메뉴 건너뛰기




Volumn 26, Issue 2, 2009, Pages 279-284

Cloning of a centaurin-α1 like gene MjCent involved in WSSV infection from shrimp Marsupeneaus japonicus

Author keywords

ARF6; centaurin 1; GAP; Marsupeneaus japonicus; PI3 K; virus; WSSV

Indexed keywords

CRUSTACEA; DECAPODA (CRUSTACEA); SHRIMP WHITE SPOT SYNDROME VIRUS;

EID: 60649101034     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2008.10.016     Document Type: Article
Times cited : (8)

References (37)
  • 1
    • 45849115442 scopus 로고    scopus 로고
    • Host-cell-dependent role of actin cytoskeleton during the replication of a human strain of influenza A virus
    • Arcangeletti M.C., De Conto F., Ferraglia F., Pinardi F., Gatti R., Orlandini G., et al. Host-cell-dependent role of actin cytoskeleton during the replication of a human strain of influenza A virus. Arch Virol 153 (2008) 1209-1221
    • (2008) Arch Virol , vol.153 , pp. 1209-1221
    • Arcangeletti, M.C.1    De Conto, F.2    Ferraglia, F.3    Pinardi, F.4    Gatti, R.5    Orlandini, G.6
  • 2
    • 35348879099 scopus 로고    scopus 로고
    • Baculovirus infectivity and the actin cytoskeleton
    • Volkman L.E. Baculovirus infectivity and the actin cytoskeleton. Curr Drug Targets 8 (2007) 1075-1083
    • (2007) Curr Drug Targets , vol.8 , pp. 1075-1083
    • Volkman, L.E.1
  • 3
    • 39149117352 scopus 로고    scopus 로고
    • Autophagy and antiviral immunity
    • Lee H.K., and Iwasaki A. Autophagy and antiviral immunity. Curr Opin Immunol 20 (2008) 23-29
    • (2008) Curr Opin Immunol , vol.20 , pp. 23-29
    • Lee, H.K.1    Iwasaki, A.2
  • 4
    • 15244362286 scopus 로고    scopus 로고
    • Differential profile of genes expressed in hemocytes of White Spot Syndrome Virus-resistant shrimp (Penaeus japonicus) by combining suppression subtractive hybridization and differential hybridization
    • He N., Qin Q., and Xu X. Differential profile of genes expressed in hemocytes of White Spot Syndrome Virus-resistant shrimp (Penaeus japonicus) by combining suppression subtractive hybridization and differential hybridization. Antiviral Res 66 (2005) 39-45
    • (2005) Antiviral Res , vol.66 , pp. 39-45
    • He, N.1    Qin, Q.2    Xu, X.3
  • 5
    • 18044369826 scopus 로고    scopus 로고
    • Interaction of white spot syndrome virus VP26 protein with actin
    • Xie X., and Yang F. Interaction of white spot syndrome virus VP26 protein with actin. Virology 336 (2005) 93-99
    • (2005) Virology , vol.336 , pp. 93-99
    • Xie, X.1    Yang, F.2
  • 6
    • 38649091675 scopus 로고    scopus 로고
    • Antiviral phagocytosis is regulated by a novel Rab-dependent complex in shrimp Penaeus japonicus
    • Wu W., Zong R., Xu J., and Zhang X. Antiviral phagocytosis is regulated by a novel Rab-dependent complex in shrimp Penaeus japonicus. J Proteome Res 7 (2008) 424-431
    • (2008) J Proteome Res , vol.7 , pp. 424-431
    • Wu, W.1    Zong, R.2    Xu, J.3    Zhang, X.4
  • 8
    • 0029763997 scopus 로고    scopus 로고
    • Identification and cloning of centaurin-α: a novel phosphatidylinositol 3,4,5-trisphosphate-binding protein from rat brain
    • Hammonds-Odie L.P., Jackson T.R., Profit A.A., Blader I.J., Turck C.W., Prestwich G.D., et al. Identification and cloning of centaurin-α: a novel phosphatidylinositol 3,4,5-trisphosphate-binding protein from rat brain. J Biol Chem 271 (1996) 18859-18868
