Signal. 5:ra53
    • (2012) Sci. Signal. , vol.5
    • Perumalsamy, L.R.1    Marcel, N.2    Kulkarni, S.3    Radtke, F.4    Sarin, A.5
  • 211
    • 40149099723 scopus 로고    scopus 로고
    • Critical roles of the PI3K/Akt signaling pathway inTcell development
    • JuntillaMM, Koretzky GA. 2008. Critical roles of the PI3K/Akt signaling pathway inTcell development. Immunol. Lett. 116:104-10
    • (2008) Immunol. Lett. , vol.116 , pp. 104-110
    • Juntilla, M.M.1    Koretzky, G.A.2
  • 212
    • 2442681621 scopus 로고    scopus 로고
    • The serine kinase phosphoinositide-dependent kinase 1 (PDK1) regulates T cell development
    • Hinton HJ, Alessi DR, Cantrell DA. 2004. The serine kinase phosphoinositide-dependent kinase 1 (PDK1) regulates T cell development. Nat. Immunol. 5:539-45
    • (2004) Nat. Immunol. , vol.5 , pp. 539-545
    • Hinton, H.J.1    Alessi, D.R.2    Cantrell, D.A.3
  • 213
    • 70449471819 scopus 로고    scopus 로고
    • Phosphoinositide-dependent kinase 1 controlsmigration andmalignant transformation but not cell growth and proliferation inPTENnull lymphocytes
    • Finlay DK, Sinclair LV, Feijoo C, Waugh CM, Hagenbeek TJ, et al. 2009. Phosphoinositide-dependent kinase 1 controlsmigration andmalignant transformation but not cell growth and proliferation inPTENnull lymphocytes. J. Exp. Med. 206:2441-54
    • (2009) J. Exp. Med. , vol.206 , pp. 2441-2454
    • Finlay, D.K.1    Sinclair, L.V.2    Feijoo, C.3    Waugh, C.M.4    Hagenbeek, T.J.5
  • 214
    • 0347505003 scopus 로고    scopus 로고
    • CD28-mediated co-stimulation: A quantitative support for TCR signalling
    • Acuto O, Michel F. 2003. CD28-mediated co-stimulation: a quantitative support for TCR signalling. Nat. Rev. Immunol. 3:939-51
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 939-951
    • Acuto, O.1    Michel, F.2
  • 215
    • 0033517125 scopus 로고    scopus 로고
    • Proline residues in CD28 and the Src homology (SH)3 domain of Lck are required for T cell costimulation
    • Holdorf AD, Green JM, Levin SD, Denny MF, Straus DB, et al. 1999. Proline residues in CD28 and the Src homology (SH)3 domain of Lck are required for T cell costimulation. J. Exp. Med. 190:375-84
    • (1999) J. Exp. Med. , vol.190 , pp. 375-384
    • Holdorf, A.D.1    Green, J.M.2    Levin, S.D.3    Denny, M.F.4    Straus, D.B.5
  • 216
    • 73949090666 scopus 로고    scopus 로고
    • Inducible costimulator promotes helper T-cell differentiation through phosphoinositide 3-kinase
    • Gigoux M, Shang J, Pak Y, Xu M, Choe J, et al. 2009. Inducible costimulator promotes helper T-cell differentiation through phosphoinositide 3-kinase. Proc. Natl. Acad. Sci. USA 106:20371-76
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 20371-20376
    • Gigoux, M.1    Shang, J.2    Pak, Y.3    Xu, M.4    Choe, J.5
  • 217
    • 29644443728 scopus 로고    scopus 로고
    • Class IBphosphatidylinositol 3-kinase (PI3K) deficiency ameliorates IA-PI3K-induced systemic lupus but not T cell invasion
    • Barber DF, Bartolome A, Hernandez C, Flores JM, Fernandez-Arias C, et al. 2006. Class IBphosphatidylinositol 3-kinase (PI3K) deficiency ameliorates IA-PI3K-induced systemic lupus but not T cell invasion. J. Immunol. 176:589-93
    • (2006) J. Immunol. , vol.176 , pp. 589-593
    • Barber, D.F.1    Bartolome, A.2    Hernandez, C.3    Flores, J.M.4    Fernandez-Arias, C.5
  • 218
    • 42149156057 scopus 로고    scopus 로고
    • Selective regulation of CD8 effector T cell migration by the p110γisoform of phosphatidylinositol 3-kinase
    • Martin AL, Schwartz MD, Jameson SC, Shimizu Y. 2008. Selective regulation of CD8 effector T cell migration by the p110γisoform of phosphatidylinositol 3-kinase. J. Immunol. 180:2081-88
    • (2008) J. Immunol. , vol.180 , pp. 2081-2088
    • Martin, A.L.1    Schwartz, M.D.2    Jameson, S.C.3    Shimizu, Y.4
  • 219
