메뉴 건너뛰기




Volumn 85, Issue 22, 2011, Pages 11544-11556

Emerging theme: Cellular PDZ proteins as common targets of pathogenic viruses

Author keywords

[No Author keywords available]

Indexed keywords

APC PROTEIN; CELL PROTEIN; CYSTIC FIBROSIS TRANSMEMBRANE REGULATOR ASSOCIATED LIGAND; E4 ORF1 PROTEIN; GUANYLATE KINASE; INTERLEUKIN 6 PRECURSOR; MAGI 1 PROTEIN; MAGI 3 PROTEIN; MUPP1 PROTEIN; NON RECEPTOR PROTEIN TYROSINE PHOSPHATASE 13; NONSTRUCTURAL PROTEIN 1; PAR3 PROTEIN; PATJ PROTEIN; PDZ PROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN DLG1; PROTEIN E6; PROTEIN E7; PROTEIN PRECURSOR; PROTEIN ZO2; TAX INTERACTING PROTEIN 1; TAX INTERACTING PROTEIN 2; TAX PROTEIN; TIP 1 PROTEIN; TIP 2 PROTEIN; TRANSFORMING GROWTH FACTOR BETA; UNCLASSIFIED DRUG; VIRUS ENVELOPE PROTEIN; VIRUS GLYCOPROTEIN; VIRUS PROTEIN;

EID: 80655143495     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.05410-11     Document Type: Short Survey
Times cited : (159)

References (135)
  • 1
    • 25844489958 scopus 로고    scopus 로고
    • The mammalian homolog of the Drosophila discs large tumor suppressor protein up-regulates expression of the ELR+ CXC chemokine Scyb5
    • Aiba, T., et al. 2005. The mammalian homolog of the Drosophila discs large tumor suppressor protein up-regulates expression of the ELR+ CXC chemokine Scyb5. Biochem. Biophys. Res. Commun. 337:191-194.
    • (2005) Biochem. Biophys. Res. Commun. , vol.337 , pp. 191-194
    • Aiba, T.1
  • 2
    • 77951236855 scopus 로고    scopus 로고
    • The PDZ domain binding motif (PBM) of human T-cell leukemia virus type 1 Tax can be substituted by heterologous PBMs from viral oncoproteins during T-cell transformation
    • Aoyagi, T., et al. 2010. The PDZ domain binding motif (PBM) of human T-cell leukemia virus type 1 Tax can be substituted by heterologous PBMs from viral oncoproteins during T-cell transformation. Virus Genes 40:193- 199.
    • (2010) Virus Genes , vol.40 , pp. 193-199
    • Aoyagi, T.1
  • 3
    • 36349027945 scopus 로고    scopus 로고
    • The PDZ domain-binding motif of the human T cell leukemia virus type 1 tax protein induces mislocalization of the tumor suppressor hScrib in T cells
    • Arpin-André, C., and J. M. Mesnard. 2007. The PDZ domain-binding motif of the human T cell leukemia virus type 1 tax protein induces mislocalization of the tumor suppressor hScrib in T cells. J. Biol. Chem. 282:33132- 33141.
    • (2007) J. Biol. Chem. , vol.282 , pp. 33132-33141
    • Arpin-André, C.1    Mesnard, J.M.2
  • 4
    • 23044480130 scopus 로고    scopus 로고
    • Engagement of specific T-cell surface molecules regulates cytoskeletal polarization in HTLV-1-infected lymphocytes
    • Barnard, A. L., T. Igakura, Y. Tanaka, G. P. Taylor, and C. R. Bangham. 2005. Engagement of specific T-cell surface molecules regulates cytoskeletal polarization in HTLV-1-infected lymphocytes. Blood 106:988-995.
    • (2005) Blood , vol.106 , pp. 988-995
    • Barnard, A.L.1    Igakura, T.2    Tanaka, Y.3    Taylor, G.P.4    Bangham, C.R.5
  • 5
    • 77957300625 scopus 로고    scopus 로고
    • The pleiotropic protein kinase CK2 phosphorylates HTLV-1 Tax protein in vitro, targeting its PDZ-binding motif
    • Bidoia, C., et al. 2010. The pleiotropic protein kinase CK2 phosphorylates HTLV-1 Tax protein in vitro, targeting its PDZ-binding motif. Virus Genes 41:149-157.
    • (2010) Virus Genes , vol.41 , pp. 149-157
    • Bidoia, C.1
  • 6
    • 4444251676 scopus 로고    scopus 로고
    • Human Dlg protein binds to the envelope glycoproteins of human T-cell leukemia virus type 1 and regulates envelope mediated cell-cell fusion in T lymphocytes
    • Blot, V., et al. 2004. Human Dlg protein binds to the envelope glycoproteins of human T-cell leukemia virus type 1 and regulates envelope mediated cell-cell fusion in T lymphocytes. J. Cell Sci. 117:3983-3993.
    • (2004) J. Cell Sci. , vol.117 , pp. 3983-3993
    • Blot, V.1
  • 7
    • 0035059418 scopus 로고    scopus 로고
    • The immunological synapse
    • Bromley, S. K., et al. 2001. The immunological synapse. Annu. Rev. Immunol. 19:375-396.
    • (2001) Annu. Rev. Immunol. , vol.19 , pp. 375-396
    • Bromley, S.K.1
  • 8
    • 3242889812 scopus 로고    scopus 로고
    • Differential expression of the human homologue of drosophila discs large oncosuppressor in histologic samples from human papillomavirus-associated lesions as a marker for progression to malignancy
    • Cavatorta, A. L., et al. 2004. Differential expression of the human homologue of drosophila discs large oncosuppressor in histologic samples from human papillomavirus-associated lesions as a marker for progression to malignancy. Int. J. Cancer 111:373-380.
