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Volumn 29, Issue 6, 2010, Pages 956-962

Characterization of two novel ADP ribosylation factors from the shrimp Marsupenaeus japonicus

Author keywords

ADP ribosylation factor; Marsupenaeus japonicus; MjArf1; MjArfn; WSSV

Indexed keywords

ANIMALIA; CRUSTACEA; DECAPODA (CRUSTACEA); HEXAPODA; MARSUPENAEUS JAPONICUS; SHRIMP WHITE SPOT SYNDROME VIRUS;

EID: 77957756323     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2010.08.003     Document Type: Article
Times cited : (12)

References (36)
  • 1
    • 21344488043 scopus 로고
    • Mass mortalities of cultured kuruma shrimp Penaeus japanicus in Japan in 1993: electron microscopic evidence of the causative virus
    • Inouye K., Miwa S., Oseko N., Nakaro H., Kimura T., Momoyama K., et al. Mass mortalities of cultured kuruma shrimp Penaeus japanicus in Japan in 1993: electron microscopic evidence of the causative virus. Fish Pathol 1994, 29:149-158.
    • (1994) Fish Pathol , vol.29 , pp. 149-158
    • Inouye, K.1    Miwa, S.2    Oseko, N.3    Nakaro, H.4    Kimura, T.5    Momoyama, K.6
  • 2
    • 0002661005 scopus 로고    scopus 로고
    • Shrimp white spot virus in the western hemisphere
    • Jory D.E., Dixon H.M. Shrimp white spot virus in the western hemisphere. Aquac Mag 1999, 25:83-91.
    • (1999) Aquac Mag , vol.25 , pp. 83-91
    • Jory, D.E.1    Dixon, H.M.2
  • 3
    • 38649091675 scopus 로고    scopus 로고
    • Antiviral phagocytosis is regulated by a novel Rab-dependent complex in shrimp Penaeus japonicus
    • Wu W.L., Zong R.R., Xu J.Y., Zhang X.B. Antiviral phagocytosis is regulated by a novel Rab-dependent complex in shrimp Penaeus japonicus. J Proteome Res 2008, 7:424-431.
    • (2008) J Proteome Res , vol.7 , pp. 424-431
    • Wu, W.L.1    Zong, R.R.2    Xu, J.Y.3    Zhang, X.B.4
  • 4
    • 65249168114 scopus 로고    scopus 로고
    • Ran GTPase regulates hemocytic phagocytosis of shrimp by interaction with myosin
    • Liu W.F., Han F., Zhang X.B. Ran GTPase regulates hemocytic phagocytosis of shrimp by interaction with myosin. J Proteome Res 2009, 8:1198-1206.
    • (2009) J Proteome Res , vol.8 , pp. 1198-1206
    • Liu, W.F.1    Han, F.2    Zhang, X.B.3
  • 5
    • 18744386949 scopus 로고    scopus 로고
    • Poliovirus protein induce membrane association of GTPase ADP-ribosylation factor
    • Belov G.A., Fogg M.H., Ehrenfeld E. Poliovirus protein induce membrane association of GTPase ADP-ribosylation factor. J Virol 2005, 79:7207-7216.
    • (2005) J Virol , vol.79 , pp. 7207-7216
    • Belov, G.A.1    Fogg, M.H.2    Ehrenfeld, E.3
  • 6
    • 34548172905 scopus 로고    scopus 로고
    • Activation of cellular Arf GTPases by poliovirus protein 3CD correlates with virus replication
    • Belov G.A., Habbersett C., Franco D., Ehrenfeld E. Activation of cellular Arf GTPases by poliovirus protein 3CD correlates with virus replication. J Virol 2007, 81:9259-9267.
    • (2007) J Virol , vol.81 , pp. 9259-9267
    • Belov, G.A.1    Habbersett, C.2    Franco, D.3    Ehrenfeld, E.4
  • 8
    • 0020069809 scopus 로고
    • Requirements for cholera toxin-dependent ADP-ribosylation of the purified regulatory component of adenylate cyclase
    • Schleifer L.S., Kahn R.A., Hanski E., Northup J.K., Sternweis P.C., Gilman A.G. Requirements for cholera toxin-dependent ADP-ribosylation of the purified regulatory component of adenylate cyclase. J Biol Chem 1982, 257:20-23.
    • (1982) J Biol Chem , vol.257 , pp. 20-23
