메뉴 건너뛰기




Volumn 205, Issue 3, 2005, Pages 452-462

The class II phosphoinositide 3-kinase PI3K-C2β regulates cell migration by a PtdIns(3)P dependent mechanism

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; FIBRONECTIN; GUANOSINE TRIPHOSPHATE; HYBRID PROTEIN; ISOENZYME; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3 KINASE C2BETA; PROTEIN CDC42; PROTEIN SUBUNIT; RECOMBINANT ENZYME; UNCLASSIFIED DRUG; VERY LATE ACTIVATION ANTIGEN 4;

EID: 27744606985     PISSN: 00219541     EISSN: None     Source Type: Journal    
DOI: 10.1002/jcp.20478     Document Type: Article
Times cited : (72)

References (63)
  • 1
    • 0034024403 scopus 로고    scopus 로고
    • Class II phosphoinositide 3-kinase are downstream targets of activated polypeptide growth factor receptors
    • Arcaro A, Zvelebil MJ, Wallasch C, Ullrich A, Waterfield MD, Domin J. 2000. Class II phosphoinositide 3-kinase are downstream targets of activated polypeptide growth factor receptors. Mol Cell Biol 20:3817-3830.
    • (2000) Mol Cell Biol , vol.20 , pp. 3817-3830
    • Arcaro, A.1    Zvelebil, M.J.2    Wallasch, C.3    Ullrich, A.4    Waterfield, M.D.5    Domin, J.6
  • 2
    • 0036791759 scopus 로고    scopus 로고
    • Two distinct phosphoinositide 3-kinases mediate polypeptide growth factor-stimulated PKB activation
    • Arcaro A, Khanzada UK, Vanhaesebroeck B, Tetley TD, Waterfield MD, Seckl MJ. 2002. Two distinct phosphoinositide 3-kinases mediate polypeptide growth factor-stimulated PKB activation. EMBO J 21:5097-5108.
    • (2002) EMBO J , vol.21 , pp. 5097-5108
    • Arcaro, A.1    Khanzada, U.K.2    Vanhaesebroeck, B.3    Tetley, T.D.4    Waterfield, M.D.5    Seckl, M.J.6
  • 3
    • 2442640271 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase is involved in alpha2(I) collagen gene expression in normal and scleroderma fibroblasts
    • Asano Y, Ihn H, Yamane K, Jinnin M, Mimura Y, Tamaki K. 2004. Phosphatidylinositol 3-kinase is involved in alpha2(I) collagen gene expression in normal and scleroderma fibroblasts. J Immunol 172:7123-7135.
    • (2004) J Immunol , vol.172 , pp. 7123-7135
    • Asano, Y.1    Ihn, H.2    Yamane, K.3    Jinnin, M.4    Mimura, Y.5    Tamaki, K.6
  • 4
    • 0942268723 scopus 로고    scopus 로고
    • Rho GTPases have diverse effects on the organization of the actin filament system
    • Aspenstrom P, Fransson A, Saras J. 2004. Rho GTPases have diverse effects on the organization of the actin filament system. Biochem J 377:327-337.
    • (2004) Biochem J , vol.377 , pp. 327-337
    • Aspenstrom, P.1    Fransson, A.2    Saras, J.3
  • 5
    • 0037986310 scopus 로고    scopus 로고
    • Loss of phosphatidylinositol 3-phosphate binding by the C-terminal Tiam-1 pleckstrin homology domain prevents in vivo Rac1 activation without affecting membrane targeting
    • Baumeister MA, Martinu L, Rossman KL, Sondek J, Lemmon MA, Chou MM. 2003. Loss of phosphatidylinositol 3-phosphate binding by the C-terminal Tiam-1 pleckstrin homology domain prevents in vivo Rac1 activation without affecting membrane targeting. J Biol Chem 278:11457-11464.
