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Volumn 88, Issue 17, 2014, Pages 9927-9933

Interactions between E6, FAK, and GIT1 at paxillin LD4 are necessary for transformation by bovine papillomavirus 1 E6

Author keywords

[No Author keywords available]

Indexed keywords

CELL CYCLE PROTEIN; FOCAL ADHESION KINASE 1; GIT1 PROTEIN, MOUSE; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; ONCOPROTEIN; PAXILLIN; PROTEIN E6, BOVINE PAPILLOMAVIRUS; PTK2 PROTEIN, MOUSE;

EID: 84921972565     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00552-14     Document Type: Article
Times cited : (7)

References (41)
  • 1
    • 0031001560 scopus 로고    scopus 로고
    • The bovine papillomavirus E6 oncoprotein interacts with paxillin and disrupts the actin cytoskeleton
    • Tong X, Howley PM. 1997. The bovine papillomavirus E6 oncoprotein interacts with paxillin and disrupts the actin cytoskeleton. Proc. Natl. Acad. Sci. U. S. A. 94:4412-4417. http://dx.doi.org/10.1073/pnas.94.9.4412.
    • (1997) Proc. Natl. Acad. Sci. U. S. A , vol.94 , pp. 4412-4417
    • Tong, X.1    Howley, P.M.2
  • 2
    • 0032495590 scopus 로고    scopus 로고
    • Association of bovine papillomavirus type 1 E6 oncoprotein with the focal adhesion protein paxillin through a conserved protein interaction motif
    • Vande Pol SB, Brown MC, Turner CE. 1998. Association of bovine papillomavirus type 1 E6 oncoprotein with the focal adhesion protein paxillin through a conserved protein interaction motif. Oncogene 16:43-52. http://dx.doi.org/10.1038/sj.onc.1201504.
    • (1998) Oncogene , vol.16 , pp. 43-52
    • Vande Pol, S.B.1    Brown, M.C.2    Turner, C.E.3
  • 3
    • 0031963628 scopus 로고    scopus 로고
    • Interaction of the bovine papillomavirus E6 protein with the clathrin adaptor complex AP-1
    • Tong X, Boll W, Kirchhausen T, Howley PM. 1998. Interaction of the bovine papillomavirus E6 protein with the clathrin adaptor complex AP-1. J. Virol. 72:476-482.
    • (1998) J. Virol , vol.72 , pp. 476-482
    • Tong, X.1    Boll, W.2    Kirchhausen, T.3    Howley, P.M.4
  • 4
    • 84867899491 scopus 로고    scopus 로고
    • Cutaneous papillomavirus E6 oncoproteins associate with MAML1 to repress transactivation andNOTCHsignaling
    • Brimer N, Lyons C, Wallberg AE, Vande Pol SB. 2012. Cutaneous papillomavirus E6 oncoproteins associate with MAML1 to repress transactivation andNOTCHsignaling. Oncogene 31:4639-4646. http://dx.doi.org/10.1038/onc.2011.589.
    • (2012) Oncogene , vol.31 , pp. 4639-4646
    • Brimer, N.1    Lyons, C.2    Wallberg, A.E.3    Vande Pol, S.B.4
  • 5
    • 84861875855 scopus 로고    scopus 로고
    • Cutaneous beta-human papillomavirus E6 proteins bind Mastermindlike coactivators and repress Notch signaling
    • Tan MJ, White EA, Sowa ME, Harper JW, Aster JC, Howley PM. 2012. Cutaneous beta-human papillomavirus E6 proteins bind Mastermindlike coactivators and repress Notch signaling. Proc. Natl. Acad. Sci. U. S. A. 109:E1473-E1480. http://dx.doi.org/10.1073/pnas.1205991109.
    • (2012) Proc. Natl. Acad. Sci. U. S. A , vol.109 , pp. E1473-E1480
    • Tan, M.J.1    White, E.A.2    Sowa, M.E.3    Harper, J.W.4    Aster, J.C.5    Howley, P.M.6
  • 7
    • 44949097476 scopus 로고    scopus 로고
    • Transformation by bovine papillomavirus type 1 E6 requires paxillin
    • Wade R, Brimer N, Vande Pol S. 2008. Transformation by bovine papillomavirus type 1 E6 requires paxillin. J. Virol. 82:5962-5966. http://dx.doi.org/10.1128/JVI.02747-07.
