메뉴 건너뛰기




Volumn 83, Issue 4, 2015, Pages 1695-1704

The class II phosphatidylinositol 3-phosphate kinase PIK3C2A promotes Shigella flexneri dissemination through formation of vacuole-like protrusions

Author keywords

[No Author keywords available]

Indexed keywords

2 MORPHOLINO 8 PHENYLCHROMONE; COMPLEMENTARY DNA; IMATINIB; PHOSPHATIDYLINOSITOL 3 PHOSPHATE; PHOSPHOTRANSFERASE; PROTEIN PIK3C2A; PROTEIN TYROSINE KINASE; UNCLASSIFIED DRUG; WORTMANNIN; BACTERIAL SECRETION SYSTEM; PHOSPHATIDYLINOSITOL 3 KINASE; PIK3C2A PROTEIN, HUMAN; POLYPHOSPHOINOSITIDE; SMALL INTERFERING RNA;

EID: 84925356216     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.03138-14     Document Type: Article
Times cited : (24)

References (50)
  • 1
    • 0023032274 scopus 로고
    • Synthesis and secretion of interferon by murine fibroblasts in response to intracellular Listeria monocytogenes
    • Havell EA. 1986. Synthesis and secretion of interferon by murine fibroblasts in response to intracellular Listeria monocytogenes. Infect Immun 54:787-792.
    • (1986) Infect Immun , vol.54 , pp. 787-792
    • Havell, E.A.1
  • 2
    • 0023050141 scopus 로고
    • A genetic determinant required for continuous reinfection of adjacent cells on large plasmid in . flexneri 2a
    • Makino S, Sasakawa C, Kamata K, Kurata T, Yoshikawa M. 1986. A genetic determinant required for continuous reinfection of adjacent cells on large plasmid in S. flexneri 2a. Cell 46:551-555. http://dx.doi.org/10.1016/0092-8674(86)90880-9.
    • (1986) Cell , vol.46 , pp. 551-555
    • Makino, S.1    Sasakawa, C.2    Kamata, K.3    Kurata, T.4    Yoshikawa, M.5
  • 3
    • 70350231616 scopus 로고    scopus 로고
    • Listeria monocytogenes membrane trafficking and lifestyle: the exception or the rule?
    • Pizarro-Cerda J, Cossart P. 2009. Listeria monocytogenes membrane trafficking and lifestyle: the exception or the rule? Annu Rev Cell Dev Biol 25:649-670. http://dx.doi.org/10.1146/annurev.cellbio.042308.113331.
    • (2009) Annu Rev Cell Dev Biol , vol.25 , pp. 649-670
    • Pizarro-Cerda, J.1    Cossart, P.2
  • 4
    • 64749104915 scopus 로고    scopus 로고
    • Life on the inside: the intracellular lifestyle of cytosolic bacteria
    • Ray K, Marteyn B, Sansonetti PJ, Tang CM. 2009. Life on the inside: the intracellular lifestyle of cytosolic bacteria. Nat Rev Microbiol 7:333-340. http://dx.doi.org/10.1038/nrmicro2112.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 333-340
    • Ray, K.1    Marteyn, B.2    Sansonetti, P.J.3    Tang, C.M.4
  • 5
    • 0025081821 scopus 로고
    • Listeria monocytogenes moves rapidly through the host-cell cytoplasm by inducing directional actin assembly
    • Dabiri GA, Sanger JM, Portnoy DA, Southwick FS. 1990. Listeria monocytogenes moves rapidly through the host-cell cytoplasm by inducing directional actin assembly. Proc Natl Acad Sci U S A 87:6068-6072. http://dx.doi.org/10.1073/pnas.87.16.6068.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 6068-6072
    • Dabiri, G.A.1    Sanger, J.M.2    Portnoy, D.A.3    Southwick, F.S.4
  • 6
    • 0026547790 scopus 로고
    • The rate of actin-based motility of intracellular Listeria monocytogenes equals the rate of actin polymerization
    • Theriot JA, Mitchison TJ, Tilney LG, Portnoy DA. 1992. The rate of actin-based motility of intracellular Listeria monocytogenes equals the rate of actin polymerization. Nature 357:257-260. http://dx.doi.org/10.1038/357257a0.