    • (2003) J Biol Chem , vol.278 , pp. 11457-11464
    • Baumeister, M.A.1    Martinu, L.2    Rossman, K.L.3    Sondek, J.4    Lemmon, M.A.5    Chou, M.M.6
  • 6
    • 0036544561 scopus 로고    scopus 로고
    • A cycle of Vam7p release from and PtdIns 3-P-dependent rebinding to the yeast vacuole is required for homotypic vacuole fusion
    • Boeddinghaus C, Merz AJ, Laage R, Ungermann C. 2002. A cycle of Vam7p release from and PtdIns 3-P-dependent rebinding to the yeast vacuole is required for homotypic vacuole fusion. J Cell Biol 157:79-89.
    • (2002) J Cell Biol , vol.157 , pp. 79-89
    • Boeddinghaus, C.1    Merz, A.J.2    Laage, R.3    Ungermann, C.4
  • 7
    • 0037904987 scopus 로고    scopus 로고
    • The integrin-actin connection, an eternal love affair
    • Brakebusch C, Fassler R. 2003. The integrin-actin connection, an eternal love affair. EMBO J 22:2324-2333.
    • (2003) EMBO J , vol.22 , pp. 2324-2333
    • Brakebusch, C.1    Fassler, R.2
  • 8
    • 0031575938 scopus 로고    scopus 로고
    • Identification and cDNA cloning of a novel mammalian C2 domain-containing phosphoinositide 3-kinase, HsC2-PI3K
    • Brown RA, Ho LK, Weber-Hall SJ, Shipley JM, Fry MJ. 1997. Identification and cDNA cloning of a novel mammalian C2 domain-containing phosphoinositide 3-kinase, HsC2-PI3K. Biochem Biophys Res Commun 233:537-544.
    • (1997) Biochem Biophys Res Commun , vol.233 , pp. 537-544
    • Brown, R.A.1    Ho, L.K.2    Weber-Hall, S.J.3    Shipley, J.M.4    Fry, M.J.5
  • 9
    • 0032111444 scopus 로고    scopus 로고
    • Phosphatidylinositol (3)-phosphate signalling mediated by specific binding to RING FYVE domains
    • Burd CG, Emr SD. 1998. Phosphatidylinositol (3)-phosphate signalling mediated by specific binding to RING FYVE domains. Mol Cell 2:157-162.
    • (1998) Mol Cell , vol.2 , pp. 157-162
    • Burd, C.G.1    Emr, S.D.2
  • 10
    • 0033551070 scopus 로고    scopus 로고
    • New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway
    • Cantley LC, Neel BG. 1999. New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway. Proc Natl Acad Sci USA 96:4240-4245.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 4240-4245
    • Cantley, L.C.1    Neel, B.G.2
  • 11
    • 0036684497 scopus 로고    scopus 로고
    • Hepatocyte growth factor activates phosphoinositide 3-kinase C2beta in renal brush-border plasma membranes
    • Crljen V, Volinia S, Banfic H. 2002. Hepatocyte growth factor activates phosphoinositide 3-kinase C2beta in renal brush-border plasma membranes. Biochem J 365:791-799.
    • (2002) Biochem J , vol.365 , pp. 791-799
    • Crljen, V.1    Volinia, S.2    Banfic, H.3
  • 12
    • 0037929688 scopus 로고    scopus 로고
    • Down-regulation of Rac activity during beta 2 integrin-mediated adhesion of human neutrophils
    • Dib K, Melander F, Axelsson L, Dagher MC, Aspenstrom P, Andersson T. 2003. Down-regulation of Rac activity during beta 2 integrin-mediated adhesion of human neutrophils. J Biol Chem 278:24181-24188.
    • (2003) J Biol Chem , vol.278 , pp. 24181-24188
    • Dib, K.1    Melander, F.2    Axelsson, L.3    Dagher, M.C.4    Aspenstrom, P.5    Andersson, T.6
  • 13
    • 0030790548 scopus 로고    scopus 로고
    • Using structure to define the function of phosphoinositide 3-kinase family members
    • Domin J, Waterfield MD. 1997. Using structure to define the function of phosphoinositide 3-kinase family members. FEBS Lett 410:91-95.
