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Volumn 87, Issue 7, 2013, Pages 4121-4127

Alphaherpesviral US3 kinase induces cofilin dephosphorylation to reorganize the actin cytoskeleton

Author keywords

[No Author keywords available]

Indexed keywords

COFILIN; PROTEIN SERINE THREONINE KINASE; UNCLASSIFIED DRUG; US3 KINASE;

EID: 84875506475     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.03107-12     Document Type: Article
Times cited : (22)

References (48)
  • 1
    • 3142550529 scopus 로고    scopus 로고
    • The pseudorabies virus serine/threonine kinase Us3 contains mitochondrial, nuclear and membrane localization signals
    • Calton CM, Randall JA, Adkins MW, Banfield BW. 2004. The pseudorabies virus serine/threonine kinase Us3 contains mitochondrial, nuclear and membrane localization signals. Virus Genes 29:131-145.
    • (2004) Virus Genes , vol.29 , pp. 131-145
    • Calton, C.M.1    Randall, J.A.2    Adkins, M.W.3    Banfield, B.W.4
  • 2
    • 21144450684 scopus 로고    scopus 로고
    • Cytoskeletal rearrangements and cell extensions induced by the US3 kinase of an alphaherpesvirus are associated with enhanced spread
    • U.S.A.
    • Favoreel HW, Van Minnebruggen G, Adriaensen D, Nauwynck HJ. 2005. Cytoskeletal rearrangements and cell extensions induced by the US3 kinase of an alphaherpesvirus are associated with enhanced spread. Proc. Natl. Acad. Sci. U. S. A. 102:8990-8995.
    • (2005) Proc. Natl. Acad. Sci. , vol.102 , pp. 8990-8995
    • Favoreel, H.W.1    Van Minnebruggen, G.2    Adriaensen, D.3    Nauwynck, H.J.4
  • 3
    • 73949121101 scopus 로고    scopus 로고
    • Analysis of filamentous process induction and nuclear localization properties of the HSV-2 serine/threonine kinase Us3
    • Finnen RL, Roy BB, Zhang H, Banfield BW. 2010. Analysis of filamentous process induction and nuclear localization properties of the HSV-2 serine/threonine kinase Us3. Virology 397:23-33.
    • (2010) Virology , vol.397 , pp. 23-33
    • Finnen, R.L.1    Roy, B.B.2    Zhang, H.3    Banfield, B.W.4
  • 5
    • 0034487382 scopus 로고    scopus 로고
    • Expression of herpes simplex virus type 2 US3 affects the Cdc42/Rac pathway and attenuates c-Jun N-terminal kinase activation
    • Murata T, Goshima F, Daikoku T, Takakuwa H, Nishiyama Y. 2000. Expression of herpes simplex virus type 2 US3 affects the Cdc42/Rac pathway and attenuates c-Jun N-terminal kinase activation. Genes Cells 5:1017-1027.
    • (2000) Genes Cells , vol.5 , pp. 1017-1027
    • Murata, T.1    Goshima, F.2    Daikoku, T.3    Takakuwa, H.4    Nishiyama, Y.5
  • 6
    • 15244359449 scopus 로고    scopus 로고
    • The protein encoded by the US3 orthologue of Marek's disease virus is required for efficient de-envelopment of perinuclear virions and involved in actin stress fiber breakdown
    • Schumacher D, Tischer BK, Trapp S, Osterrieder N. 2005. The protein encoded by the US3 orthologue of Marek's disease virus is required for efficient de-envelopment of perinuclear virions and involved in actin stress fiber breakdown. J. Virol. 79:3987-3997.
    • (2005) J. Virol. , vol.79 , pp. 3987-3997
    • Schumacher, D.1    Tischer, B.K.2    Trapp, S.3    Osterrieder, N.4
  • 7
    • 0041707652 scopus 로고    scopus 로고
    • Pseudorabies virus US3 protein kinase mediates actin stress fiber breakdown
    • Van Minnebruggen G, Favoreel HW, Jacobs L, Nauwynck HJ. 2003. Pseudorabies virus US3 protein kinase mediates actin stress fiber breakdown. J. Virol. 77:9074-9080.
    • (2003) J. Virol. , vol.77 , pp. 9074-9080
    • Van Minnebruggen, G.1    Favoreel, H.W.2    Jacobs, L.3    Nauwynck, H.J.4
  • 9
    • 0029678546 scopus 로고    scopus 로고
    • Phosphorylation of Ser-3 of cofilin regulates its essential function on actin