    • (2004) Int. J. Cancer , vol.111 , pp. 373-380
    • Cavatorta, A.L.1
  • 9
    • 39849107737 scopus 로고    scopus 로고
    • Functionally distinct monomers and trimers produced by a viral oncoprotein
    • Chung, S. H., R. S. Weiss, B. V. V. Prasad, and R. T. Javier. 2008. Functionally distinct monomers and trimers produced by a viral oncoprotein. Oncogene 27:1412-1420.
    • (2008) Oncogene , vol.27 , pp. 1412-1420
    • Chung, S.H.1    Weiss, R.S.2    Prasad, B.V.V.3    Javier, R.T.4
  • 10
    • 0032441833 scopus 로고    scopus 로고
    • Altered gap and tight junctions in human thyroid oncocytic tumors: a study of 8 cases by freeze-fracture
    • Cochand-Priollet, B., et al. 1998. Altered gap and tight junctions in human thyroid oncocytic tumors: a study of 8 cases by freeze-fracture. Ultrastruct. Pathol. 22:413-420.
    • (1998) Ultrastruct. Pathol. , vol.22 , pp. 413-420
    • Cochand-Priollet, B.1
  • 11
    • 33644854068 scopus 로고    scopus 로고
    • Erbin inhibits RAF activation by disrupting the sur-8-Ras-Raf complex
    • Dai, P., W. C. Xiong, and L. Mei. 2006. Erbin inhibits RAF activation by disrupting the sur-8-Ras-Raf complex. J. Biol. Chem. 281:927-933.
    • (2006) J. Biol. Chem. , vol.281 , pp. 927-933
    • Dai, P.1    Xiong, W.C.2    Mei, L.3
  • 12
    • 24944508592 scopus 로고    scopus 로고
    • Association of cottontail rabbit papillomavirus E6 oncoproteins with the hDlg/SAP97 tumor suppressor
    • Du, M., et al. 2005. Association of cottontail rabbit papillomavirus E6 oncoproteins with the hDlg/SAP97 tumor suppressor. J. Cell. Biochem. 94:1038-1045.
    • (2005) J. Cell. Biochem. , vol.94 , pp. 1038-1045
    • Du, M.1
  • 13
    • 0037385738 scopus 로고    scopus 로고
    • Viral spread through protoplasmic kiss
    • Dustin, M. 2003. Viral spread through protoplasmic kiss. Nat. Cell Biol. 5:271-272.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 271-272
    • Dustin, M.1
  • 14
    • 64849087370 scopus 로고    scopus 로고
    • Flavivirus NS5 associates with host-cell proteins zonula occludens-1 (ZO-1) and regulating synaptic membrane exocytosis-2 (RIMS2) via an internal PDZ binding mechanism
    • Ellencrona, K., A. Syed, and M. Johansson. 2009. Flavivirus NS5 associates with host-cell proteins zonula occludens-1 (ZO-1) and regulating synaptic membrane exocytosis-2 (RIMS2) via an internal PDZ binding mechanism. Biol. Chem. 390:319-323.
    • (2009) Biol. Chem. , vol.390 , pp. 319-323
    • Ellencrona, K.1    Syed, A.2    Johansson, M.3
  • 15
    • 33746257209 scopus 로고    scopus 로고
    • The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism
    • Engelman, J. A., J. Luo, and L. C. Cantley. 2006. The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism. Nat. Rev. Genet. 7:606-619.
    • (2006) Nat. Rev. Genet. , vol.7 , pp. 606-619
    • Engelman, J.A.1    Luo, J.2    Cantley, L.C.3
  • 16
    • 0347510642 scopus 로고    scopus 로고
    • The protein tyrosine phosphatase PTP-basophil/ basophil-like: interacting proteins and molecular functions
    • Erdmann, K. S. 2003. The protein tyrosine phosphatase PTP-basophil/ basophil-like: interacting proteins and molecular functions. Eur. J. Biochem. 270:4789-4798.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4789-4798
    • Erdmann, K.S.1
  • 17
    • 24944577909 scopus 로고    scopus 로고
    • Cdc42 and Par6-PKCzeta regulate the spatially localized association of Dlg1 and APC to control cell polarization
    • Etienne-Manneville, S., J. B. Manneville, S. Nicholls, M. A. Ferenczi, and A. Hall. 2005. Cdc42 and Par6-PKCzeta regulate the spatially localized association of Dlg1 and APC to control cell polarization. J. Cell Biol. 170:895-901.
    • (2005) J. Cell Biol. , vol.170 , pp. 895-901
    • Etienne-Manneville, S.1    Manneville, J.B.2    Nicholls, S.3    Ferenczi, M.A.4    Hall, A.5
  • 18
    • 78449234718 scopus 로고    scopus 로고
    • The SR-BI partner PDZK1 facilitates hepatitis C virus entry
    • Eyre, N. S., H. E. Drummer, and M. R. Beard. 2010. The SR-BI partner PDZK1 facilitates hepatitis C virus entry. PLoS Pathog. 6:e1001130.
    • (2010) PLoS Pathog , vol.6
    • Eyre, N.S.1    Drummer, H.E.2    Beard, M.R.3
  • 19
    • 67249084776 scopus 로고    scopus 로고
    • Zonula occludens-1 and -2 are cytosolic scaffolds that regulate the assembly of cellular junctions
    • Fanning, A. S., and J. M. Anderson. 2009. Zonula occludens-1 and -2 are cytosolic scaffolds that regulate the assembly of cellular junctions. Ann. N. Y. Acad. Sci. 1165:113-120.