    • (2008) J. Virol , vol.82 , pp. 5962-5966
    • Wade, R.1    Brimer, N.2    Vande Pol, S.3
  • 8
    • 0027169680 scopus 로고
    • Localization of the E6-AP regions that direct human papillomavirus E6 binding, association with p53, and ubiquitination of associated proteins
    • Huibregtse JM, Scheffner M, Howley PM. 1993. Localization of the E6-AP regions that direct human papillomavirus E6 binding, association with p53, and ubiquitination of associated proteins. Mol. Cell. Biol. 13: 4918-4927.
    • (1993) Mol. Cell. Biol , vol.13 , pp. 4918-4927
    • Huibregtse, J.M.1    Scheffner, M.2    Howley, P.M.3
  • 9
    • 0032577466 scopus 로고    scopus 로고
    • Identification of an alpha helical motif sufficient for association with papillomavirus E6
    • Chen JJ, Hong Y, Rustamzadeh E, Baleja JD, Androphy EJ. 1998. Identification of an alpha helical motif sufficient for association with papillomavirus E6. J. Biol. Chem. 273:13537-13544. http://dx.doi.org/10.1074/jbc.273.22.13537.
    • (1998) J. Biol. Chem , vol.273 , pp. 13537-13544
    • Chen, J.J.1    Hong, Y.2    Rustamzadeh, E.3    Baleja, J.D.4    Androphy, E.J.5
  • 10
    • 33846359589 scopus 로고    scopus 로고
    • Association of E6AP (UBE3A) with human papillomavirus type 11 E6 protein
    • Brimer N, Lyons C, Vande Pol SB. 2007. Association of E6AP (UBE3A) with human papillomavirus type 11 E6 protein. Virology 358:303-310. http://dx.doi.org/10.1016/j.virol.2006.08.038.
    • (2007) Virology , vol.358 , pp. 303-310
    • Brimer, N.1    Lyons, C.2    Vande Pol, S.B.3
  • 11
    • 84870716604 scopus 로고    scopus 로고
    • Comprehensive analysis of host cellular interactions with human papillomavirus E6 proteins identifies new E6 binding partners and reflects viral diversity
    • White EA, Kramer RE, Tan MJ, Hayes SD, Harper JW, Howley PM. 2012. Comprehensive analysis of host cellular interactions with human papillomavirus E6 proteins identifies new E6 binding partners and reflects viral diversity. J. Virol. 86:13174-13186. http://dx.doi.org/10.1128/JVI.02172-12.
    • (2012) J. Virol , vol.86 , pp. 13174-13186
    • White, E.A.1    Kramer, R.E.2    Tan, M.J.3    Hayes, S.D.4    Harper, J.W.5    Howley, P.M.6
  • 12
    • 0036142219 scopus 로고    scopus 로고
    • The adaptor protein paxillin is essential for normal development in the mouse and is a critical transducer of fibronectin signaling
    • Hagel M, George EL, Kim A, Tamimi R, Opitz SL, Turner CE, Imamoto A, Thomas SM. 2002. The adaptor protein paxillin is essential for normal development in the mouse and is a critical transducer of fibronectin signaling. Mol. Cell. Biol. 22:901-915. http://dx.doi.org/10.1128/MCB.22.3.901-915.2002.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 901-915
    • Hagel, M.1    George, E.L.2    Kim, A.3    Tamimi, R.4    Opitz, S.L.5    Turner, C.E.6    Imamoto, A.7    Thomas, S.M.8
  • 13
    • 12844269955 scopus 로고    scopus 로고
    • Regulation of Rho and Rac signaling to the actin cytoskeleton by paxillin during Drosophila development
    • Chen GC, Turano B, Ruest PJ, Hagel M, Settleman J, Thomas SM. 2005. Regulation of Rho and Rac signaling to the actin cytoskeleton by paxillin during Drosophila development. Mol. Cell. Biol. 25:979-987. http://dx.doi.org/10.1128/MCB.25.3.979-987.2005.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 979-987
    • Chen, G.C.1    Turano, B.2    Ruest, P.J.3    Hagel, M.4    Settleman, J.5    Thomas, S.M.6
  • 14
    • 50249107474 scopus 로고    scopus 로고
    • Paxillin comes of age
    • Deakin NO, Turner CE. 2008. Paxillin comes of age. J. Cell Sci. 121:2435-2444. http://dx.doi.org/10.1242/jcs.018044.
    • (2008) J. Cell Sci , vol.121 , pp. 2435-2444
    • Deakin, N.O.1    Turner, C.E.2
  • 15
    • 33748286819 scopus 로고    scopus 로고
    • Integrin-regulated FAK-Src signaling in normal and cancer cells
    • Mitra SK, Schlaepfer DD. 2006. Integrin-regulated FAK-Src signaling in normal and cancer cells. Curr. Opin. Cell Biol. 18:516-523. http://dx.doi.org/10.1016/j.ceb.2006.08.011.