    • Moriyama K, Iida K, Yahara I. 1996. Phosphorylation of Ser-3 of cofilin regulates its essential function on actin. Genes Cells 1:73-86.
    • (1996) Genes Cells , vol.1 , pp. 73-86
    • Moriyama, K.1    Iida, K.2    Yahara, I.3
  • 11
    • 33947359826 scopus 로고    scopus 로고
    • Expression of rotavirus NSP4 alters the actin network organization through the actin remodeling protein cofilin
    • Berkova Z, Crawford SE, Blutt SE, Morris AP, Estes MK. 2007. Expression of rotavirus NSP4 alters the actin network organization through the actin remodeling protein cofilin. J. Virol. 81:3545-3553.
    • (2007) J. Virol. , vol.81 , pp. 3545-3553
    • Berkova, Z.1    Crawford, S.E.2    Blutt, S.E.3    Morris, A.P.4    Estes, M.K.5
  • 12
    • 80051553821 scopus 로고    scopus 로고
    • InlB-mediated Listeria monocytogenes internalization requires a balanced phospholipase D activity maintained through phospho-cofilin
    • Han X, Yu R, Ji L, Zhen D, Tao S, Li S, Sun Y, Huang L, Feng Z, Li X, Han G, Schmidt M, Han L. 2011. InlB-mediated Listeria monocytogenes internalization requires a balanced phospholipase D activity maintained through phospho-cofilin. Mol. Microbiol. 81:860-880.
    • (2011) Mol. Microbiol. , vol.81 , pp. 860-880
    • Han, X.1    Yu, R.2    Ji, L.3    Zhen, D.4    Tao, S.5    Li, S.6    Sun, Y.7    Huang, L.8    Feng, Z.9    Li, X.10    Han, G.11    Schmidt, M.12    Han, L.13
  • 13
    • 84858297793 scopus 로고    scopus 로고
    • Porphyromonas gingivalis SerB-mediated dephosphorylation of host cell cofilin modulates invasion efficiency
    • Moffatt CE, Inaba H, Hirano T, Lamont RJ. 2012. Porphyromonas gingivalis SerB-mediated dephosphorylation of host cell cofilin modulates invasion efficiency. Cell Microbiol. 14:577-588.
    • (2012) Cell Microbiol. , vol.14 , pp. 577-588
    • Moffatt, C.E.1    Inaba, H.2    Hirano, T.3    Lamont, R.J.4
  • 17
    • 79953332144 scopus 로고    scopus 로고
    • LIM kinase 1 modulates cortical actin and CXCR4 cycling and is activated by HIV-1 to initiate viral infection
    • Vorster PJ, Guo J, Yoder A, Wang W, Zheng Y, Xu X, Yu D, Spear M, Wu Y. 2011. LIM kinase 1 modulates cortical actin and CXCR4 cycling and is activated by HIV-1 to initiate viral infection. J. Biol. Chem. 286: 12554-12564.
    • (2011) J. Biol. Chem. , vol.286 , pp. 12554-12564
    • Vorster, P.J.1    Guo, J.2    Yoder, A.3    Wang, W.4    Zheng, Y.5    Xu, X.6    Yu, D.7    Spear, M.8    Wu, Y.9
  • 20
    • 9944258951 scopus 로고    scopus 로고
    • The pseudorabies virus US3 protein kinase possesses anti-apoptotic activity that protects cells from apoptosis during infection and after treatment with sorbitol or staurosporine
    • Geenen K, Favoreel HW, Olsen L, Enquist LW, Nauwynck HJ. 2005. The pseudorabies virus US3 protein kinase possesses anti-apoptotic activity that protects cells from apoptosis during infection and after treatment with sorbitol or staurosporine. Virology 331:144-150.
    • (2005) Virology , vol.331 , pp. 144-150
    • Geenen, K.1    Favoreel, H.W.2    Olsen, L.3    Enquist, L.W.4    Nauwynck, H.J.5
  • 21
  • 22
    • 0028814399 scopus 로고
    • Effect of specific antibodies on the cell-associated spread of pseudorabies virus in monolayers of different cell types
    • Nauwynck HJ, Pensaert MB. 1995. Effect of specific antibodies on the cell-associated spread of pseudorabies virus in monolayers of different cell types. Arch. Virol. 140:1137-1146.
    • (1995) Arch. Virol. , vol.140 , pp. 1137-1146
    • Nauwynck, H.J.1    Pensaert, M.B.2
  • 24
    • 49749129617 scopus 로고    scopus 로고
    • Two viral kinases are required for sustained long distance axon transport of a neuroinvasive herpesvirus
    • Coller KE, Smith GA. 2008. Two viral kinases are required for sustained long distance axon transport of a neuroinvasive herpesvirus. Traffic 9:1458-1470.