    • (1992) Nature , vol.357 , pp. 257-260
    • Theriot, J.A.1    Mitchison, T.J.2    Tilney, L.G.3    Portnoy, D.A.4
  • 7
    • 0026095008 scopus 로고
    • Intercellular spread of Shigella flexneri through a monolayer mediated by membranous protrusions and associated with reorganization of the cytoskeletal protein vinculin
    • Kadurugamuwa JL, Rohde M, Wehland J, Timmis KN. 1991. Intercellular spread of Shigella flexneri through a monolayer mediated by membranous protrusions and associated with reorganization of the cytoskeletal protein vinculin. Infect Immun 59:3463-3471.
    • (1991) Infect Immun , vol.59 , pp. 3463-3471
    • Kadurugamuwa, J.L.1    Rohde, M.2    Wehland, J.3    Timmis, K.N.4
  • 8
    • 0024741693 scopus 로고
    • Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite, Listeria monocytogenes
    • Tilney LG, Portnoy DA. 1989. Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite, Listeria monocytogenes. J Cell Biol 109:1597-1608. http://dx.doi.org/10.1083/jcb.109.4.1597.
    • (1989) J Cell Biol , vol.109 , pp. 1597-1608
    • Tilney, L.G.1    Portnoy, D.A.2
  • 9
    • 84883850330 scopus 로고    scopus 로고
    • Arp2/3-mediated actin-based motility: a tail of pathogen abuse
    • Welch MD, Way M. 2013. Arp2/3-mediated actin-based motility: a tail of pathogen abuse. Cell Host Microbe 14:242-255. http://dx.doi.org/10.1016/j.chom.2013.08.011.
    • (2013) Cell Host Microbe , vol.14 , pp. 242-255
    • Welch, M.D.1    Way, M.2
  • 10
    • 0033533789 scopus 로고    scopus 로고
    • Reconstitution of actin-based motility of Listeria and Shigella using pure proteins
    • Loisel TP, Boujemaa R, Pantaloni D, Carlier MF. 1999. Reconstitution of actin-based motility of Listeria and Shigella using pure proteins. Nature 401:613-616. http://dx.doi.org/10.1038/44183.
    • (1999) Nature , vol.401 , pp. 613-616
    • Loisel, T.P.1    Boujemaa, R.2    Pantaloni, D.3    Carlier, M.F.4
  • 11
    • 0031021153 scopus 로고    scopus 로고
    • Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes
    • Welch MD, Iwamatsu A, Mitchison TJ. 1997. Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes. Nature 385:265-269. http://dx.doi.org/10.1038/385265a0.
    • (1997) Nature , vol.385 , pp. 265-269
    • Welch, M.D.1    Iwamatsu, A.2    Mitchison, T.J.3
  • 13
    • 0033574722 scopus 로고    scopus 로고
    • The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly
    • Rohatgi R, Ma L, Miki H, Lopez M, Kirchhausen T, Takenawa T, Kirschner MW. 1999. The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell 97:221-231. http://dx.doi.org/10.1016/S0092-8674(00)80732-1.
    • (1999) Cell , vol.97 , pp. 221-231
    • Rohatgi, R.1    Ma, L.2    Miki, H.3    Lopez, M.4    Kirchhausen, T.5    Takenawa, T.6    Kirschner, M.W.7
  • 14
    • 0024362336 scopus 로고
    • Identification of icsA, a plasmid locus of Shigella flexneri that governs bacterial intra-and intercellular spread through interaction with F-actin
    • Bernardini ML, Mounier J, d'Hauteville H, Coquis-Rondon M, Sansonetti PJ. 1989. Identification of icsA, a plasmid locus of Shigella flexneri that governs bacterial intra-and intercellular spread through interaction with F-actin. Proc Natl Acad Sci U S A 86:3867-3871. http://dx.doi.org/10.1073/pnas.86.10.3867.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 3867-3871
    • Bernardini, M.L.1    Mounier, J.2    d'Hauteville, H.3    Coquis-Rondon, M.4    Sansonetti, P.J.5
  • 15
    • 0033588990 scopus 로고    scopus 로고
    • Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility
    • Egile C, Loisel TP, Laurent V, Li R, Pantaloni D, Sansonetti PJ, Carlier MF. 1999. Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility. J Cell Biol 146:1319-1332. http://dx.doi.org/10.1083/jcb.146.6.1319.