    • Schleifer, L.S.1    Kahn, R.A.2    Hanski, E.3    Northup, J.K.4    Sternweis, P.C.5    Gilman, A.G.6
  • 9
    • 0021250807 scopus 로고
    • Purification of a protein cofactor required for ADP-ribosylation of the stimulatory regulatory component of adenylate cyclase by cholera toxin
    • Kahn R.A., Gilman A.G. Purification of a protein cofactor required for ADP-ribosylation of the stimulatory regulatory component of adenylate cyclase by cholera toxin. J Biol Chem 1984, 259:6228-6234.
    • (1984) J Biol Chem , vol.259 , pp. 6228-6234
    • Kahn, R.A.1    Gilman, A.G.2
  • 10
    • 23844548266 scopus 로고    scopus 로고
    • Localization and function of Arf family GTPase
    • Donaldson J.G., Honda A. Localization and function of Arf family GTPase. Biochem Soc Trans 2005, 33:639-642.
    • (2005) Biochem Soc Trans , vol.33 , pp. 639-642
    • Donaldson, J.G.1    Honda, A.2
  • 11
    • 33646184680 scopus 로고    scopus 로고
    • ARF proteins: roles in membrane traffic and beyond
    • D'Souza-Schorey C., Chavrier P. ARF proteins: roles in membrane traffic and beyond. Nat Rev Mol Cell Biol 2006, 7:347-358.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 347-358
    • D'Souza-Schorey, C.1    Chavrier, P.2
  • 12
    • 41149162021 scopus 로고    scopus 로고
    • Regulation of actin cytoskeleton dynamics by Arf-family GTPases
    • Myers K.R., Casanova J.E. Regulation of actin cytoskeleton dynamics by Arf-family GTPases. Trends Cell Biol 2008, 18:184-192.
    • (2008) Trends Cell Biol , vol.18 , pp. 184-192
    • Myers, K.R.1    Casanova, J.E.2
  • 14
    • 37749001768 scopus 로고    scopus 로고
    • ARF1 is directly involved in dynamin-independent endocytosis
    • Kumari S., Mayor S. ARF1 is directly involved in dynamin-independent endocytosis. Nat Cell Biol 2008, 10:30-41.
    • (2008) Nat Cell Biol , vol.10 , pp. 30-41
    • Kumari, S.1    Mayor, S.2
  • 16
    • 0028918959 scopus 로고
    • Inhibition of cellular protein secretion by poliovirus proteins 2B and 3A
    • Doedens J.R., Kirkegaard K. Inhibition of cellular protein secretion by poliovirus proteins 2B and 3A. EMBO J 1995, 14:894-907.
    • (1995) EMBO J , vol.14 , pp. 894-907
    • Doedens, J.R.1    Kirkegaard, K.2
  • 17
    • 0031926171 scopus 로고    scopus 로고
    • Brefeldin A inhibits cell-free, de novo synthesis of poliovirus
    • Cuconati A., Molla A., Wimmer E. Brefeldin A inhibits cell-free, de novo synthesis of poliovirus. J Virol 1998, 72:6456-6464.
    • (1998) J Virol , vol.72 , pp. 6456-6464
    • Cuconati, A.1    Molla, A.2    Wimmer, E.3
  • 19
    • 53849098555 scopus 로고    scopus 로고
    • HIV-1 Nef induces a Rab11-dependent routing of endocytosed immune costimulatory proteins CD80 and CD86 to the golgi
    • Chaudhry A., das Ranjan S., Jameel S., George A., Bal V., Mayor S., et al. HIV-1 Nef induces a Rab11-dependent routing of endocytosed immune costimulatory proteins CD80 and CD86 to the golgi. Traffic 2008, 8:1925-1935.
    • (2008) Traffic , vol.8 , pp. 1925-1935
    • Chaudhry, A.1    das Ranjan, S.2    Jameel, S.3    George, A.4    Bal, V.5    Mayor, S.6
  • 20
    • 60649101034 scopus 로고    scopus 로고
    • Cloning of a centaurin-α1 like gene MjCent involved in WSSV infection from shrimp Marsupeneaus japonicus
    • Wang H.F., Ma J.Y., Ruan L.W., Xu X. Cloning of a centaurin-α1 like gene MjCent involved in WSSV infection from shrimp Marsupeneaus japonicus. Fish Shellfish Immunol 2009, 26:279-284.