    • (2006) Curr. Opin. Cell Biol , vol.18 , pp. 516-523
    • Mitra, S.K.1    Schlaepfer, D.D.2
  • 16
    • 0032513047 scopus 로고    scopus 로고
    • Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin
    • Shen Y, Schneider G, Cloutier JF, Veillette A, Schaller MD. 1998. Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin. J. Biol. Chem. 273:6474-6481. http://dx.doi.org/10.1074/jbc.273.11.6474.
    • (1998) J. Biol. Chem , vol.273 , pp. 6474-6481
    • Shen, Y.1    Schneider, G.2    Cloutier, J.F.3    Veillette, A.4    Schaller, M.D.5
  • 18
    • 0141533030 scopus 로고    scopus 로고
    • Illuminating adhesion complexes in migrating cells: moving toward a bright future
    • Webb DJ, Brown CM, Horwitz AF. 2003. Illuminating adhesion complexes in migrating cells: moving toward a bright future. Curr. Opin. Cell Biol. 15:614-620. http://dx.doi.org/10.1016/S0955-0674(03)00105-4.
    • (2003) Curr. Opin. Cell Biol , vol.15 , pp. 614-620
    • Webb, D.J.1    Brown, C.M.2    Horwitz, A.F.3
  • 20
    • 84870209800 scopus 로고    scopus 로고
    • Rho family GTPases
    • Hall A. 2012. Rho family GTPases. Biochem. Soc. Trans. 40:1378-1382. http://dx.doi.org/10.1042/BST20120103.
    • (2012) Biochem. Soc. Trans , vol.40 , pp. 1378-1382
    • Hall, A.1
  • 21
    • 80055066706 scopus 로고    scopus 로고
    • Paxillin enables attachment-independent tyrosine phosphorylation of focal adhesion kinase and transformation by RAS
    • Wade R, Brimer N, Lyons C, Vande Pol S. 2011. Paxillin enables attachment-independent tyrosine phosphorylation of focal adhesion kinase and transformation by RAS. J. Biol. Chem. 286:37932-37944. http://dx.doi.org/10.1074/jbc.M111.294504.
    • (2011) J. Biol. Chem , vol.286 , pp. 37932-37944
    • Wade, R.1    Brimer, N.2    Lyons, C.3    Vande Pol, S.4
  • 22
    • 0034739856 scopus 로고    scopus 로고
    • Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion
    • Nikolopoulos SN, Turner CE. 2000. Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion. J. Cell Biol. 151:1435-1448. http://dx.doi.org/10.1083/jcb.151.7.1435.
    • (2000) J. Cell Biol , vol.151 , pp. 1435-1448
    • Nikolopoulos, S.N.1    Turner, C.E.2
  • 23
    • 0035968234 scopus 로고    scopus 로고
    • Integrin-linked kinase (ILK) binding to paxillin LD1 motif regulates ILK localization to focal adhesions
    • Nikolopoulos SN, Turner CE. 2001. Integrin-linked kinase (ILK) binding to paxillin LD1 motif regulates ILK localization to focal adhesions. J. Biol. Chem. 276:23499-23505. http://dx.doi.org/10.1074/jbc.M102163200.
    • (2001) J. Biol. Chem , vol.276 , pp. 23499-23505
    • Nikolopoulos, S.N.1    Turner, C.E.2
  • 24
    • 84873152707 scopus 로고    scopus 로고
    • NMR structure of integrin alpha4 cytosolic tail and its interactions with paxillin
    • Chua GL, Patra AT, Tan SM, Bhattacharjya S. 2013. NMR structure of integrin alpha4 cytosolic tail and its interactions with paxillin. PLoS One 8:e55184. http://dx.doi.org/10.1371/journal.pone.0055184.
    • (2013) PLoS One , vol.8
    • Chua, G.L.1    Patra, A.T.2    Tan, S.M.3    Bhattacharjya, S.4
  • 25
    • 84964902871 scopus 로고    scopus 로고
    • Stability of the tumor suppressor merlin depends on its ability to bind paxillin LD3 and associate with beta1 integrin and actin at the plasma membrane
    • Manetti ME, Geden S, Bott M, Sparrow N, Lambert S, Fernandez-Valle C. 2012. Stability of the tumor suppressor merlin depends on its ability to bind paxillin LD3 and associate with beta1 integrin and actin at the plasma membrane. Biol. Open 1:949-957. http://dx.doi.org/10.1242/bio.20122121.