    • (2009) Ann. N. Y. Acad. Sci. , vol.1165 , pp. 113-120
    • Fanning, A.S.1    Anderson, J.M.2
  • 20
    • 15244360247 scopus 로고    scopus 로고
    • Human papillomavirus type 18 E6 protein binds the cellular PDZ protein TIP-2/ GIPC, which is involved in transforming growth factor beta signaling and triggers its degradation by the proteasome
    • Favre-Bonvin, A., C. Reynaud, C. Kretz-Remy, and P. Jalinot. 2005. Human papillomavirus type 18 E6 protein binds the cellular PDZ protein TIP-2/ GIPC, which is involved in transforming growth factor beta signaling and triggers its degradation by the proteasome. J. Virol. 79:4229-4237.
    • (2005) J. Virol. , vol.79 , pp. 4229-4237
    • Favre-Bonvin, A.1    Reynaud, C.2    Kretz-Remy, C.3    Jalinot, P.4
  • 21
    • 33645310154 scopus 로고    scopus 로고
    • Oncogenic function for the Dlg1 mammalian homolog of the Drosophila discs-large tumor suppressor
    • Frese, K. K., et al. 2006. Oncogenic function for the Dlg1 mammalian homolog of the Drosophila discs-large tumor suppressor. EMBO J. 25: 1406-1417.
    • (2006) EMBO J , vol.25 , pp. 1406-1417
    • Frese, K.K.1
  • 22
    • 0037421970 scopus 로고    scopus 로고
    • Selective PDZ protein-dependent stimulation of phosphatidylinositol 3-kinase by the adenovirus E4-ORF1 oncoprotein
    • Frese, K. K., et al. 2003. Selective PDZ protein-dependent stimulation of phosphatidylinositol 3-kinase by the adenovirus E4-ORF1 oncoprotein. Oncogene 22:710-721.
    • (2003) Oncogene , vol.22 , pp. 710-721
    • Frese, K.K.1
  • 23
    • 78650033289 scopus 로고    scopus 로고
    • Molecular determinants of PDLIM2 in suppressing HTLV-I Tax-mediated tumorigenesis
    • Fu, J., P. Yan, S. Li, Z. Qu, and G. Xiao. 2010. Molecular determinants of PDLIM2 in suppressing HTLV-I Tax-mediated tumorigenesis. Oncogene 29:6499-6507.
    • (2010) Oncogene , vol.29 , pp. 6499-6507
    • Fu, J.1    Yan, P.2    Li, S.3    Qu, Z.4    Xiao, G.5
  • 24
    • 0033619139 scopus 로고    scopus 로고
    • Oncogenic human papillomavirus E6 proteins target the discs large tumour suppressor for proteasome-mediated degradation
    • Gardiol, D., et al. 1999. Oncogenic human papillomavirus E6 proteins target the discs large tumour suppressor for proteasome-mediated degradation. Oncogene 18:5487-5496.
    • (1999) Oncogene , vol.18 , pp. 5487-5496
    • Gardiol, D.1
  • 25
    • 0034597533 scopus 로고    scopus 로고
    • Interactions of the PDZ-protein MAGI-1 with adenovirus E4-ORF1 and high-risk papillomavirus E6 oncoproteins
    • Glaunsinger, B. A., S. S. Lee, M. Thomas, L. Banks, and R. Javier. 2000. Interactions of the PDZ-protein MAGI-1 with adenovirus E4-ORF1 and high-risk papillomavirus E6 oncoproteins. Oncogene 19:5270-5280.
    • (2000) Oncogene , vol.19 , pp. 5270-5280
    • Glaunsinger, B.A.1    Lee, S.S.2    Thomas, M.3    Banks, L.4    Javier, R.5
  • 26
    • 0035887255 scopus 로고    scopus 로고
    • Link of the unique oncogenic properties of adenovirus type 9 E4-ORF1 to a select interaction with the candidate tumor suppressor protein ZO-2
    • Glaunsinger, B. A., R. S. Weiss, S. S. Lee, and R. Javier. 2001. Link of the unique oncogenic properties of adenovirus type 9 E4-ORF1 to a select interaction with the candidate tumor suppressor protein ZO-2. EMBO J. 20:5578-5586.
    • (2001) EMBO J , vol.20 , pp. 5578-5586
    • Glaunsinger, B.A.1    Weiss, R.S.2    Lee, S.S.3    Javier, R.4
  • 27
    • 80054997526 scopus 로고    scopus 로고
    • The avian influenza virus NS1 ESEV PDZ binding motif associates with DlgI and Scribble to disrupt cellular tight junctions
    • Golebiewski, L., H. Liu, R. T. Javier, and A. P. Rice. 2011. The avian influenza virus NS1 ESEV PDZ binding motif associates with DlgI and Scribble to disrupt cellular tight junctions. J. Virol. 85:10639-10648.
    • (2011) J. Virol. , vol.85 , pp. 10639-10648
    • Golebiewski, L.1    Liu, H.2    Javier, R.T.3    Rice, A.P.4
  • 28
    • 54449099369 scopus 로고    scopus 로고
    • The multifunctional NS1 protein of influenza A viruses
    • Hale, B. G., R. E. Randall, J. Ortin, and D. Jackson. 2008. The multifunctional NS1 protein of influenza A viruses. J. Gen. Virol. 89:2359-2376.
    • (2008) J. Gen. Virol. , vol.89 , pp. 2359-2376
    • Hale, B.G.1    Randall, R.E.2    Ortin, J.3    Jackson, D.4
  • 29
    • 0037016668 scopus 로고    scopus 로고
    • Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions through its possible interaction with claudin-1 and junctional adhesion molecule
    • Hamazaki, Y., M. Itoh, H. Sasaki, M. Furuse, and S. Tsukita. 2002. Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions through its possible interaction with claudin-1 and junctional adhesion molecule. J. Biol. Chem. 277:455-461.