    • (1997) FEBS Lett , vol.410 , pp. 91-95
    • Domin, J.1    Waterfield, M.D.2
  • 14
    • 0030884527 scopus 로고    scopus 로고
    • Cloning of a human phosphatidylinositol 3-kinase with a C2 domain which displays reduced sensitivity to the inhibitor wortmannin
    • Domin J, Pages F, Volinia S, Rittenhouse SE, Zvelebil MJ, Stein RC, Waterfield MD. 1997. Cloning of a human phosphatidylinositol 3-kinase with a C2 domain which displays reduced sensitivity to the inhibitor wortmannin. Biochem J 326:139-147.
    • (1997) Biochem J , vol.326 , pp. 139-147
    • Domin, J.1    Pages, F.2    Volinia, S.3    Rittenhouse, S.E.4    Zvelebil, M.J.5    Stein, R.C.6    Waterfield, M.D.7
  • 16
    • 0035282910 scopus 로고    scopus 로고
    • Fgd1, the Cdc42 guanine nucleotide exchange factor responsible for faciogenital dysplasia, is localized to the subcortical actin cytoskeleton and Golgi membrane
    • Estrada L, Caron E, Gorski JL. 2001. Fgd1, the Cdc42 guanine nucleotide exchange factor responsible for faciogenital dysplasia, is localized to the subcortical actin cytoskeleton and Golgi membrane. Hum Mol Genet 10:485-495.
    • (2001) Hum Mol Genet , vol.10 , pp. 485-495
    • Estrada, L.1    Caron, E.2    Gorski, J.L.3
  • 17
    • 0035943401 scopus 로고    scopus 로고
    • Integrin-mediated activation of Cdc42 controls cell polarity in migrating astrocytes through PKCzeta
    • Etienne-Manneville S, Hall A. 2001. Integrin-mediated activation of Cdc42 controls cell polarity in migrating astrocytes through PKCzeta. Cell 106:489-498.
    • (2001) Cell , vol.106 , pp. 489-498
    • Etienne-Manneville, S.1    Hall, A.2
  • 18
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology
    • Etienne-Manneville S, Hall A. 2002. Rho GTPases in cell biology. Nature 420:629-635.
    • (2002) Nature , vol.420 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, A.2
  • 19
    • 0037205265 scopus 로고    scopus 로고
    • Spatial and temporal regulation of 3-phosphoinositides by PI 3-kinase and PTEN mediates chemotaxis
    • Funamoto S, Meili R, Lee S, Parry L, Firtel RA. 2002. Spatial and temporal regulation of 3-phosphoinositides by PI 3-kinase and PTEN mediates chemotaxis. Cell 109:611-623.
    • (2002) Cell , vol.109 , pp. 611-623
    • Funamoto, S.1    Meili, R.2    Lee, S.3    Parry, L.4    Firtel, R.A.5
  • 21
    • 0038247883 scopus 로고    scopus 로고
    • Receptor-mediated regulation of PI3Ks confines PI(3,4,5)P3 to the leading edge of chemotaxing cells
    • Huang YE, Iijima M, Parent CA, Funamoto S, Firtel RA, Devreotes P. 2003. Receptor-mediated regulation of PI3Ks confines PI(3,4,5)P3 to the leading edge of chemotaxing cells. Mol Biol Cell 14:1913-1922.
    • (2003) Mol Biol Cell , vol.14 , pp. 1913-1922
    • Huang, Y.E.1    Iijima, M.2    Parent, C.A.3    Funamoto, S.4    Firtel, R.A.5    Devreotes, P.6
  • 22
    • 0000446084 scopus 로고    scopus 로고
    • ERBB-2 overexpression confers PI 3′ kinase-dependent invasion capacity on human mammary epithelial cells
    • Ignatoski KM, Maehama T, Markwart SM, Dixon JE, Livant DL, Ethier SP. 2000. ERBB-2 overexpression confers PI 3′ kinase-dependent invasion capacity on human mammary epithelial cells. Br J Cancer 82:666-674.