    • (1996) J Biol Chem , vol.271 , pp. 18859-18868
    • Hammonds-Odie, L.P.1    Jackson, T.R.2    Profit, A.A.3    Blader, I.J.4    Turck, C.W.5    Prestwich, G.D.6
  • 9
    • 34047136098 scopus 로고    scopus 로고
    • PI-3-kinase-dependent membrane recruitment of centaurin-alpha2 is essential for its effect on ARF6-mediated actin cytoskeleton reorganization
    • Venkateswarlu K., Brandom K.G., and Yun H. PI-3-kinase-dependent membrane recruitment of centaurin-alpha2 is essential for its effect on ARF6-mediated actin cytoskeleton reorganization. J Cell Sci 120 (2007) 792-801
    • (2007) J Cell Sci , vol.120 , pp. 792-801
    • Venkateswarlu, K.1    Brandom, K.G.2    Yun, H.3
  • 11
    • 0034737658 scopus 로고    scopus 로고
    • Phosphoinositide-dependent activation of the ADP-ribosylation factor GTPase-activating protein ASAP1: evidence for the pleckstrin homology domain functioning as an allosteric site
    • Kam J.L., Miura K., Jackson T.R., Gruschus J., Roller P., Stauffer S., et al. Phosphoinositide-dependent activation of the ADP-ribosylation factor GTPase-activating protein ASAP1: evidence for the pleckstrin homology domain functioning as an allosteric site. J Biol Chem 275 (2000) 9653-9663
    • (2000) J Biol Chem , vol.275 , pp. 9653-9663
    • Kam, J.L.1    Miura, K.2    Jackson, T.R.3    Gruschus, J.4    Roller, P.5    Stauffer, S.6
  • 12
    • 1342282990 scopus 로고    scopus 로고
    • Centaurin-alpha1 is an in vivo phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating protein for ARF6 that is involved in actin cytoskeleton organization
    • Venkateswarlu K., Brandom K.G., and Lawrence J.L. Centaurin-alpha1 is an in vivo phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating protein for ARF6 that is involved in actin cytoskeleton organization. J Biol Chem 279 (2004) 6205-6208
    • (2004) J Biol Chem , vol.279 , pp. 6205-6208
    • Venkateswarlu, K.1    Brandom, K.G.2    Lawrence, J.L.3
  • 13
    • 33646184680 scopus 로고    scopus 로고
    • ARF proteins: roles in membrane traffic and beyond
    • D'Souza-Schorey C., and Chavrier P. ARF proteins: roles in membrane traffic and beyond. Nat Rev Mol Cell Biol 7 (2006) 347-358
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 347-358
    • D'Souza-Schorey, C.1    Chavrier, P.2
  • 14
    • 0035378663 scopus 로고    scopus 로고
    • Casein kinase I associates with members of the centaurin-alpha family of phosphatidylinositol 3,4,5-trisphosphate-binding proteins
    • Dubois T., Kerai P., Zemlickova E., Howell S., Jackson T.R., Venkateswarlu K., et al. Casein kinase I associates with members of the centaurin-alpha family of phosphatidylinositol 3,4,5-trisphosphate-binding proteins. J Biol Chem 276 (2001) 18757-18764
    • (2001) J Biol Chem , vol.276 , pp. 18757-18764
    • Dubois, T.1    Kerai, P.2    Zemlickova, E.3    Howell, S.4    Jackson, T.R.5    Venkateswarlu, K.6
  • 15
    • 0037165636 scopus 로고    scopus 로고
    • Identification of casein kinase Ialpha interacting protein partners
    • Dubois T., Howell S., Zemlickova E., and Aitken A. Identification of casein kinase Ialpha interacting protein partners. FEBS Lett 517 (2002) 167-171
    • (2002) FEBS Lett , vol.517 , pp. 167-171