    • 50849122062 scopus 로고    scopus 로고
    • The p110γ isoform of phosphatidylinositol 3-kinase regulates migration of effector CD4 T lymphocytes into peripheral inflammatory sites
    • Thomas MS, Mitchell JS, DeNucci CC, Martin AL, Shimizu Y. 2008. The p110γ isoform of phosphatidylinositol 3-kinase regulates migration of effector CD4 T lymphocytes into peripheral inflammatory sites. J. Leukoc. Biol. 84:814-23
    • (2008) J. Leukoc. Biol. , vol.84 , pp. 814-823
    • Thomas, M.S.1    Mitchell, J.S.2    De Nucci, C.C.3    Martin, A.L.4    Shimizu, Y.5
  • 220
    • 4444335344 scopus 로고    scopus 로고
    • Differential requirements for DOCK2 and phosphoinositide-3-kinase γ during T and B lymphocyte homing
    • Nombela-Arrieta C, Lacalle RA, Montoya MC, Kunisaki Y, Megias D, et al. 2004. Differential requirements for DOCK2 and phosphoinositide-3-kinase γ during T and B lymphocyte homing. Immunity 21:429-41
    • (2004) Immunity , vol.21 , pp. 429-441
    • Nombela-Arrieta, C.1    Lacalle, R.A.2    Montoya, M.C.3    Kunisaki, Y.4    Megias, D.5
  • 221
    • 33749515632 scopus 로고    scopus 로고
    • The p110∞ isoform of phosphoinositide 3-kinase controls clonal expansion and differentiation of Th cells
    • Okkenhaug K, Patton DT, Bilancio A, Garcon F, RowanWC, et al. 2006. The p110∞ isoform of phosphoinositide 3-kinase controls clonal expansion and differentiation of Th cells. J. Immunol. 177:5122-28
    • (2006) J. Immunol. , vol.177 , pp. 5122-5128
    • Okkenhaug, K.1    Patton, D.T.2    Bilancio, A.3    Garcon, F.4    Rowan, W.C.5
  • 222
    • 77950457187 scopus 로고    scopus 로고
    • PI3K p110∞regulates T-cell cytokine production during primary and secondary immune responses in mice and humans
    • Soond DR, Bjorgo E, Moltu K, Dale VQ, Patton DT, et al. 2010. PI3K p110∞regulates T-cell cytokine production during primary and secondary immune responses in mice and humans. Blood 115:2203-13
    • (2010) Blood , vol.115 , pp. 2203-2213
    • Soond, D.R.1    Bjorgo, E.2    Moltu, K.3    Dale, V.Q.4    Patton, D.T.5
  • 223
    • 79954603523 scopus 로고    scopus 로고
    • PI3K∞drives the pathogenesis of experimental autoimmune encephalomyelitis by inhibiting effector T cell apoptosis and promoting Th17 differentiation
    • Haylock-Jacobs S, Comerford I, Bunting M, Kara E, Townley S, et al. 2011. PI3K∞drives the pathogenesis of experimental autoimmune encephalomyelitis by inhibiting effector T cell apoptosis and promoting Th17 differentiation. J. Autoimmun. 36:278-87
    • (2011) J. Autoimmun. , vol.36 , pp. 278-287
    • Haylock-Jacobs, S.1    Comerford, I.2    Bunting, M.3    Kara, E.4    Townley, S.5
  • 224
    • 33947729717 scopus 로고    scopus 로고
    • Role of the phosphoinositide 3-kinase p110∞ in generation of type 2 cytokine responses and allergic airway inflammation
    • Nashed BF, Zhang T, Al-Alwan M, Srinivasan G, Halayko AJ, et al. 2007. Role of the phosphoinositide 3-kinase p110∞ in generation of type 2 cytokine responses and allergic airway inflammation. Eur. J. Immunol. 37:416-24
    • (2007) Eur. J. Immunol. , vol.37 , pp. 416-424
    • Nashed, B.F.1    Zhang, T.2    Al-Alwan, M.3    Srinivasan, G.4    Halayko, A.J.5
  • 225
    • 84861134382 scopus 로고    scopus 로고
    • PI3K-Akt-mTORC1-S6K1/2 axis controls Th17 differentiation by regulating Gfi1 expression and nuclear translocation of RORγ
    • Kurebayashi Y, Nagai S, Ikejiri A, OhtaniM, Ichiyama K, et al. 2012. PI3K-Akt-mTORC1-S6K1/2 axis controls Th17 differentiation by regulating Gfi1 expression and nuclear translocation of RORγ. Cell Rep. 1:360-73
    • (2012) Cell Rep. , vol.1 , pp. 360-373
    • Kurebayashi, Y.1    Nagai, S.2    Ikejiri, A.3    Ohtanim Ichiyama, K.4
  • 226
    • 33847239467 scopus 로고    scopus 로고
    • PI3K∞ and PI3Kγ: Partners in crime in inflammation in rheumatoid arthritis and beyond?