    • (2012) Biol. Open , vol.1 , pp. 949-957
    • Manetti, M.E.1    Geden, S.2    Bott, M.3    Sparrow, N.4    Lambert, S.5    Fernandez-Valle, C.6
  • 26
    • 30744468126 scopus 로고    scopus 로고
    • Minimal features of paxillin that are required for the tyrosine phosphorylation of focal adhesion kinase
    • Wade R, Vande Pol S. 2006. Minimal features of paxillin that are required for the tyrosine phosphorylation of focal adhesion kinase. Biochem. J. 393:565-573. http://dx.doi.org/10.1042/BJ20051241.
    • (2006) Biochem. J , vol.393 , pp. 565-573
    • Wade, R.1    Vande Pol, S.2
  • 27
    • 0031439110 scopus 로고    scopus 로고
    • The bovine papillomavirus E6 protein binds to the LD motif repeats of paxillin and blocks its interaction with vinculin and the focal adhesion kinase
    • Tong X, Salgia R, Li JL, Griffin JD, Howley PM. 1997. The bovine papillomavirus E6 protein binds to the LD motif repeats of paxillin and blocks its interaction with vinculin and the focal adhesion kinase. J. Biol. Chem. 272:33373-33376. http://dx.doi.org/10.1074/jbc.272.52.33373.
    • (1997) J. Biol. Chem , vol.272 , pp. 33373-33376
    • Tong, X.1    Salgia, R.2    Li, J.L.3    Griffin, J.D.4    Howley, P.M.5
  • 28
    • 0029827130 scopus 로고    scopus 로고
    • Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding
    • Brown MC, Perotta JA, Turner CE. 1996. Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding. J. Cell. Biol. 135:1109-1123. http://dx.doi.org/10.1083/jcb.135.4.1109.
    • (1996) J. Cell. Biol , vol.135 , pp. 1109-1123
    • Brown, M.C.1    Perotta, J.A.2    Turner, C.E.3
  • 29
    • 0039180030 scopus 로고    scopus 로고
    • Intact LIM 3 and LIM 4 domains of paxillin are required for the association to a novel polyproline region (Pro 2) of protein-tyrosine phosphatase-PEST
    • Cote JF, Turner CE, Tremblay ML. 1999. Intact LIM 3 and LIM 4 domains of paxillin are required for the association to a novel polyproline region (Pro 2) of protein-tyrosine phosphatase-PEST. J. Biol. Chem. 274: 20550-20560. http://dx.doi.org/10.1074/jbc.274.29.20550.
    • (1999) J. Biol. Chem , vol.274 , pp. 20550-20560
    • Cote, J.F.1    Turner, C.E.2    Tremblay, M.L.3
  • 30
    • 0028171070 scopus 로고
    • Characterization of the TGF beta 1-inducible hic-5 gene that encodes a putative novel zinc finger protein and its possible involvement in cellular senescence
    • Shibanuma M, Mashimo J, Kuroki T, Nose K. 1994. Characterization of the TGF beta 1-inducible hic-5 gene that encodes a putative novel zinc finger protein and its possible involvement in cellular senescence. J. Biol. Chem. 269:26767-26774.
    • (1994) J. Biol. Chem , vol.269 , pp. 26767-26774
    • Shibanuma, M.1    Mashimo, J.2    Kuroki, T.3    Nose, K.4
  • 31
    • 3843126775 scopus 로고    scopus 로고
    • A LIM protein, Hic-5, functions as a potential coactivator for Sp1
    • Shibanuma M, Kim-Kaneyama JR, Sato S, Nose K. 2004. A LIM protein, Hic-5, functions as a potential coactivator for Sp1. J. Cell. Biochem. 91: 633-645. http://dx.doi.org/10.1002/jcb.10754.
    • (2004) J. Cell. Biochem , vol.91 , pp. 633-645
    • Shibanuma, M.1    Kim-Kaneyama, J.R.2    Sato, S.3    Nose, K.4
  • 32
    • 33746921906 scopus 로고    scopus 로고
    • Hic-5/ARA55, a LIM domaincontaining nuclear receptor coactivator expressed in prostate stromal cells
    • Heitzer MD, DeFranco DB. 2006. Hic-5/ARA55, a LIM domaincontaining nuclear receptor coactivator expressed in prostate stromal cells. Cancer Res. 66:7326-7333. http://dx.doi.org/10.1158/0008-5472.CAN-05-2379.