    • Dubois, T.1    Howell, S.2    Zemlickova, E.3    Aitken, A.4
  • 16
    • 44649130056 scopus 로고    scopus 로고
    • RanBPM, a novel interaction partner of the brain-specific protein p42(IP4)/centaurin alpha-1
    • [Epub ahead of print]
    • Haase A., Nordmann C., Sedehizade F., Borrmann C., and Reiser G. RanBPM, a novel interaction partner of the brain-specific protein p42(IP4)/centaurin alpha-1. J Neurochem (2008 Mar 18) [Epub ahead of print]
    • (2008) J Neurochem
    • Haase, A.1    Nordmann, C.2    Sedehizade, F.3    Borrmann, C.4    Reiser, G.5
  • 17
    • 21044433466 scopus 로고    scopus 로고
    • Centaurin-alpha1 interacts directly with kinesin motor protein KIF13B
    • Venkateswarlu K., Hanada T., and Chishti A.H. Centaurin-alpha1 interacts directly with kinesin motor protein KIF13B. J Cell Sci 118 (2005) 2471-2484
    • (2005) J Cell Sci , vol.118 , pp. 2471-2484
    • Venkateswarlu, K.1    Hanada, T.2    Chishti, A.H.3
  • 18
    • 28844454228 scopus 로고    scopus 로고
    • Centaurin-alpha1 and KIF13B kinesin motor protein interaction in ARF6 signalling
    • Kanamarlapudi V. Centaurin-alpha1 and KIF13B kinesin motor protein interaction in ARF6 signalling. Biochem Soc Trans 33 (2005) 1279-1281
    • (2005) Biochem Soc Trans , vol.33 , pp. 1279-1281
    • Kanamarlapudi, V.1
  • 20
    • 23144450821 scopus 로고    scopus 로고
    • A novel and evolutionarily conserved PtdIns(3,4,5)P3-binding domain is necessary for DOCK180 signaling
    • Côté J.F., Motoyama A.B., and Bush J.A. A novel and evolutionarily conserved PtdIns(3,4,5)P3-binding domain is necessary for DOCK180 signaling. Nat Cell Biol 7 (2005) 797-807
    • (2005) Nat Cell Biol , vol.7 , pp. 797-807
    • Côté, J.F.1    Motoyama, A.B.2    Bush, J.A.3
  • 21
    • 0032407241 scopus 로고    scopus 로고
    • Phosphoinositide lipids as signaling molecules: common themes for signal transduction, cytoskeletal regulation, and membrane trafficking
    • Martin T.F. Phosphoinositide lipids as signaling molecules: common themes for signal transduction, cytoskeletal regulation, and membrane trafficking. Annu Rev Cell Dev Biol 14 (1998) 231-264
    • (1998) Annu Rev Cell Dev Biol , vol.14 , pp. 231-264
    • Martin, T.F.1
  • 22
    • 0032929762 scopus 로고    scopus 로고
    • Signalling through phosphoinositide 3-kinases: the lipids take centre stage
    • Leevers S.J., Vanhaesebroeck B., and Waterfield M.D. Signalling through phosphoinositide 3-kinases: the lipids take centre stage. Curr Opin Cell Biol 11 (1999) 219-225
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 219-225
    • Leevers, S.J.1    Vanhaesebroeck, B.2    Waterfield, M.D.3
  • 23
    • 35348858953 scopus 로고    scopus 로고
    • Regulation of hepatitis B virus replication by the phosphatidylinositol 3-kinase-akt signal transduction pathway
    • Guo H., Zhou T., Jiang D., et al. Regulation of hepatitis B virus replication by the phosphatidylinositol 3-kinase-akt signal transduction pathway. J Virol 81 (2007) 10072-10080
    • (2007) J Virol , vol.81 , pp. 10072-10080
    • Guo, H.1    Zhou, T.2    Jiang, D.3
  • 24
    • 37349043240 scopus 로고    scopus 로고
    • Rotavirus replication in intestinal cells differentially regulates integrin expression by a phosphatidylinositol 3-kinase-dependent pathway, resulting in increased cell adhesion and virus yield