    • (1999) J Cell Biol , vol.146 , pp. 1319-1332
    • Egile, C.1    Loisel, T.P.2    Laurent, V.3    Li, R.4    Pantaloni, D.5    Sansonetti, P.J.6    Carlier, M.F.7
  • 16
    • 0036232011 scopus 로고    scopus 로고
    • Neural Wiskott-Aldrich syndrome protein (N-WASP) is the specific ligand for Shigella VirG among the WASP family and determines the host cell type allowing actin-based spreading
    • Suzuki T, Mimuro H, Suetsugu S, Miki H, Takenawa T, Sasakawa C. 2002. Neural Wiskott-Aldrich syndrome protein (N-WASP) is the specific ligand for Shigella VirG among the WASP family and determines the host cell type allowing actin-based spreading. Cell Microbiol 4:223-233. http://dx.doi.org/10.1046/j.1462-5822.2002.00185.x.
    • (2002) Cell Microbiol , vol.4 , pp. 223-233
    • Suzuki, T.1    Mimuro, H.2    Suetsugu, S.3    Miki, H.4    Takenawa, T.5    Sasakawa, C.6
  • 17
    • 0026577663 scopus 로고
    • A novel bacterial virulence gene in Listeria monocytogenes required for host cell microfilament interaction with homology to the proline-rich region of vinculin
    • Domann E, Wehland J, Rohde M, Pistor S, Hartl M, Goebel W, Leimeister-Wachter M, Wuenscher M, Chakraborty T. 1992. A novel bacterial virulence gene in Listeria monocytogenes required for host cell microfilament interaction with homology to the proline-rich region of vinculin. EMBO J 11:1981-1990.
    • (1992) EMBO J , vol.11 , pp. 1981-1990
    • Domann, E.1    Wehland, J.2    Rohde, M.3    Pistor, S.4    Hartl, M.5    Goebel, W.6    Leimeister-Wachter, M.7    Wuenscher, M.8    Chakraborty, T.9
  • 18
    • 0026515440 scopus 로고
    • L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein
    • Kocks C, Gouin E, Tabouret M, Berche P, Ohayon H, Cossart P. 1992. L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein. Cell 68:521-531.
    • (1992) Cell , vol.68 , pp. 521-531
    • Kocks, C.1    Gouin, E.2    Tabouret, M.3    Berche, P.4    Ohayon, H.5    Cossart, P.6
  • 20
    • 0030900504 scopus 로고    scopus 로고
    • Identification of two regions in the N-terminal domain of ActA involved in the actin comet tail formation by Listeria monocytogenes
    • Lasa I, Gouin E, Goethals M, Vancompernolle K, David V, Vandekerckhove J, Cossart P. 1997. Identification of two regions in the N-terminal domain of ActA involved in the actin comet tail formation by Listeria monocytogenes.EMBOJ 16:1531-1540. http://dx.doi.org/10.1093/emboj/16.7.1531.
    • (1997) EMBO J , vol.16 , pp. 1531-1540
    • Lasa, I.1    Gouin, E.2    Goethals, M.3    Vancompernolle, K.4    David, V.5    Vandekerckhove, J.6    Cossart, P.7
  • 21
    • 0034617996 scopus 로고    scopus 로고
    • Three regions within ActA promote Arp2/3 complex-mediated actin nucleation and Listeria monocytogenes motility
    • Skoble J, Portnoy DA, Welch MD. 2000. Three regions within ActA promote Arp2/3 complex-mediated actin nucleation and Listeria monocytogenes motility. J Cell Biol 150:527-538. http://dx.doi.org/10.1083/jcb.150.3.527.
    • (2000) J Cell Biol , vol.150 , pp. 527-538
    • Skoble, J.1    Portnoy, D.A.2    Welch, M.D.3
  • 22
    • 0033588919 scopus 로고    scopus 로고
    • Listeria monocytogenes exploits normal host cell processes to spread from cell to cell
    • Robbins JR, Barth AI, Marquis H, de Hostos EL, Nelson WJ, Theriot JA. 1999. Listeria monocytogenes exploits normal host cell processes to spread from cell to cell. J Cell Biol 146:1333-1350. http://dx.doi.org/10.1083/jcb.146.6.1333.
    • (1999) J Cell Biol , vol.146 , pp. 1333-1350
    • Robbins, J.R.1    Barth, A.I.2    Marquis, H.3    de Hostos, E.L.4    Nelson, W.J.5    Theriot, J.A.6
  • 23
    • 84891430173 scopus 로고    scopus 로고
    • Actin network disassembly powers dissemination of Listeria monocytogenes
    • Talman AM, Chong R, Chia J, Svitkina T, Agaisse H. 2014. Actin network disassembly powers dissemination of Listeria monocytogenes. J Cell Sci 127:240-249. http://dx.doi.org/10.1242/jcs.140038.