    • (2006) Cancer Res , vol.66 , pp. 7326-7333
    • Heitzer, M.D.1    DeFranco, D.B.2
  • 33
    • 56649106486 scopus 로고    scopus 로고
    • Smad7 is inactivated through a direct physical interaction with the LIM protein Hic-5/ARA55
    • Wang H, Song K, Krebs TL, Yang J, Danielpour D. 2008. Smad7 is inactivated through a direct physical interaction with the LIM protein Hic-5/ARA55. Oncogene 27:6791-6805. http://dx.doi.org/10.1038/onc.2008.291.
    • (2008) Oncogene , vol.27 , pp. 6791-6805
    • Wang, H.1    Song, K.2    Krebs, T.L.3    Yang, J.4    Danielpour, D.5
  • 34
    • 0031027206 scopus 로고    scopus 로고
    • Induction of senescence-like phenotypes by forced expression of hic-5, which encodes a novel LIM motif protein, in immortalized human fibroblasts
    • Shibanuma M, Mochizuki E, Maniwa R, Mashimo J, Nishiya N, Imai S, Takano T, Oshimura M, Nose K. 1997. Induction of senescence-like phenotypes by forced expression of hic-5, which encodes a novel LIM motif protein, in immortalized human fibroblasts. Mol. Cell. Biol. 17: 1224-1235.
    • (1997) Mol. Cell. Biol , vol.17 , pp. 1224-1235
    • Shibanuma, M.1    Mochizuki, E.2    Maniwa, R.3    Mashimo, J.4    Nishiya, N.5    Imai, S.6    Takano, T.7    Oshimura, M.8    Nose, K.9
  • 37
    • 0034713295 scopus 로고    scopus 로고
    • Competitive binding to a charged leucine motif represses transformation by a papillomavirus E6 oncoprotein
    • Bohl J, Das K, Dasgupta B, Vande Pol SB. 2000. Competitive binding to a charged leucine motif represses transformation by a papillomavirus E6 oncoprotein. Virology 271:163-170. http://dx.doi.org/10.1006/viro.2000.0316.
    • (2000) Virology , vol.271 , pp. 163-170
    • Bohl, J.1    Das, K.2    Dasgupta, B.3    Vande Pol, S.B.4
  • 38
    • 0039797301 scopus 로고
    • Cap-independent translation of mRNA conferred by encephalomyocarditis virus 5= sequence improves the performance of the vaccinia virus/bacteriophage T7 hybrid expression system
    • Elroy-Stein O, Fuerst TR, Moss B. 1989. Cap-independent translation of mRNA conferred by encephalomyocarditis virus 5= sequence improves the performance of the vaccinia virus/bacteriophage T7 hybrid expression system. Proc. Natl. Acad. Sci. U. S. A. 86:6126-6130. http://dx.doi.org/10.1073/pnas.86.16.6126.
    • (1989) Proc. Natl. Acad. Sci. U. S. A , vol.86 , pp. 6126-6130
    • Elroy-Stein, O.1    Fuerst, T.R.2    Moss, B.3
  • 39
    • 70349243073 scopus 로고    scopus 로고
    • The stability of the human papillomavirus E6 oncoprotein is E6AP dependent
    • Tomaic V, Pim D, Banks L. 2009. The stability of the human papillomavirus E6 oncoprotein is E6AP dependent. Virology 393:7-10. http://dx.doi.org/10.1016/j.virol.2009.07.029.
    • (2009) Virology , vol.393 , pp. 7-10
    • Tomaic, V.1    Pim, D.2    Banks, L.3
  • 40
    • 84869072384 scopus 로고    scopus 로고
    • Peptide interactions stabilize and restructure human papillomavirus type 16 E6 to interact with p53
    • Ansari T, Brimer N, Vande Pol SB. 2012. Peptide interactions stabilize and restructure human papillomavirus type 16 E6 to interact with p53. J. Virol. 86:11386-11391. http://dx.doi.org/10.1128/JVI.01236-12.
    • (2012) J. Virol , vol.86 , pp. 11386-11391
    • Ansari, T.1    Brimer, N.2    Vande Pol, S.B.3
  • 41
    • 0037012038 scopus 로고    scopus 로고
    • Paxillin null embryonic stem cells are impaired in cell spreading and tyrosine phosphorylation of focal adhesion kinase
    • Wade R, Bohl J, Vande Pol S. 2002. Paxillin null embryonic stem cells are impaired in cell spreading and tyrosine phosphorylation of focal adhesion kinase. Oncogene 21:96-107. http://dx.doi.org/10.1038/sj.onc.1205013.
    • (2002) Oncogene , vol.21 , pp. 96-107
    • Wade, R.1    Bohl, J.2    Vande Pol, S.3


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