    • Halasz P., Holloway G., Turner S.J., and Coulson B.S. Rotavirus replication in intestinal cells differentially regulates integrin expression by a phosphatidylinositol 3-kinase-dependent pathway, resulting in increased cell adhesion and virus yield. J Virol 82 (2008) 148-160
    • (2008) J Virol , vol.82 , pp. 148-160
    • Halasz, P.1    Holloway, G.2    Turner, S.J.3    Coulson, B.S.4
  • 25
    • 41149125404 scopus 로고    scopus 로고
    • Early phosphatidylinositol 3-kinase/Akt pathway activation limits poliovirus-induced JNK-mediated cell death
    • Autret A., Martin-Latil S., Brisac C., Mousson L., Colbère-Garapin F., and Blondel B. Early phosphatidylinositol 3-kinase/Akt pathway activation limits poliovirus-induced JNK-mediated cell death. J Virol 82 (2008) 3796-3802
    • (2008) J Virol , vol.82 , pp. 3796-3802
    • Autret, A.1    Martin-Latil, S.2    Brisac, C.3    Mousson, L.4    Colbère-Garapin, F.5    Blondel, B.6
  • 26
    • 33847644660 scopus 로고    scopus 로고
    • Effect of the phosphatidylinositol 3-kinase/Akt pathway on influenza A virus propagation
    • Shin Y.K., Liu Q., Tikoo S.K., Babiuk L.A., and Zhou Y. Effect of the phosphatidylinositol 3-kinase/Akt pathway on influenza A virus propagation. J Gen Virol 88 (2007) 942-950
    • (2007) J Gen Virol , vol.88 , pp. 942-950
    • Shin, Y.K.1    Liu, Q.2    Tikoo, S.K.3    Babiuk, L.A.4    Zhou, Y.5
  • 27
    • 33745753573 scopus 로고    scopus 로고
    • Bivalent role of the phosphatidylinositol-3-kinase(PI3K) during influenza virus infection and host cell defence
    • Christina E., Henju M., Thorsten W., Nurnberg B., Planz O., Pleschka S., et al. Bivalent role of the phosphatidylinositol-3-kinase(PI3K) during influenza virus infection and host cell defence. Cell Microbiol 8 (2006) 1336-1348
    • (2006) Cell Microbiol , vol.8 , pp. 1336-1348
    • Christina, E.1    Henju, M.2    Thorsten, W.3    Nurnberg, B.4    Planz, O.5    Pleschka, S.6
  • 28
    • 0033584404 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of a human homologue of centaurin-a1
    • Venkateswarlu K., and Cullen P.J. Molecular cloning and functional characterization of a human homologue of centaurin-a1. Biochem Biophys Res Commun 262 (1999) 237-244
    • (1999) Biochem Biophys Res Commun , vol.262 , pp. 237-244
    • Venkateswarlu, K.1    Cullen, P.J.2
  • 29
    • 0034306280 scopus 로고    scopus 로고
    • Cytohesins and centaurins: mediators of PI 3-kinase-regulated Arf signaling
    • Jackson T.R., Kearns B.G., and Theibert A.B. Cytohesins and centaurins: mediators of PI 3-kinase-regulated Arf signaling. Trends Biochem Sci 25 (2000) 489-495
    • (2000) Trends Biochem Sci , vol.25 , pp. 489-495
    • Jackson, T.R.1    Kearns, B.G.2    Theibert, A.B.3
  • 30
    • 13144276311 scopus 로고    scopus 로고
    • Identification of white spot syndrome virus (WSSV) envelope proteins involved in shrimp infection
    • Wu W., Wang L., and Zhang X. Identification of white spot syndrome virus (WSSV) envelope proteins involved in shrimp infection. Virology 332 (2005) 578-583
    • (2005) Virology , vol.332 , pp. 578-583
    • Wu, W.1    Wang, L.2    Zhang, X.3
  • 31
    • 33748734669 scopus 로고    scopus 로고
    • Detection of prawn white spot baculovirus by polymerase chain reaction