    • (2014) J Cell Sci , vol.127 , pp. 240-249
    • Talman, A.M.1    Chong, R.2    Chia, J.3    Svitkina, T.4    Agaisse, H.5
  • 24
    • 0028218982 scopus 로고
    • Cadherin expression is required for the spread of Shigella flexneri between epithelial cells
    • Sansonetti PJ, Mounier J, Prevost MC, Mege RM. 1994. Cadherin expression is required for the spread of Shigella flexneri between epithelial cells. Cell 76:829-839. http://dx.doi.org/10.1016/0092-8674(94)90358-1.
    • (1994) Cell , vol.76 , pp. 829-839
    • Sansonetti, P.J.1    Mounier, J.2    Prevost, M.C.3    Mege, R.M.4
  • 25
    • 0043198046 scopus 로고    scopus 로고
    • Connexin-dependent inter-cellular communication increases invasion and dissemination of Shigella in epithelial cells
    • Tran Van Nhieu G, Clair C, Bruzzone R, Mesnil M, Sansonetti P, Combettes L. 2003. Connexin-dependent inter-cellular communication increases invasion and dissemination of Shigella in epithelial cells. Nat Cell Biol 5:720-726. http://dx.doi.org/10.1038/ncb1021.
    • (2003) Nat Cell Biol , vol.5 , pp. 720-726
    • Tran Van Nhieu, G.1    Clair, C.2    Bruzzone, R.3    Mesnil, M.4    Sansonetti, P.5    Combettes, L.6
  • 26
    • 84918532087 scopus 로고    scopus 로고
    • Myosin IIA is essential for Shigella flexneri cell-tocell spread
    • Lum M, Morona R. 2014. Myosin IIA is essential for Shigella flexneri cell-tocell spread. Pathog Dis 72:174-187. http://dx.doi.org/10.1111/2049-632X.12202.
    • (2014) Pathog Dis , vol.72 , pp. 174-187
    • Lum, M.1    Morona, R.2
  • 27
    • 0033756186 scopus 로고    scopus 로고
    • Myosin light chain kinase plays an essential role in S. flexneri dissemination
    • Rathman M, de Lanerolle P, Ohayon H, Gounon P, Sansonetti P. 2000. Myosin light chain kinase plays an essential role in S. flexneri dissemination. J Cell Sci 113:3375-3386.
    • (2000) J Cell Sci , vol.113 , pp. 3375-3386
    • Rathman, M.1    de Lanerolle, P.2    Ohayon, H.3    Gounon, P.4    Sansonetti, P.5
  • 29
    • 17144399487 scopus 로고    scopus 로고
    • Listeria monocytogenes exploits ERM protein functions to efficiently spread from cell to cell
    • Pust S, Morrison H, Wehland J, Sechi AS, Herrlich P. 2005. Listeria monocytogenes exploits ERM protein functions to efficiently spread from cell to cell. EMBO J 24:1287-1300. http://dx.doi.org/10.1038/sj.emboj.7600595.
    • (2005) EMBO J , vol.24 , pp. 1287-1300
    • Pust, S.1    Morrison, H.2    Wehland, J.3    Sechi, A.S.4    Herrlich, P.5
  • 30
    • 70349634308 scopus 로고    scopus 로고
    • The bacterial virulence factor InlC perturbs apical cell junctions and promotes cell-to-cell spread of Listeria
    • Rajabian T, Gavicherla B, Heisig M, Muller-Altrock S, Goebel W, Gray-Owen SD, Ireton K. 2009. The bacterial virulence factor InlC perturbs apical cell junctions and promotes cell-to-cell spread of Listeria. Nat Cell Biol 11:1212-1218. http://dx.doi.org/10.1038/ncb1964.
    • (2009) Nat Cell Biol , vol.11 , pp. 1212-1218
    • Rajabian, T.1    Gavicherla, B.2    Heisig, M.3    Muller-Altrock, S.4    Goebel, W.5    Gray-Owen, S.D.6    Ireton, K.7
  • 32
    • 73449146304 scopus 로고    scopus 로고
    • Requirement for formin-induced actin polymerization during spread of Shigella flexneri
    • Heindl JE, Saran I, Yi CR, Lesser CF, Goldberg MB. 2010. Requirement for formin-induced actin polymerization during spread of Shigella flexneri. Infect Immun 78:193-203. http://dx.doi.org/10.1128/IAI.00252-09.