    • (2002) J. Biol. Chem. , vol.277 , pp. 455-461
    • Hamazaki, Y.1    Itoh, M.2    Sasaki, H.3    Furuse, M.4    Tsukita, S.5
  • 30
    • 16644367540 scopus 로고    scopus 로고
    • The PDZ protein Tip-1 is a gain of function target of the HPV16 E6 oncoprotein
    • Hampson, L., C. Li, A. W. Oliver, H. C. Kitchener, and I. N. Hampson. 2004. The PDZ protein Tip-1 is a gain of function target of the HPV16 E6 oncoprotein. Int. J. Oncol. 25:1249-1256.
    • (2004) Int. J. Oncol. , vol.25 , pp. 1249-1256
    • Hampson, L.1    Li, C.2    Oliver, A.W.3    Kitchener, H.C.4    Hampson, I.N.5
  • 31
    • 33846467609 scopus 로고    scopus 로고
    • E6AP-dependent degradation of DLG4/PSD95 by high-risk human papillomavirus type 18 E6 protein
    • Handa, K., et al. 2007. E6AP-dependent degradation of DLG4/PSD95 by high-risk human papillomavirus type 18 E6 protein. J. Virol. 81:1379-1389.
    • (2007) J. Virol. , vol.81 , pp. 1379-1389
    • Handa, K.1
  • 32
    • 77956636731 scopus 로고    scopus 로고
    • PDZD8 is a novel Gag-interacting factor that promotes retroviral infection
    • Henning, M. S., S. G. Morham, S. P. Goff, and M. H. Naghavi. 2010. PDZD8 is a novel Gag-interacting factor that promotes retroviral infection. J. Virol. 84:8990-8995.
    • (2010) J. Virol. , vol.84 , pp. 8990-8995
    • Henning, M.S.1    Morham, S.G.2    Goff, S.P.3    Naghavi, M.H.4
  • 33
    • 79957785375 scopus 로고    scopus 로고
    • PDZD8 is a novel moesin-interacting cytoskeletal regulatory protein that suppresses infection by herpes simplex virus type 1
    • Henning, M. S., et al. 2011. PDZD8 is a novel moesin-interacting cytoskeletal regulatory protein that suppresses infection by herpes simplex virus type 1. Virology 415:114-121.
    • (2011) Virology , vol.415 , pp. 114-121
    • Henning, M.S.1
  • 34
    • 34247092058 scopus 로고    scopus 로고
    • ZO- 2 silencing in epithelial cells perturbs the gate and fence function of tight junctions and leads to an atypical monolayer architecture
    • Hernandez, S., B. Chavez Munguia, and L. Gonzalez-Mariscal. 2007. ZO-2 silencing in epithelial cells perturbs the gate and fence function of tight junctions and leads to an atypical monolayer architecture. Exp. Cell Res. 313:1533-1547.
    • (2007) Exp. Cell Res. , vol.313 , pp. 1533-1547
    • Hernandez, S.1    Chavez Munguia, B.2    Gonzalez-Mariscal, L.3
  • 35
    • 35448938507 scopus 로고    scopus 로고
    • Cooperation of NF-kappaB2/p100 activation and the PDZ domain binding motif signal in human T-cell leukemia virus type 1 (HTLV-1) Tax1 but not HTLV-2 Tax2 is crucial for interleukin-2-independent growth transformation of a T-cell line
    • Higuchi, M., et al. 2007. Cooperation of NF-kappaB2/p100 activation and the PDZ domain binding motif signal in human T-cell leukemia virus type 1 (HTLV-1) Tax1 but not HTLV-2 Tax2 is crucial for interleukin-2-independent growth transformation of a T-cell line. J. Virol. 81:11900-11907.
    • (2007) J. Virol. , vol.81 , pp. 11900-11907
    • Higuchi, M.1
  • 36
    • 10744225827 scopus 로고    scopus 로고
    • PDZ domain-binding motif of human T-cell leukemia virus type 1 Tax oncoprotein augments the transforming activity in a rat fibroblast cell line
    • Hirata, A., et al. 2004. PDZ domain-binding motif of human T-cell leukemia virus type 1 Tax oncoprotein augments the transforming activity in a rat fibroblast cell line. Virology 318:327-336.
    • (2004) Virology , vol.318 , pp. 327-336
    • Hirata, A.1
  • 37
    • 33751347857 scopus 로고    scopus 로고
    • The Scribble and Par complexes in polarity and migration: friends or foes?
    • Humbert, P. O., L. E. Dow, and S. M. Russell. 2006. The Scribble and Par complexes in polarity and migration: friends or foes? Trends Cell Biol. 16:622-630.
    • (2006) Trends Cell Biol , vol.16 , pp. 622-630
    • Humbert, P.O.1    Dow, L.E.2    Russell, S.M.3
  • 38
    • 0037155199 scopus 로고    scopus 로고
    • PDZ domains: structural modules for protein complex assembly
    • Hung, A. Y., and M. Sheng. 2002. PDZ domains: structural modules for protein complex assembly. J. Biol. Chem. 277:5699-5702.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5699-5702
    • Hung, A.Y.1    Sheng, M.2
  • 39
    • 0242515763 scopus 로고    scopus 로고
    • Spread of HTLV-I between lymphocytes by virusinduced polarization of the cytoskeleton
    • Igakura, T., et al. 2003. Spread of HTLV-I between lymphocytes by virusinduced polarization of the cytoskeleton. Science 299:1713-1716.