    • Wang W., He J., Yang F., Wu G., and Xu X. Detection of prawn white spot baculovirus by polymerase chain reaction. Acta Oceanol Sin 18 (1999) 591-598
    • (1999) Acta Oceanol Sin , vol.18 , pp. 591-598
    • Wang, W.1    He, J.2    Yang, F.3    Wu, G.4    Xu, X.5
  • 32
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2-ΔΔCT method
    • Livak K.J., and Schmittgen T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2-ΔΔCT method. Methods 25 (2001) 402-408
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 33
    • 0034688180 scopus 로고    scopus 로고
    • Identification of two major virion protein genes of white spot syndrome virus of shrimp
    • van Hulten M.C., Westenberg M., Goodall S.D., and Vlak J.M. Identification of two major virion protein genes of white spot syndrome virus of shrimp. Virology 266 (2000) 227-236
    • (2000) Virology , vol.266 , pp. 227-236
    • van Hulten, M.C.1    Westenberg, M.2    Goodall, S.D.3    Vlak, J.M.4
  • 34
    • 33644986197 scopus 로고    scopus 로고
    • Centaurin-α1 is a phosphatidylinositol 3-kinase-dependent activator of ERK1/2 mitogen-activated protein kinases
    • Hayashi H., Matsuzaki O., Muramatsu S., Tsuchiya Y., Harada T., Suzuki Y., et al. Centaurin-α1 is a phosphatidylinositol 3-kinase-dependent activator of ERK1/2 mitogen-activated protein kinases. J Biol Chem 281 (2006) 1332-1337
    • (2006) J Biol Chem , vol.281 , pp. 1332-1337
    • Hayashi, H.1    Matsuzaki, O.2    Muramatsu, S.3    Tsuchiya, Y.4    Harada, T.5    Suzuki, Y.6
  • 35
    • 0032530384 scopus 로고    scopus 로고
    • Identification and analysis of PH domain-containing targets of phosphatidylinositol 3-kinase using a novel in vivo assay in yeast
    • Steven J.I., Tim C., and Julian A. Identification and analysis of PH domain-containing targets of phosphatidylinositol 3-kinase using a novel in vivo assay in yeast. EMBO J 17 (1998) 5374-5387
    • (1998) EMBO J , vol.17 , pp. 5374-5387
    • Steven, J.I.1    Tim, C.2    Julian, A.3
  • 36
    • 0033151946 scopus 로고    scopus 로고
    • Identification of centaurin-α1 as a potential in vivo phosphatidylinositol 3,4,5-trisphosphate-binding protein that is functionally homologous to the yeast ADP-ribosylation factor (ARF) GTPase-activating protein, Gcs1
    • Venkateswarlu K., Oatey P.B., Tavaré J.M., Jackson T.R., and Cullen P.J. Identification of centaurin-α1 as a potential in vivo phosphatidylinositol 3,4,5-trisphosphate-binding protein that is functionally homologous to the yeast ADP-ribosylation factor (ARF) GTPase-activating protein, Gcs1. Biochem J 340 (1999) 359-363
    • (1999) Biochem J , vol.340 , pp. 359-363
    • Venkateswarlu, K.1    Oatey, P.B.2    Tavaré, J.M.3    Jackson, T.R.4    Cullen, P.J.5
  • 37
    • 3042850742 scopus 로고    scopus 로고
    • Identification of genes involved in the response of haemocytes of Penaeus japonicus by suppression subtractive hybridization (SSH) following microbial challenge
    • He N., Liu H., and Xu X. Identification of genes involved in the response of haemocytes of Penaeus japonicus by suppression subtractive hybridization (SSH) following microbial challenge. Fish Shellfish Immunol 17 (2004) 121-128
    • (2004) Fish Shellfish Immunol , vol.17 , pp. 121-128
    • He, N.1    Liu, H.2    Xu, X.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.