    • (2000) Br J Cancer , vol.82 , pp. 666-674
    • Ignatoski, K.M.1    Maehama, T.2    Markwart, S.M.3    Dixon, J.E.4    Livant, D.L.5    Ethier, S.P.6
  • 23
    • 0035656919 scopus 로고    scopus 로고
    • PIP3, PIP2, and cell movement-Similar messages, different meanings?
    • Insall RH, Weiner OD. 2001. PIP3, PIP2, and cell movement-Similar messages, different meanings? Dev Cell 1:743-747.
    • (2001) Dev Cell , vol.1 , pp. 743-747
    • Insall, R.H.1    Weiner, O.D.2
  • 24
    • 0036201871 scopus 로고    scopus 로고
    • The FYVE domain in Smad anchor for receptor activation (SARA) is sufficient for localization of SARA in early endosomes and regulates TGF-beta/ Smad signalling
    • Itoh F, Divecha N, Brocks L, Oomen L, Janssen H, Calafat J, Itoh S, Dijke PP. 2002. The FYVE domain in Smad anchor for receptor activation (SARA) is sufficient for localization of SARA in early endosomes and regulates TGF-beta/ Smad signalling. Genes Cells 7:321-331.
    • (2002) Genes Cells , vol.7 , pp. 321-331
    • Itoh, F.1    Divecha, N.2    Brocks, L.3    Oomen, L.4    Janssen, H.5    Calafat, J.6    Itoh, S.7    Dijke, P.P.8
  • 25
    • 0025777183 scopus 로고
    • The minimal essential sequence for a major cell type-specific adhesion site (CS1) within the alternatively spliced type III connecting segment domain of fibronectin is leucine-aspartic acid-valine
    • Komoriya A, Green LJ, Mervic M, Yamada SS, Yamada KM, Humphries MJ. 1991. The minimal essential sequence for a major cell type-specific adhesion site (CS1) within the alternatively spliced type III connecting segment domain of fibronectin is leucine-aspartic acid-valine. J Biol Chem 266:15075-15079.
    • (1991) J Biol Chem , vol.266 , pp. 15075-15079
    • Komoriya, A.1    Green, L.J.2    Mervic, M.3    Yamada, S.S.4    Yamada, K.M.5    Humphries, M.J.6
  • 26
    • 0036677159 scopus 로고    scopus 로고
    • The PtdIns3P phosphatase myotubularin is a cytoplasmic protein that also localizes to Rac1-inducible plasma membrane ruffles
    • Laporte J, Blondeau F, Gansmuller A, Lutz Y, Vonesch JL, Mandel JL. 2002. The PtdIns3P phosphatase myotubularin is a cytoplasmic protein that also localizes to Rac1-inducible plasma membrane ruffles. J Cell Sci 115:3105-3117.
    • (2002) J Cell Sci , vol.115 , pp. 3105-3117
    • Laporte, J.1    Blondeau, F.2    Gansmuller, A.3    Lutz, Y.4    Vonesch, J.L.5    Mandel, J.L.6
  • 28
    • 0032929762 scopus 로고    scopus 로고
    • Signalling through phosphoinositide 3-kinases: The lipids take centre stage
    • Leevers SJ, Vanhaesebroeck B, Waterfield MD. 1999. Signalling through phosphoinositide 3-kinases: The lipids take centre stage. Curr Opin Cell Biol 11:219-225.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 219-225
    • Leevers, S.J.1    Vanhaesebroeck, B.2    Waterfield, M.D.3
  • 29
    • 0034912744 scopus 로고    scopus 로고
    • PTEN and myotubularin: Novel phosphoinositide phosphatases
    • Maehama T, Taylor GS, Dixon JE. 2001. PTEN and myotubularin: Novel phosphoinositide phosphatases. Annu Rev Biochem 70:247-279.
    • (2001) Annu Rev Biochem , vol.70 , pp. 247-279
    • Maehama, T.1    Taylor, G.S.2    Dixon, J.E.3
  • 30
    • 0042466604 scopus 로고    scopus 로고
    • Insulin induces phosphatidylinositol-3-phosphate formation through TC10 activation
    • Maffucci T, Brancaccio A, Piccolo E, Stein RC, Falasca M. 2003. Insulin induces phosphatidylinositol-3-phosphate formation through TC10 activation. Embo J 22:4178-4189.