    • (2003) Science , vol.299 , pp. 1713-1716
    • Igakura, T.1
  • 40
    • 77953795571 scopus 로고    scopus 로고
    • Opposing effects of a tyrosine-based sorting motif and a PDZ-binding motif regulate human T-lymphotropic virus type 1 envelope trafficking
    • Ilinskaya, A., G. Heidecker, and D. Derse. 2010. Opposing effects of a tyrosine-based sorting motif and a PDZ-binding motif regulate human T-lymphotropic virus type 1 envelope trafficking. J. Virol. 84:6995-7004.
    • (2010) J. Virol. , vol.84 , pp. 6995-7004
    • Ilinskaya, A.1    Heidecker, G.2    Derse, D.3
  • 41
    • 0034688150 scopus 로고    scopus 로고
    • The APC-hDLG complex negatively regulates cell cycle progression from the G0/G1 to S phase
    • Ishidate, T., A. Matsumine, K. Toyoshima, and T. Akiyama. 2000. The APC-hDLG complex negatively regulates cell cycle progression from the G0/G1 to S phase. Oncogene 19:365-372.
    • (2000) Oncogene , vol.19 , pp. 365-372
    • Ishidate, T.1    Matsumine, A.2    Toyoshima, K.3    Akiyama, T.4
  • 42
    • 33750396874 scopus 로고    scopus 로고
    • Inactivation of tumor suppressor Dlg1 augments transformation of a T-cell line induced by human T-cell leukemia virus type 1 Tax protein
    • Ishioka, K., et al. 2006. Inactivation of tumor suppressor Dlg1 augments transformation of a T-cell line induced by human T-cell leukemia virus type 1 Tax protein. Retrovirology 3:71.
    • (2006) Retrovirology , vol.3 , pp. 71
    • Ishioka, K.1
  • 43
    • 41949123710 scopus 로고    scopus 로고
    • A new influenza virus virulence determinant: the NS1 protein four C-terminal residues modulate pathogenicity
    • Jackson, D., M. J. Hossain, D. Hickman, D. R. Perez, and R. A. Lamb. 2008. A new influenza virus virulence determinant: the NS1 protein four C-terminal residues modulate pathogenicity. Proc. Natl. Acad. Sci. U. S. A. 105:4381-4386.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 4381-4386
    • Jackson, D.1    Hossain, M.J.2    Hickman, D.3    Perez, D.R.4    Lamb, R.A.5
  • 44
    • 33646727381 scopus 로고    scopus 로고
    • Human papillomavirus type 16 E6 activates NF-kappaB, induces cIAP-2 expression, and protects against apoptosis in a PDZ binding motif-dependent manner
    • James, M. A., J. H. Lee, and A. J. Klingelhutz. 2006. Human papillomavirus type 16 E6 activates NF-kappaB, induces cIAP-2 expression, and protects against apoptosis in a PDZ binding motif-dependent manner. J. Virol. 80:5301-5307.
    • (2006) J. Virol. , vol.80 , pp. 5301-5307
    • James, M.A.1    Lee, J.H.2    Klingelhutz, A.J.3
  • 45
    • 56749150051 scopus 로고    scopus 로고
    • Cell polarity proteins: common targets for tumorigenic human viruses
    • Javier, R. T. 2008. Cell polarity proteins: common targets for tumorigenic human viruses. Oncogene 27:7031-7046.
    • (2008) Oncogene , vol.27 , pp. 7031-7046
    • Javier, R.T.1
  • 46
    • 34547643210 scopus 로고    scopus 로고
    • PDZ domains: folding and binding
    • Jemth, P., and S. Gianni. 2007. PDZ domains: folding and binding. Biochemistry 46:8701-8708.
    • (2007) Biochemistry , vol.46 , pp. 8701-8708
    • Jemth, P.1    Gianni, S.2
  • 47
    • 33846495746 scopus 로고    scopus 로고
    • Human papillomavirus type 16 E6 protein interacts with cystic fibrosis transmembrane regulator-associated ligand and promotes E6-associated protein-mediated ubiquitination and proteasomal degradation
    • Jeong, K. W., H. Z. Kim, S. Kim, Y. S. Kim, and J. Choe. 2007. Human papillomavirus type 16 E6 protein interacts with cystic fibrosis transmembrane regulator-associated ligand and promotes E6-associated protein-mediated ubiquitination and proteasomal degradation. Oncogene 26:487-499.
    • (2007) Oncogene , vol.26 , pp. 487-499
    • Jeong, K.W.1    Kim, H.Z.2    Kim, S.3    Kim, Y.S.4    Choe, J.5
  • 48
    • 0028287035 scopus 로고
    • Molecular characterization and tissue distribution of ZO-2, a tight junction protein homologous to ZO-1 and the Drosophila discs-large tumor suppressor protein
    • Jesaitis, L. A., and D. A. Goodenough. 1994. Molecular characterization and tissue distribution of ZO-2, a tight junction protein homologous to ZO-1 and the Drosophila discs-large tumor suppressor protein. J. Cell Biol. 124:949-961.
    • (1994) J. Cell Biol. , vol.124 , pp. 949-961
    • Jesaitis, L.A.1    Goodenough, D.A.2
  • 49
    • 33847190660 scopus 로고    scopus 로고
    • Degradation of tyrosine phosphatase PTPN3 (PTPH1) by association with oncogenic human papillomavirus E6 proteins
    • Jing, M., J. Bohl, N. Brimer, M. Kinter, and S. B. Vande Pol. 2007. Degradation of tyrosine phosphatase PTPN3 (PTPH1) by association with oncogenic human papillomavirus E6 proteins. J. Virol. 81:2231-2239.