    • (2009) Fish Shellfish Immunol , vol.26 , pp. 279-284
    • Wang, H.F.1    Ma, J.Y.2    Ruan, L.W.3    Xu, X.4
  • 21
    • 73249119924 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a class II ADP ribosylation factor from the shrimp Marsupenaeus japonicus
    • Zhang M.C., Ma J.Y., Lei K.Y., Xu X. Molecular cloning and characterization of a class II ADP ribosylation factor from the shrimp Marsupenaeus japonicus. Fish Shellfish Immunol 2010, 28(1):128-133.
    • (2010) Fish Shellfish Immunol , vol.28 , Issue.1 , pp. 128-133
    • Zhang, M.C.1    Ma, J.Y.2    Lei, K.Y.3    Xu, X.4
  • 23
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0
    • Tamura K., Dudley J., Nei M., Kumar S. MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol Biol Evol 2007, 24:1596-1599.
    • (2007) Mol Biol Evol , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 24
    • 0031802483 scopus 로고    scopus 로고
    • The distribution and translocation of the G protein ADP-ribosylation factor 1 in live cells is determined by its GTPase activity
    • Vasudevan C., Han W.P., Tan Y.D., Nie Y.M., Li D.Q., Shome K., et al. The distribution and translocation of the G protein ADP-ribosylation factor 1 in live cells is determined by its GTPase activity. J Cell Sci 1998, 111:1277-1285.
    • (1998) J Cell Sci , vol.111 , pp. 1277-1285
    • Vasudevan, C.1    Han, W.P.2    Tan, Y.D.3    Nie, Y.M.4    Li, D.Q.5    Shome, K.6
  • 25
    • 0027953550 scopus 로고
    • Dominant inhibitory mutants of ARF1 block endoplasmic reticulum to golgi transport and trigger disassembly of the golgi apparatus
    • Dascher C., Balch W.E. Dominant inhibitory mutants of ARF1 block endoplasmic reticulum to golgi transport and trigger disassembly of the golgi apparatus. J Biol Chem 1994, 269:1437-1448.
    • (1994) J Biol Chem , vol.269 , pp. 1437-1448
    • Dascher, C.1    Balch, W.E.2
  • 26
    • 0026708135 scopus 로고
    • The amino terminus of ADP-ribosylation factor (ARF) is a critical determinant of ARF activities and is potent and specific inhibitor of protien transport
    • Kahn R.A., Randazzo P., Serafini T., Weiss O., Rulka C., Clark J., et al. The amino terminus of ADP-ribosylation factor (ARF) is a critical determinant of ARF activities and is potent and specific inhibitor of protien transport. J Biol Chem 1992, 267:13039-13046.
    • (1992) J Biol Chem , vol.267 , pp. 13039-13046
    • Kahn, R.A.1    Randazzo, P.2    Serafini, T.3    Weiss, O.4    Rulka, C.5    Clark, J.6
  • 27
    • 33748734669 scopus 로고    scopus 로고
    • Detection of prawn white spot baculovirus by polymerase chain reaction
    • Wang W., He J., Yang F., Wu G.K., Xu X. Detection of prawn white spot baculovirus by polymerase chain reaction. Acta Oceanol Sin 1999, 18:591-598.
    • (1999) Acta Oceanol Sin , vol.18 , pp. 591-598
    • Wang, W.1    He, J.2    Yang, F.3    Wu, G.K.4    Xu, X.5
  • 28
    • 49949095079 scopus 로고    scopus 로고
    • Mj-DWD, a double WAP domain-containing protein with antiviral relevance in Marsupenaeus japonicus
    • Chen D.D., He N.H., Xu X. Mj-DWD, a double WAP domain-containing protein with antiviral relevance in Marsupenaeus japonicus. Fish Shellfish Immunol 2008, 25:775-781.
    • (2008) Fish Shellfish Immunol , vol.25 , pp. 775-781
    • Chen, D.D.1    He, N.H.2    Xu, X.3
  • 30
    • 10044297008 scopus 로고    scopus 로고
    • Functional genomic analysis of the ADP-ribosylation factor family of GTPases: phylogeny among diverse eukaryotes and function in C. elegans