    • (2003) Embo J , vol.22 , pp. 4178-4189
    • Maffucci, T.1    Brancaccio, A.2    Piccolo, E.3    Stein, R.C.4    Falasca, M.5
  • 31
    • 0041327718 scopus 로고    scopus 로고
    • Leading the way: Directional sensing through phosphatidylinositol 3-kinase and other signaling pathways
    • Merlot S, Firtel RA. 2003. Leading the way: Directional sensing through phosphatidylinositol 3-kinase and other signaling pathways. J Cell Sci 116:3471-3478.
    • (2003) J Cell Sci , vol.116 , pp. 3471-3478
    • Merlot, S.1    Firtel, R.A.2
  • 32
    • 0028837170 scopus 로고
    • Activation of the small GTP-binding proteins rho and rac by growth factor receptors
    • Nobes CD, Hawkins P, Stephens L, Hall A. 1995. Activation of the small GTP-binding proteins rho and rac by growth factor receptors. J Cell Sci 108(Pt 1):225-233.
    • (1995) J Cell Sci , vol.108 , Issue.PART 1 , pp. 225-233
    • Nobes, C.D.1    Hawkins, P.2    Stephens, L.3    Hall, A.4
  • 34
    • 0032571317 scopus 로고    scopus 로고
    • A novel class II phosphoinositide 3-kinase predominantly expressed in the liver and its enhanced expression during liver regeneration
    • Ono F, Nakagawa T, Saito S, Owada Y, Sakagami H, Goto K, Suzuki M, Matsuno S, Kondo H. 1998. A novel class II phosphoinositide 3-kinase predominantly expressed in the liver and its enhanced expression during liver regeneration. J Biol Chem 273:7731-7736.
    • (1998) J Biol Chem , vol.273 , pp. 7731-7736
    • Ono, F.1    Nakagawa, T.2    Saito, S.3    Owada, Y.4    Sakagami, H.5    Goto, K.6    Suzuki, M.7    Matsuno, S.8    Kondo, H.9
  • 36
    • 0034467058 scopus 로고    scopus 로고
    • Activation of synovial fibroblasts in rheumatoid arthritis: Lack of Expression of the tumour suppressor PTEN at sites of invasive growth and destruction
    • Pap T, Franz JK, Hummel KM, Jeisy E, Gay R, Gay S. 2000. Activation of synovial fibroblasts in rheumatoid arthritis: Lack of Expression of the tumour suppressor PTEN at sites of invasive growth and destruction. Arthritis Res 2:59-64.
    • (2000) Arthritis Res , vol.2 , pp. 59-64
    • Pap, T.1    Franz, J.K.2    Hummel, K.M.3    Jeisy, E.4    Gay, R.5    Gay, S.6
  • 37
    • 15144339719 scopus 로고    scopus 로고
    • Homing and trafficking of hemopoietic progenitor cells
    • Papayannopoulou T, Craddock C. 1997. Homing and trafficking of hemopoietic progenitor cells. Acta Haematol 97:97-104.
    • (1997) Acta Haematol , vol.97 , pp. 97-104
    • Papayannopoulou, T.1    Craddock, C.2
  • 38
    • 0028126564 scopus 로고
    • Isolation and characterization of the faciogenital dysplasia (Aarskog-Scott syndrome) gene: A putative Rho/Rac guanine nucleotide exchange factor
    • Pasteris NG, Cadle A, Logie LJ, Porteous ME, Schwartz CE, Stevenson RE, Glover TW, Wilroy RS, Gorski JL. 1994. Isolation and characterization of the faciogenital dysplasia (Aarskog-Scott syndrome) gene: A putative Rho/Rac guanine nucleotide exchange factor. Cell 79:669-678.