    • (2007) J. Virol. , vol.81 , pp. 2231-2239
    • Jing, M.1    Bohl, J.2    Brimer, N.3    Kinter, M.4    Vande Pol, S.B.5
  • 50
    • 0141643206 scopus 로고    scopus 로고
    • The PDZ protein tax-interacting protein-1 inhibits beta-catenin transcriptional activity and growth of colorectal cancer cells
    • Kanamori, M., et al. 2003. The PDZ protein tax-interacting protein-1 inhibits beta-catenin transcriptional activity and growth of colorectal cancer cells. J. Biol. Chem. 278:38758-38764.
    • (2003) J. Biol. Chem. , vol.278 , pp. 38758-38764
    • Kanamori, M.1
  • 51
    • 0030774987 scopus 로고    scopus 로고
    • Binding of high-risk human papillomavirus E6 oncoproteins to the human homologue of the Drosophila discs large tumor suppressor protein
    • Kiyono, T., et al. 1997. Binding of high-risk human papillomavirus E6 oncoproteins to the human homologue of the Drosophila discs large tumor suppressor protein. Proc. Natl. Acad. Sci. U. S. A. 94:11612-11616.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 11612-11616
    • Kiyono, T.1
  • 52
    • 78951488641 scopus 로고    scopus 로고
    • A systematic analysis of human papillomavirus (HPV) E6 PDZ substrates identifies MAGI-1 as a major target of HPV type 16 (HPV-16) and HPV-18 whose loss accompanies disruption of tight junctions
    • Kranjec, C., and L. Banks. 2011. A systematic analysis of human papillomavirus (HPV) E6 PDZ substrates identifies MAGI-1 as a major target of HPV type 16 (HPV-16) and HPV-18 whose loss accompanies disruption of tight junctions. J. Virol. 85:1757-1764.
    • (2011) J. Virol. , vol.85 , pp. 1757-1764
    • Kranjec, C.1    Banks, L.2
  • 53
    • 0037565268 scopus 로고    scopus 로고
    • Intracellular warfare between human influenza viruses and human cells: the roles of the viral NS1 protein
    • Krug, R. M., W. Yuan, D. L. Noah, and A. G. Latham. 2003. Intracellular warfare between human influenza viruses and human cells: the roles of the viral NS1 protein. Virology 309:181-189.
    • (2003) Virology , vol.309 , pp. 181-189
    • Krug, R.M.1    Yuan, W.2    Noah, D.L.3    Latham, A.G.4
  • 54
    • 33750117119 scopus 로고    scopus 로고
    • Maintenance and modulation of T cell polarity
    • Krummel, M. F., and I. Macara. 2006. Maintenance and modulation of T cell polarity. Nat. Immunol. 7:1143-1149.
    • (2006) Nat. Immunol. , vol.7 , pp. 1143-1149
    • Krummel, M.F.1    Macara, I.2
  • 55
    • 57349135723 scopus 로고    scopus 로고
    • Hypertonic stress increases claudin-4 expression and tight junction integrity in association with MUPP1 in IMCD3 cells
    • Lanaspa, M. A., A. Andres-Hernando, C. J. Rivard, Y. Dai, and T. Berl. 2008. Hypertonic stress increases claudin-4 expression and tight junction integrity in association with MUPP1 in IMCD3 cells. Proc. Natl. Acad. Sci. U. S. A. 105:15797-15802.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 15797-15802
    • Lanaspa, M.A.1    Andres-Hernando, A.2    Rivard, C.J.3    Dai, Y.4    Berl, T.5
  • 56
    • 1642342675 scopus 로고    scopus 로고
    • Human homolog of disc-large is required for adherens junction assembly and differentiation of human intestinal epithelial cells
    • Laprise, P., A. Viel, and N. Rivard. 2004. Human homolog of disc-large is required for adherens junction assembly and differentiation of human intestinal epithelial cells. J. Biol. Chem. 279:10157-10166.
    • (2004) J. Biol. Chem. , vol.279 , pp. 10157-10166
    • Laprise, P.1    Viel, A.2    Rivard, N.3
  • 57
    • 27144466422 scopus 로고    scopus 로고
    • Viral oncoprotein-induced mislocalization of select PDZ proteins disrupts tight junctions and causes polarity defects in epithelial cells
    • Latorre, I. J., et al. 2005. Viral oncoprotein-induced mislocalization of select PDZ proteins disrupts tight junctions and causes polarity defects in epithelial cells. J. Cell Sci. 118:4283-4293.
    • (2005) J. Cell Sci. , vol.118 , pp. 4283-4293
    • Latorre, I.J.1
  • 58
    • 7644226723 scopus 로고    scopus 로고
    • Role of the PDZ domain-binding motif of the oncoprotein E6 in the pathogenesis of human papillomavirus type 31
    • Lee, C., and L. A. Laimins. 2004. Role of the PDZ domain-binding motif of the oncoprotein E6 in the pathogenesis of human papillomavirus type 31. J. Virol. 78:12366-12377.
    • (2004) J. Virol. , vol.78 , pp. 12366-12377
    • Lee, C.1    Laimins, L.A.2
  • 59
    • 77952705907 scopus 로고    scopus 로고
    • PDZ domains and their binding partners: structure, specificity, and modification
    • Lee, H. J., and J. J. Zheng. 2010. PDZ domains and their binding partners: structure, specificity, and modification. Cell Commun. Signal. 8:8.