    • Rommel C, Camps M, Ji H. 2007. PI3K∞ and PI3Kγ: partners in crime in inflammation in rheumatoid arthritis and beyond? Nat. Rev. Immunol. 7:191-201
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 191-201
    • Rommel, C.1    Camps, M.2    Ji, H.3
  • 227
    • 84870984149 scopus 로고    scopus 로고
    • The therapeutic potential for PI3K inhibitors in autoimmune rheumatic diseases
    • Banham-Hall E, Clatworthy MR, Okkenhaug K. 2012. The therapeutic potential for PI3K inhibitors in autoimmune rheumatic diseases. Open Rheumatol. J. 6:245-58
    • (2012) Open Rheumatol. J. , vol.6 , pp. 245-258
    • Banham-Hall, E.1    Clatworthy, M.R.2    Okkenhaug, K.3
  • 228
    • 0036707521 scopus 로고    scopus 로고
    • PI3K-mediated negative feedback regulation of IL-12 production in DCs
    • Fukao T, Tanabe M, Terauchi Y, Ota T, Matsuda S, et al. 2002. PI3K-mediated negative feedback regulation of IL-12 production in DCs. Nat. Immunol. 3:875-81
    • (2002) Nat. Immunol. , vol.3 , pp. 875-881
    • Fukao, T.1    Tanabe, M.2    Terauchi, Y.3    Ota, T.4    Matsuda, S.5
  • 230
    • 84874205927 scopus 로고    scopus 로고
    • Does the PI3K pathway promote or antagonize regulatory T cell development and function?
    • Soond DR, Slack EC, Garden OA, Patton DT, Okkenhaug K. 2012. Does the PI3K pathway promote or antagonize regulatory T cell development and function? Front. Immunol. 3:244
    • (2012) Front. Immunol. , vol.3 , pp. 244
    • Soond, D.R.1    Slack, E.C.2    Garden, O.A.3    Patton, D.T.4    Okkenhaug, K.5
  • 231
    • 45549098562 scopus 로고    scopus 로고
    • T cell receptor signaling controls Foxp3 expression via PI3K, Akt, and mTOR
    • Sauer S, Bruno L, Hertweck A, Finlay D, Leleu M, et al. 2008. T cell receptor signaling controls Foxp3 expression via PI3K, Akt, and mTOR. Proc. Natl. Acad. Sci. USA 105:7797-802
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 7797-7802
    • Sauer, S.1    Bruno, L.2    Hertweck, A.3    Finlay, D.4    Leleu, M.5
  • 234
    • 74649085700 scopus 로고    scopus 로고
    • + T cell fate by regulating the expression of transcription factors T-bet and Eomesodermin
    • + T cell fate by regulating the expression of transcription factors T-bet and Eomesodermin. Immunity 32:67-78
    • (2010) Immunity , vol.32 , pp. 67-78
    • Rao, R.R.1    Li, Q.2    Odunsi, K.3    Shrikant, P.A.4
  • 235
    • 68149100422 scopus 로고    scopus 로고
    • The p110∞ isoform of phosphatidylinositol 3-kinase controls susceptibility to Leishmania major by regulating expansion and tissue homing of regulatory T cells
    • Liu D, Zhang T, Marshall AJ, Okkenhaug K, Vanhaesebroeck B, et al. 2009. The p110∞ isoform of phosphatidylinositol 3-kinase controls susceptibility to Leishmania major by regulating expansion and tissue homing of regulatory T cells. J. Immunol. 183:1921-33
    • (2009) J. Immunol. , vol.183 , pp. 1921-1933
    • Liu, D.1    Zhang, T.2    Marshall, A.J.3    Okkenhaug, K.4    Vanhaesebroeck, B.5
  • 236
    • 84874205694 scopus 로고    scopus 로고
    • Selective inhibitors of phosphoinositide 3-kinase delta: Modulators of B-cell function with potential for treating autoimmune inflammatory diseases and B-cell malignancies
    • Gold MR, Puri KD. 2012. Selective inhibitors of phosphoinositide 3-kinase delta: modulators of B-cell function with potential for treating autoimmune inflammatory diseases and B-cell malignancies. Front. Immunol. 3:256
    • (2012) Front. Immunol. , vol.3 , pp. 256
    • Gold, M.R.1    Puri, K.D.2
  • 237
    • 84857844598 scopus 로고    scopus 로고
    • PI3K∞inhibitors in cancer: Rationale and serendipity merge in the clinic
    • Fruman DA, Rommel C. 2011. PI3K∞inhibitors in cancer: rationale and serendipity merge in the clinic. Cancer Discov. 1:562-72
    • (2011) Cancer Discov. , vol.1 , pp. 562-572
    • Fruman, D.A.1    Rommel, C.2
  • 238
    • 78751553221 scopus 로고    scopus 로고
    • CAL-101, a p110∞selective phosphatidylinositol-3-kinase inhibitor for the treatment of B-cell malignancies, inhibits PI3K signaling and cellular viability
    • Lannutti BJ, Meadows SA, Herman SE, Kashishian A, Steiner B, et al. 2011. CAL-101, a p110∞selective phosphatidylinositol-3-kinase inhibitor for the treatment of B-cell malignancies, inhibits PI3K signaling and cellular viability. Blood 117:591-94
    • (2011) Blood , vol.117 , pp. 591-594
    • Lannutti, B.J.1    Meadows, S.A.2    Herman, S.E.3    Kashishian, A.4    Steiner, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.