    • (2008) Traffic , vol.9 , pp. 1458-1470
    • Coller, K.E.1    Smith, G.A.2
  • 26
    • 12344251814 scopus 로고    scopus 로고
    • Translational control in virus-infected cells: models for cellular stress responses
    • Clemens MJ. 2005. Translational control in virus-infected cells: models for cellular stress responses. Semin. Cell Dev. Biol. 16:13-20.
    • (2005) Semin. Cell Dev. Biol. , vol.16 , pp. 13-20
    • Clemens, M.J.1
  • 27
    • 0028265352 scopus 로고
    • Stress responses to viral infection
    • Jindal S, Malkovsky M. 1994. Stress responses to viral infection. Trends Microbiol. 2:89-91
    • (1994) Trends Microbiol. , vol.2 , pp. 89-91
    • Jindal, S.1    Malkovsky, M.2
  • 28
    • 0029684298 scopus 로고    scopus 로고
    • Viral infection
    • Santoro MG. 1996. Viral infection. EXS 77:337-357.
    • (1996) EXS , vol.77 , pp. 337-357
    • Santoro, M.G.1
  • 29
    • 79960415006 scopus 로고    scopus 로고
    • Overexpression of HSP70 inhibits cofilin phosphorylation and promotes lymphocyte migration in heat-stressed cells
    • Simard JP, Reynolds DN, Kraguljac AP, Smith GS, Mosser DD. 2011. Overexpression of HSP70 inhibits cofilin phosphorylation and promotes lymphocyte migration in heat-stressed cells. J. Cell Sci. 124:2367-2374.
    • (2011) J. Cell Sci. , vol.124 , pp. 2367-2374
    • Simard, J.P.1    Reynolds, D.N.2    Kraguljac, A.P.3    Smith, G.S.4    Mosser, D.D.5
  • 30
    • 55549103324 scopus 로고    scopus 로고
    • Effect of LIMK2 RNAi on reorganization of the actin cytoskeleton in osteoblasts induced by fluid shear stress
    • Fu Q, Wu C, Shen Y, Zheng S, Chen R. 2008. Effect of LIMK2 RNAi on reorganization of the actin cytoskeleton in osteoblasts induced by fluid shear stress. J. Biomech. 41:3225-3228.
    • (2008) J. Biomech. , vol.41 , pp. 3225-3228
    • Fu, Q.1    Wu, C.2    Shen, Y.3    Zheng, S.4    Chen, R.5
  • 31
    • 84886951305 scopus 로고    scopus 로고
    • Effects of cofilin phosphorylation on the actin cytoskeleton reorganization induced by shear stress
    • Liu YH, Li YR, Shao MF, Zhang XJ, Fu Q. 2010. Effects of cofilin phosphorylation on the actin cytoskeleton reorganization induced by shear stress. Zhonghua Kou Qiang Yi Xue Za Zhi 45:763-766.
    • (2010) Zhonghua Kou Qiang Yi Xue Za Zhi , vol.45 , pp. 763-766
    • Liu, Y.H.1    Li, Y.R.2    Shao, M.F.3    Zhang, X.J.4    Fu, Q.5
  • 33
    • 84857137299 scopus 로고    scopus 로고
    • Cofilin under control of beta-arrestin-2 in NMDA-dependent dendritic spine plasticity, long-term depression (LTD), and learning
    • Pontrello CG, Sun MY, Lin A, Fiacco TA, DeFea KA, Ethell IM. 2012. Cofilin under control of beta-arrestin-2 in NMDA-dependent dendritic spine plasticity, long-term depression (LTD), and learning. Proc. Natl. Acad. Sci. U. S. A. 109:E442-E451.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109
    • Pontrello, C.G.1    Sun, M.Y.2    Lin, A.3    Fiacco, T.A.4    DeFea, K.A.5    Ethell, I.M.6
  • 36
    • 77950514618 scopus 로고    scopus 로고
    • Lentiviral Nef proteins utilize PAK2-mediated deregulation of cofilin as a general strategy to interfere with actin remodeling
    • Stolp B, Abraham L, Rudolph JM, Fackler OT. 2010. Lentiviral Nef proteins utilize PAK2-mediated deregulation of cofilin as a general strategy to interfere with actin remodeling. J. Virol. 84:3935-3948.
    • (2010) J. Virol. , vol.84 , pp. 3935-3948
    • Stolp, B.1    Abraham, L.2    Rudolph, J.M.3    Fackler, O.T.4
  • 37
    • 33644508365 scopus 로고    scopus 로고
    • MAPKAPK-2-mediated LIM-kinase activation is critical for VEGFinduced actin remodeling and cell migration
    • Kobayashi M, Nishita M, Mishima T, Ohashi K, Mizuno K. 2006. MAPKAPK-2-mediated LIM-kinase activation is critical for VEGFinduced actin remodeling and cell migration. EMBO J. 25:713-726.