    • (2010) Cell Commun. Signal. , vol.8 , pp. 8
    • Lee, H.J.1    Zheng, J.J.2
  • 60
    • 0033815457 scopus 로고    scopus 로고
    • Multi-PDZ domain protein MUPP1 is a cellular target for both adenovirus E4-ORF1 and high-risk papillomavirus type 18 E6 oncoproteins
    • Lee, S. S., B. Glaunsinger, F. Mantovani, L. Banks, and R. T. Javier. 2000. Multi-PDZ domain protein MUPP1 is a cellular target for both adenovirus E4-ORF1 and high-risk papillomavirus type 18 E6 oncoproteins. J. Virol. 74:9680-9693.
    • (2000) J. Virol. , vol.74 , pp. 9680-9693
    • Lee, S.S.1    Glaunsinger, B.2    Mantovani, F.3    Banks, L.4    Javier, R.T.5
  • 61
    • 0030950410 scopus 로고    scopus 로고
    • Binding of human virus oncoproteins to hDlg/SAP97, a mammalian homolog of the Drosophila discs large tumor suppressor protein
    • Lee, S. S., R. S. Weiss, and R. T. Javier. 1997. Binding of human virus oncoproteins to hDlg/SAP97, a mammalian homolog of the Drosophila discs large tumor suppressor protein. Proc. Natl. Acad. Sci. U. S. A. 94: 6670-6675.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 6670-6675
    • Lee, S.S.1    Weiss, R.S.2    Javier, R.T.3
  • 62
    • 57749178160 scopus 로고    scopus 로고
    • Interaction of the human somatostatin receptor 3 with the multiple PDZ domain protein MUPP1 enables somatostatin to control permeability of epithelial tight junctions
    • Liew, C. W., et al. 2009. Interaction of the human somatostatin receptor 3 with the multiple PDZ domain protein MUPP1 enables somatostatin to control permeability of epithelial tight junctions. FEBS Lett. 583:49-54.
    • (2009) FEBS Lett , vol.583 , pp. 49-54
    • Liew, C.W.1
  • 63
    • 77957970275 scopus 로고    scopus 로고
    • The ESEV PDZ-binding motif of the avian influenza A virus NS1 protein protects infected cells from apoptosis by directly targeting Scribble
    • Liu, H., et al. 2010. The ESEV PDZ-binding motif of the avian influenza A virus NS1 protein protects infected cells from apoptosis by directly targeting Scribble. J. Virol. 84:11164-11174.
    • (2010) J. Virol. , vol.84 , pp. 11164-11174
    • Liu, H.1
  • 64
    • 20444445916 scopus 로고    scopus 로고
    • A network of PDZ-containing proteins regulates T cell polarity and morphology during migration and immunological synapse formation
    • Ludford-Menting, M. J., et al. 2005. A network of PDZ-containing proteins regulates T cell polarity and morphology during migration and immunological synapse formation. Immunity 22:737-748.
    • (2005) Immunity , vol.22 , pp. 737-748
    • Ludford-Menting, M.J.1
  • 65
    • 78049499222 scopus 로고    scopus 로고
    • Dlg1 binds GKAP to control dynein association with microtubules, centrosome positioning, and cell polarity
    • Manneville, J. B., M. Jehanno, and S. Etienne-Manneville. 2010. Dlg1 binds GKAP to control dynein association with microtubules, centrosome positioning, and cell polarity. J. Cell Biol. 191:585-598.
    • (2010) J. Cell Biol. , vol.191 , pp. 585-598
    • Manneville, J.B.1    Jehanno, M.2    Etienne-Manneville, S.3
  • 66
    • 69449087112 scopus 로고    scopus 로고
    • Tick-borne encephalitis virus: a review of an emerging zoonosis
    • Mansfield, K. L., et al. 2009. Tick-borne encephalitis virus: a review of an emerging zoonosis. J. Gen. Virol. 90:1781-1794.
    • (2009) J. Gen. Virol. , vol.90 , pp. 1781-1794
    • Mansfield, K.L.1
  • 67
    • 7944234859 scopus 로고    scopus 로고
    • HPV E6 specifically targets different cellular pools of its PDZ domain-containing tumour suppressor substrates for proteasome-mediated degradation
    • Massimi, P., N. Gammoh, M. Thomas, and L. Banks. 2004. HPV E6 specifically targets different cellular pools of its PDZ domain-containing tumour suppressor substrates for proteasome-mediated degradation. Oncogene 23:8033-8039.
    • (2004) Oncogene , vol.23 , pp. 8033-8039
    • Massimi, P.1    Gammoh, N.2    Thomas, M.3    Banks, L.4
  • 68
    • 33746257302 scopus 로고    scopus 로고
    • Phosphorylation of the discs large tumour suppressor protein controls its membrane localisation and enhances its susceptibility to HPV E6-induced degradation
    • Massimi, P., N. Narayan, A. Cuenda, and L. Banks. 2006. Phosphorylation of the discs large tumour suppressor protein controls its membrane localisation and enhances its susceptibility to HPV E6-induced degradation. Oncogene 25:4276-4285.
    • (2006) Oncogene , vol.25 , pp. 4276-4285
    • Massimi, P.1    Narayan, N.2    Cuenda, A.3    Banks, L.4
  • 69
    • 9344271549 scopus 로고    scopus 로고
    • Binding of APC to the human homolog of the Drosophila discs large tumor suppressor protein
    • Matsumine, A., A. Ogai, T. Senda, N. Okumura, K. Satoh, et al. 1996. Binding of APC to the human homolog of the Drosophila discs large tumor suppressor protein. Science 272:1020-1023.
    • (1996) Science , vol.272 , pp. 1020-1023
    • Matsumine, A.1    Ogai, A.2    Senda, T.3    Okumura, N.4    Satoh, K.5
  • 70
    • 70349906831 scopus 로고    scopus 로고
    • Planar cell polarity and the kidney
    • McNeill, H. 2009. Planar cell polarity and the kidney. J. Am. Soc. Nephrol. 20:2104-2111.