    • (2010) Infect Immun , vol.78 , pp. 193-203
    • Heindl, J.E.1    Saran, I.2    Yi, C.R.3    Lesser, C.F.4    Goldberg, M.B.5
  • 33
    • 84907956156 scopus 로고    scopus 로고
    • The serine/threonine kinase STK11 promotes Shigella flexneri dissemination through establishment of cell-cell contacts competent for tyrosine kinase signaling
    • Dragoi AM, Agaisse H. 2014. The serine/threonine kinase STK11 promotes Shigella flexneri dissemination through establishment of cell-cell contacts competent for tyrosine kinase signaling. Infect Immun 82:4447-4457. http://dx.doi.org/10.1128/IAI.02078-14.
    • (2014) Infect Immun , vol.82 , pp. 4447-4457
    • Dragoi, A.M.1    Agaisse, H.2
  • 34
    • 84925347721 scopus 로고    scopus 로고
    • Tyrosine kinases, drugs, and Shigella flexneri dissemination
    • Dragoi AM, Agaisse H. 2014. Tyrosine kinases, drugs, and Shigella flexneri dissemination. Gut Microbes 5:44-47. http://dx.doi.org/10.4161/gmic.26523.
    • (2014) Gut Microbes , vol.5 , pp. 44-47
    • Dragoi, A.M.1    Agaisse, H.2
  • 35
    • 84873041749 scopus 로고    scopus 로고
    • Bruton's tyrosine kinase regulates Shigella flexneri dissemination in HT-29 intestinal cells
    • Dragoi AM, Talman AM, Agaisse H. 2013. Bruton's tyrosine kinase regulates Shigella flexneri dissemination in HT-29 intestinal cells. Infect Immun 81:598-607. http://dx.doi.org/10.1128/IAI.00853-12.
    • (2013) Infect Immun , vol.81 , pp. 598-607
    • Dragoi, A.M.1    Talman, A.M.2    Agaisse, H.3
  • 36
    • 84859938186 scopus 로고    scopus 로고
    • Shigella targets epithelial tricellular junctions and uses a noncanonical clathrin-dependent endocytic pathway to spread between cells
    • Fukumatsu M, Ogawa M, Arakawa S, Suzuki M, Nakayama K, Shimizu S, Kim M, Mimuro H, Sasakawa C. 2012. Shigella targets epithelial tricellular junctions and uses a noncanonical clathrin-dependent endocytic pathway to spread between cells. Cell Host Microbe 11:325-336. http://dx.doi.org/10.1016/j.chom.2012.03.001.
    • (2012) Cell Host Microbe , vol.11 , pp. 325-336
    • Fukumatsu, M.1    Ogawa, M.2    Arakawa, S.3    Suzuki, M.4    Nakayama, K.5    Shimizu, S.6    Kim, M.7    Mimuro, H.8    Sasakawa, C.9
  • 37
    • 84913554611 scopus 로고    scopus 로고
    • The Shigella flexneri type 3 secretion system is required for tyrosine kinase-dependent protrusion resolution, and vacuole escape during bacterial dissemination
    • Kuehl CJ, Dragoi AM, Agaisse H. 2014. The Shigella flexneri type 3 secretion system is required for tyrosine kinase-dependent protrusion resolution, and vacuole escape during bacterial dissemination. PLoS One 9:e112738. http://dx.doi.org/10.1371/journal.pone.0112738.
    • (2014) PLoS One , vol.9
    • Kuehl, C.J.1    Dragoi, A.M.2    Agaisse, H.3
  • 38
    • 0000843289 scopus 로고
    • Epithelial cell penetration as an essential step in the pathogenesis of bacillary dysentery
    • Labrec EH, Schneider H, Magnani TJ, Formal SB. 1964. Epithelial cell penetration as an essential step in the pathogenesis of bacillary dysentery. J Bacteriol 88:1503-1518.