    • (1994) Cell , vol.79 , pp. 669-678
    • Pasteris, N.G.1    Cadle, A.2    Logie, L.J.3    Porteous, M.E.4    Schwartz, C.E.5    Stevenson, R.E.6    Glover, T.W.7    Wilroy, R.S.8    Gorski, J.L.9
  • 39
    • 0037452054 scopus 로고    scopus 로고
    • The cytoskeleton, cellular motility and the reductionist agenda
    • Pollard TD. 2003. The cytoskeleton, cellular motility and the reductionist agenda. Nature 422:741-745.
    • (2003) Nature , vol.422 , pp. 741-745
    • Pollard, T.D.1
  • 40
    • 0345731237 scopus 로고    scopus 로고
    • Cell migration: Rho GTPases lead the way
    • Raftopoulou M, Hall A. 2004. Cell migration: Rho GTPases lead the way. Dev Biol 265:23-32.
    • (2004) Dev Biol , vol.265 , pp. 23-32
    • Raftopoulou, M.1    Hall, A.2
  • 41
    • 1242284600 scopus 로고    scopus 로고
    • Regulation of cell migration by the C2 domain of the tumor suppressor PTEN
    • Raftopoulou M, Etienne-Manneville S, Self A, Nicholls S, Hall A. 2004. Regulation of cell migration by the C2 domain of the tumor suppressor PTEN. Science 303:1179-1181.
    • (2004) Science , vol.303 , pp. 1179-1181
    • Raftopoulou, M.1    Etienne-Manneville, S.2    Self, A.3    Nicholls, S.4    Hall, A.5
  • 42
    • 0034685801 scopus 로고    scopus 로고
    • The role of the pleckstrin homology domain in membrane targeting and activation of phospholipase Cbeta(1)
    • Razzini G, Brancaccio A, Lemmon MA, Guarnieri S, Falasca M. 2000. The role of the pleckstrin homology domain in membrane targeting and activation of phospholipase Cbeta(1). J Biol Chem 275:14873-14881.
    • (2000) J Biol Chem , vol.275 , pp. 14873-14881
    • Razzini, G.1    Brancaccio, A.2    Lemmon, M.A.3    Guarnieri, S.4    Falasca, M.5
  • 44
    • 0034108503 scopus 로고    scopus 로고
    • Activation of cdc42, rac, PAK, and rho-kinase in response to hepatocyte growth factor differentially regulates epithelial cell colony spreading and dissociation
    • Royal I, Lamarche-Vane N, Lamorte L, Kaibuchi K, Park M. 2000. Activation of cdc42, rac, PAK, and rho-kinase in response to hepatocyte growth factor differentially regulates epithelial cell colony spreading and dissociation. Mol Biol Cell 11:1709-1725.
    • (2000) Mol Biol Cell , vol.11 , pp. 1709-1725
    • Royal, I.1    Lamarche-Vane, N.2    Lamorte, L.3    Kaibuchi, K.4    Park, M.5
  • 45
    • 0032583205 scopus 로고    scopus 로고
    • Matrix-dependent Tiam1/Rac signaling in epithelial cells promotes either cell-cell adhesion or cell migration and is regulated by phosphatidylinositol 3-kinase
    • Sander EE, van Delft S, ten Klooster JP, Reid T, van der Kammen RA, Michiels F, Collard JG. 1998. Matrix-dependent Tiam1/Rac signaling in epithelial cells promotes either cell-cell adhesion or cell migration and is regulated by phosphatidylinositol 3-kinase. J Cell Biol 143:1385-1398.
    • (1998) J Cell Biol , vol.143 , pp. 1385-1398
    • Sander, E.E.1    Van Delft, S.2    Ten Klooster, J.P.3    Reid, T.4    Van Der Kammen, R.A.5    Michiels, F.6    Collard, J.G.7
  • 46
    • 0027905021 scopus 로고
    • Phosphatidylinositol 3-kinase encoded by the yeast VPS34 gene essential for protein sorting
    • Schu PV, Takegawa K, Fry MJ, Stack JH, Waterfield MD, Emr SD. 1993. Phosphatidylinositol 3-kinase encoded by the yeast VPS34 gene essential for protein sorting. Science 260:88-92.