    • (2006) EMBO J. , vol.25 , pp. 713-726
    • Kobayashi, M.1    Nishita, M.2    Mishima, T.3    Ohashi, K.4    Mizuno, K.5
  • 39
    • 34249887660 scopus 로고    scopus 로고
    • LIM kinases: function, regulation and association with human disease
    • Scott RW, Olson MF. 2007. LIM kinases: function, regulation and association with human disease. J. Mol. Med. (Berl.) 85:555-568.
    • (2007) J. Mol. Med. (Berl.) , vol.85 , pp. 555-568
    • Scott, R.W.1    Olson, M.F.2
  • 40
    • 34547107639 scopus 로고    scopus 로고
    • Beta-arrestin-dependent regulation of the cofilin pathway downstream of protease-activated receptor-2
    • Zoudilova M, Kumar P, Ge L, Wang P, Bokoch GM, DeFea KA. 2007. Beta-arrestin-dependent regulation of the cofilin pathway downstream of protease-activated receptor-2. J. Biol. Chem. 282:20634-20646.
    • (2007) J. Biol. Chem. , vol.282 , pp. 20634-20646
    • Zoudilova, M.1    Kumar, P.2    Ge, L.3    Wang, P.4    Bokoch, G.M.5    DeFea, K.A.6
  • 41
    • 44949176114 scopus 로고    scopus 로고
    • Pak1 and Pak2 mediate tumor cell invasion through distinct signaling mechanisms
    • Coniglio SJ, Zavarella S, Symons MH. 2008. Pak1 and Pak2 mediate tumor cell invasion through distinct signaling mechanisms. Mol. Cell. Biol. 28:4162-4172.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 4162-4172
    • Coniglio, S.J.1    Zavarella, S.2    Symons, M.H.3
  • 42
    • 1042279545 scopus 로고    scopus 로고
    • Intracellular localization and functional effects of P21-activated kinase-1 (Pak1) in cardiac myocytes
    • Ke Y, Wang L, Pyle WG, de Tombe PP, Solaro RJ. 2004. Intracellular localization and functional effects of P21-activated kinase-1 (Pak1) in cardiac myocytes. Circ. Res. 94:194-200.
    • (2004) Circ. Res. , vol.94 , pp. 194-200
    • Ke, Y.1    Wang, L.2    Pyle, W.G.3    de Tombe, P.P.4    Solaro, R.J.5
  • 44
    • 78649510655 scopus 로고    scopus 로고
    • ALDH1L1 inhibits cell motility via dephosphorylation of cofilin by PP1 and PP2A
    • Oleinik NV, Krupenko NI, Krupenko SA. 2010. ALDH1L1 inhibits cell motility via dephosphorylation of cofilin by PP1 and PP2A. Oncogene 29:6233-6244.
    • (2010) Oncogene , vol.29 , pp. 6233-6244
    • Oleinik, N.V.1    Krupenko, N.I.2    Krupenko, S.A.3
  • 45
    • 0028286061 scopus 로고
    • Dephosphorylation of cofilin in stimulated platelets: roles for a GTP-binding protein and Ca2+
    • Davidson MM, Haslam RJ. 1994. Dephosphorylation of cofilin in stimulated platelets: roles for a GTP-binding protein and Ca2+. Biochem. J. 301(Pt 1):41-47.
    • (1994) Biochem. J. , vol.301 , Issue.PART 1 , pp. 41-47
    • Davidson, M.M.1    Haslam, R.J.2
  • 46
    • 0030601313 scopus 로고    scopus 로고
    • Dephosphorylation of cofilin in polymorphonuclear leukocytes derived from peripheral blood
    • Okada K, Takano-Ohmuro H, Obinata T, Abe H. 1996. Dephosphorylation of cofilin in polymorphonuclear leukocytes derived from peripheral blood. Exp. Cell Res. 227:116-122.
    • (1996) Exp. Cell Res. , vol.227 , pp. 116-122
    • Okada, K.1    Takano-Ohmuro, H.2    Obinata, T.3    Abe, H.4
  • 47
    • 0030004208 scopus 로고    scopus 로고
    • Inhibition of constitutive serine phosphatase activity in T lymphoma cells results in phosphorylation of pp19/cofilin and induces apoptosis
    • Samstag Y, Dreizler EM, Ambach A, Sczakiel G, Meuer SC. 1996. Inhibition of constitutive serine phosphatase activity in T lymphoma cells results in phosphorylation of pp19/cofilin and induces apoptosis. J. Immunol. 156:4167-4173.
    • (1996) J. Immunol. , vol.156 , pp. 4167-4173
    • Samstag, Y.1    Dreizler, E.M.2    Ambach, A.3    Sczakiel, G.4    Meuer, S.C.5


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