    • (1964) J Bacteriol , vol.88 , pp. 1503-1518
    • Labrec, E.H.1    Schneider, H.2    Magnani, T.J.3    Formal, S.B.4
  • 39
    • 0023226329 scopus 로고
    • Adoptive transfer of immunity to Listeria monocytogenes. The influence of in vitro stimulation on lymphocyte subset requirements
    • Bishop DK, Hinrichs DJ. 1987. Adoptive transfer of immunity to Listeria monocytogenes. The influence of in vitro stimulation on lymphocyte subset requirements. J Immunol 139:2005-2009.
    • (1987) J Immunol , vol.139 , pp. 2005-2009
    • Bishop, D.K.1    Hinrichs, D.J.2
  • 41
    • 80051516633 scopus 로고    scopus 로고
    • RNAi screen reveals host cell kinases specifically involved in Listeria monocytogenes spread from cell to cell
    • Chong R, Squires R, Swiss R, Agaisse H. 2011. RNAi screen reveals host cell kinases specifically involved in Listeria monocytogenes spread from cell to cell. PLoS One 6:e23399. http://dx.doi.org/10.1371/journal.pone.0023399.
    • (2011) PLoS One , vol.6
    • Chong, R.1    Squires, R.2    Swiss, R.3    Agaisse, H.4
  • 43
    • 0029612196 scopus 로고
    • A family of phosphoinositide 3-kinases in Drosophila identifies a new mediator of signal transduction
    • MacDougall LK, Domin J, Waterfield MD. 1995. A family of phosphoinositide 3-kinases in Drosophila identifies a new mediator of signal transduction. Curr Biol 5:1404-1415. http://dx.doi.org/10.1016/S0960-9822 (95)00278-8.
    • (1995) Curr Biol , vol.5 , pp. 1404-1415
    • MacDougall, L.K.1    Domin, J.2    Waterfield, M.D.3
  • 44
    • 26244461921 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase C2alpha is essential for ATP-dependent priming of neurosecretory granule exocytosis
    • Meunier FA, Osborne SL, Hammond GR, Cooke FT, Parker PJ, Domin J, Schiavo G. 2005. Phosphatidylinositol 3-kinase C2alpha is essential for ATP-dependent priming of neurosecretory granule exocytosis. Mol Biol Cell 16:4841-4851. http://dx.doi.org/10.1091/mbc.E05-02-0171.
    • (2005) Mol Biol Cell , vol.16 , pp. 4841-4851
    • Meunier, F.A.1    Osborne, S.L.2    Hammond, G.R.3    Cooke, F.T.4    Parker, P.J.5    Domin, J.6    Schiavo, G.7
  • 47
    • 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. http://dx.doi.org/10.1093/emboj/cdg402.
    • (2003) EMBO J , vol.22 , pp. 4178-4189
    • Maffucci, T.1    Brancaccio, A.2    Piccolo, E.3    Stein, R.C.4    Falasca, M.5
  • 48
    • 84921777202 scopus 로고    scopus 로고
    • Dynamic shaping of cellular membranes by phospholipids and membrane-deforming proteins
    • Suetsugu S, Kurisu S, Takenawa T. 2014. Dynamic shaping of cellular membranes by phospholipids and membrane-deforming proteins. Physiol Rev 94:1219-1248. http://dx.doi.org/10.1152/physrev.00040.2013.
    • (2014) Physiol Rev , vol.94 , pp. 1219-1248
    • Suetsugu, S.1    Kurisu, S.2    Takenawa, T.3
  • 49
    • 0033591247 scopus 로고    scopus 로고
    • Insulin activates the alpha isoform of class II phosphoinositide 3-kinase
    • Brown RA, Domin J, Arcaro A, Waterfield MD, Shepherd PR. 1999. Insulin activates the alpha isoform of class II phosphoinositide 3-kinase. J Biol Chem 274:14529-14532. http://dx.doi.org/10.1074/jbc.274.21.14529.
    • (1999) J Biol Chem , vol.274 , pp. 14529-14532
    • Brown, R.A.1    Domin, J.2    Arcaro, A.3    Waterfield, M.D.4    Shepherd, P.R.5
  • 50
    • 31544439411 scopus 로고    scopus 로고
    • Actin-dependent movement of bacterial pathogens
    • Stevens JM, Galyov EE, Stevens MP. 2006. Actin-dependent movement of bacterial pathogens. Nat Rev Microbiol 4:91-101. http://dx.doi.org/10.1038/nrmicro1320.
    • (2006) Nat Rev Microbiol , vol.4 , pp. 91-101
    • Stevens, J.M.1    Galyov, E.E.2    Stevens, M.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.