    • (1993) Science , vol.260 , pp. 88-92
    • Schu, P.V.1    Takegawa, K.2    Fry, M.J.3    Stack, J.H.4    Waterfield, M.D.5    Emr, S.D.6
  • 52
    • 0028334738 scopus 로고
    • A novel phosphoinositide 3 kinase activity in myeloid-derived cells is activated by G protein beta gamma subunits
    • Stephens L, Smrcka A, Cooke FT, Jackson TR, Sternweis PC, Hawkins PT. 1994b. A novel phosphoinositide 3 kinase activity in myeloid-derived cells is activated by G protein beta gamma subunits. Cell 77:83-93.
    • (1994) Cell , vol.77 , pp. 83-93
    • Stephens, L.1    Smrcka, A.2    Cooke, F.T.3    Jackson, T.R.4    Sternweis, P.C.5    Hawkins, P.T.6
  • 53
    • 0036532121 scopus 로고    scopus 로고
    • Roles of PI3Ks in leukocyte chemotaxis and phagocytosis
    • Stephens L, Ellson C, Hawkins P. 2002. Roles of PI3Ks in leukocyte chemotaxis and phagocytosis. Curr Opin Cell Biol 14:203-213.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 203-213
    • Stephens, L.1    Ellson, C.2    Hawkins, P.3
  • 54
    • 0030006284 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization
    • Symons M, Derry JM, Karlak B, Jiang S, Lemahieu V, McCormick F, Francke U, Abo A. 1996. Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization. Cell 84:723-734.
    • (1996) Cell , vol.84 , pp. 723-734
    • Symons, M.1    Derry, J.M.2    Karlak, B.3    Jiang, S.4    Lemahieu, V.5    McCormick, F.6    Francke, U.7    Abo, A.8
  • 55
    • 0030992837 scopus 로고    scopus 로고
    • Signalling through the lipid products of phosphoinositide-3-OH kinase
    • Toker A, Cantley LC. 1997. Signalling through the lipid products of phosphoinositide-3-OH kinase. Nature 387:673-676.
    • (1997) Nature , vol.387 , pp. 673-676
    • Toker, A.1    Cantley, L.C.2
  • 56
    • 0032476036 scopus 로고    scopus 로고
    • The CC chemokine Monocyte Chemotactic Peptide-1 activates both the Class I p85/ p110 Phosphatidylinositol 3-kinase and the Class II PI3K-C2a
    • Turner SJ, Domin J, Waterfield MD, Ward SG, Westwick J. 1998. The CC chemokine Monocyte Chemotactic Peptide-1 activates both the Class I p85/ p110 Phosphatidylinositol 3-kinase and the Class II PI3K-C2a. J Biol Chem 273:25987-25995.
    • (1998) J Biol Chem , vol.273 , pp. 25987-25995
    • Turner, S.J.1    Domin, J.2    Waterfield, M.D.3    Ward, S.G.4    Westwick, J.5
  • 61
    • 0034816499 scopus 로고    scopus 로고
    • Recruitment of the class II phosphoinositide 3-kinase C2beta to the epidermal growth factor receptor: Role of Grb2
    • Wheeler M, Domin J. 2001. Recruitment of the class II phosphoinositide 3-kinase C2beta to the epidermal growth factor receptor: Role of Grb2. Mol Cell Biol 21:6660-6667.
    • (2001) Mol Cell Biol , vol.21 , pp. 6660-6667
    • Wheeler, M.1    Domin, J.2
  • 63
    • 0032486378 scopus 로고    scopus 로고
    • A type II phosphoinositide 3-kinase is stimulated via activated integrin in platelets. A source of phosphatidylinositol 3-phosphate
    • Zhang J, Banfic H, Straforini F, Tosi L, Volinia S, Rittenhouse S. 1998. A type II phosphoinositide 3-kinase is stimulated via activated integrin in platelets. A source of phosphatidylinositol 3-phosphate. J Biol Chem 273:14081-14084.
    • (1998) J Biol Chem , vol.273 , pp. 14081-14084
    • Zhang, J.1    Banfic, H.2    Straforini, F.3    Tosi, L.4    Volinia, S.5    Rittenhouse, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.