    • Li Y.W., Kelly W.G., Logsdon J.M., Schurko A.M., Harfe B.D., Hill-Harfe K.L., et al. Functional genomic analysis of the ADP-ribosylation factor family of GTPases: phylogeny among diverse eukaryotes and function in C. elegans. FASEB J 2004, 18:1834-1850.
    • (2004) FASEB J , vol.18 , pp. 1834-1850
    • Li, Y.W.1    Kelly, W.G.2    Logsdon, J.M.3    Schurko, A.M.4    Harfe, B.D.5    Hill-Harfe, K.L.6
  • 31
    • 0027482720 scopus 로고
    • Selective amplification of additional members of the ADP-ribosylation factor (ARF) family: cloning of additional human and Drosophila ARF-like genes
    • Clark J., Moore L., Krasinskas A., Way J., Battey J., Tamkun J., et al. Selective amplification of additional members of the ADP-ribosylation factor (ARF) family: cloning of additional human and Drosophila ARF-like genes. Proc Natl Acad Sci USA 1993, 90:8952-8956.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8952-8956
    • Clark, J.1    Moore, L.2    Krasinskas, A.3    Way, J.4    Battey, J.5    Tamkun, J.6
  • 32
    • 54249119254 scopus 로고    scopus 로고
    • Characterization of class I and II ADP-ribosylation factors (Arfs) in live cells: GDP-bound class II Arfs associate with the ER-golgi intermediate compartment independently of GBF1
    • Chun J., Shapovalova Z., Dejgaard S.Y., Presley J.F., Melançon P. Characterization of class I and II ADP-ribosylation factors (Arfs) in live cells: GDP-bound class II Arfs associate with the ER-golgi intermediate compartment independently of GBF1. Mol Biol Cell 2008, 19:3488-3500.
    • (2008) Mol Biol Cell , vol.19 , pp. 3488-3500
    • Chun, J.1    Shapovalova, Z.2    Dejgaard, S.Y.3    Presley, J.F.4    Melançon, P.5
  • 33
    • 43549119995 scopus 로고    scopus 로고
    • Localization and function of ADP ribosylation factor A in Aspergillus nidulans
    • Lee S.C., Show B.D. Localization and function of ADP ribosylation factor A in Aspergillus nidulans. FEMS Microbiol Lett 2008, 283:216-222.
    • (2008) FEMS Microbiol Lett , vol.283 , pp. 216-222
    • Lee, S.C.1    Show, B.D.2
  • 34
    • 0030891289 scopus 로고    scopus 로고
    • N-terminal hydrophobic residues of the G-protein ADP-ribosylation factor-1 insert into membrane phospholipids upon GDP to GTP exchange
    • Antonny B., Beraud-Dufour S., Chardin P., Chabre M. N-terminal hydrophobic residues of the G-protein ADP-ribosylation factor-1 insert into membrane phospholipids upon GDP to GTP exchange. Biochemistry 1997, 36:4675-4684.
    • (1997) Biochemistry , vol.36 , pp. 4675-4684
    • Antonny, B.1    Beraud-Dufour, S.2    Chardin, P.3    Chabre, M.4
  • 35
    • 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.H., Liu H.P., 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 2004, 17:121-128.
    • (2004) Fish Shellfish Immunol , vol.17 , pp. 121-128
    • He, N.H.1    Liu, H.P.2    Xu, X.3
  • 36
    • 4644229512 scopus 로고    scopus 로고
    • Differential gene expression profile in hepatopancreas of WSSV-resistant shrimp (Penaeus japonicus) by suppression subtractive hybridization
    • Pan D., He N.H., Yang Z.Y., Liu H.P., Xu X. Differential gene expression profile in hepatopancreas of WSSV-resistant shrimp (Penaeus japonicus) by suppression subtractive hybridization. Dev Comp Immunol 2005, 29:103-112.
    • (2005) Dev Comp Immunol , vol.29 , pp. 103-112
    • Pan, D.1    He, N.H.2    Yang, Z.Y.3    Liu, H.P.4    Xu, X.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.