    • (2009) J. Am. Soc. Nephrol. , vol.20 , pp. 2104-2111
    • McNeill, H.1
  • 71
    • 26244441572 scopus 로고    scopus 로고
    • PATJ connects and stabilizes apical and lateral components of tight junctions in human intestinal cells
    • Michel, D., et al. 2005. PATJ connects and stabilizes apical and lateral components of tight junctions in human intestinal cells. J. Cell Sci. 118: 4049-4057.
    • (2005) J. Cell Sci. , vol.118 , pp. 4049-4057
    • Michel, D.1
  • 72
    • 77956175013 scopus 로고    scopus 로고
    • NFAT, immunity and cancer: a transcription factor comes of age
    • Müller, M. R., and A. Rao. 2010. NFAT, immunity and cancer: a transcription factor comes of age. Nat. Rev. Immunol. 10:645-656.
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 645-656
    • Müller, M.R.1    Rao, A.2
  • 73
    • 0033776810 scopus 로고    scopus 로고
    • Human scribble (Vartul) is targeted for ubiquitin-mediated degradation by the high-risk papillomavirus E6 proteins and the E6AP ubiquitin-protein ligase
    • Nakagawa, S., and J. M. Huibregtse. 2000. Human scribble (Vartul) is targeted for ubiquitin-mediated degradation by the high-risk papillomavirus E6 proteins and the E6AP ubiquitin-protein ligase. Mol. Cell. Biol. 20:8244-8253.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8244-8253
    • Nakagawa, S.1    Huibregtse, J.M.2
  • 74
    • 0842329915 scopus 로고    scopus 로고
    • Analysis of the expression and localisation of a LAP protein, human scribble, in the normal and neoplastic epithelium of uterine cervix
    • Nakagawa, S., et al. 2004. Analysis of the expression and localisation of a LAP protein, human scribble, in the normal and neoplastic epithelium of uterine cervix. Br. J. Cancer 90:194-199.
    • (2004) Br. J. Cancer , vol.90 , pp. 194-199
    • Nakagawa, S.1
  • 75
    • 77951238830 scopus 로고    scopus 로고
    • Remodeling epithelial cell organization: transitions between front-rear and apical-basal polarity
    • Nelson, W. J. 2009. Remodeling epithelial cell organization: transitions between front-rear and apical-basal polarity. Cold Spring Harb. Perspect. Biol. 1:a000513.
    • (2009) Cold Spring Harb. Perspect. Biol. , vol.1
    • Nelson, W.J.1
  • 76
    • 0038618733 scopus 로고    scopus 로고
    • The PDZ ligand domain of the human papillomavirus type 16 E6 protein is required for E6's induction of epithelial hyperplasia in vivo
    • Nguyen, M. L., M. M. Nguyen, D. Lee, A. E. Griep, and P. F. Lambert. 2003. The PDZ ligand domain of the human papillomavirus type 16 E6 protein is required for E6's induction of epithelial hyperplasia in vivo. J. Virol. 77: 6957-6964.
    • (2003) J. Virol. , vol.77 , pp. 6957-6964
    • Nguyen, M.L.1    Nguyen, M.M.2    Lee, D.3    Griep, A.E.4    Lambert, P.F.5
  • 77
    • 0344629666 scopus 로고    scopus 로고
    • Requirement of PDZ-containing proteins for cell cycle regulation and differentiation in the mouse lens epithelium
    • Nguyen, M. M., et al. 2003. Requirement of PDZ-containing proteins for cell cycle regulation and differentiation in the mouse lens epithelium. Mol. Cell. Biol. 23:8970-8981.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8970-8981
    • Nguyen, M.M.1
  • 78
    • 0012927828 scopus 로고    scopus 로고
    • PDZ domain proteins: plug and play!
    • Nourry, C., S. G. Grant, and J. P. Borg. 2003. PDZ domain proteins: plug and play! Sci. STKE 2003:RE7.
    • (2003) Sci. STKE , vol.2003
    • Nourry, C.1    Grant, S.G.2    Borg, J.P.3
  • 79
    • 33645067624 scopus 로고    scopus 로고
    • Large-scale sequence analysis of avian influenza isolates
    • Obenauer, J. C., et al. 2006. Large-scale sequence analysis of avian influenza isolates. Science 311:1576-1580.
    • (2006) Science , vol.311 , pp. 1576-1580
    • Obenauer, J.C.1
  • 80
    • 10744227205 scopus 로고    scopus 로고
    • Human T-cell leukemia virus type 1 Tax oncoprotein induces and interacts with a multi-PDZ domain protein, MAGI-3
    • Ohashi, M., et al. 2004. Human T-cell leukemia virus type 1 Tax oncoprotein induces and interacts with a multi-PDZ domain protein, MAGI-3. Virology 320:52-62.
    • (2004) Virology , vol.320 , pp. 52-62
    • Ohashi, M.1
  • 81
    • 78751575654 scopus 로고    scopus 로고
    • The HPV16 E6 binding protein Tip-1 interacts with ARHGEF16, which activates Cdc42
    • Oliver, A. W., et al. 2011. The HPV16 E6 binding protein Tip-1 interacts with ARHGEF16, which activates Cdc42. Br. J. Cancer 104:324-331.
    • (2011) Br. J. Cancer , vol.104 , pp. 324-331
    • Oliver, A.W.1
  • 82
    • 17144403770 scopus 로고    scopus 로고
    • Adenoviral proteins mimic nutrient/growth signals to activate the mTOR pathway for viral replication
    • O'Shea, C., et al. 2005. Adenoviral proteins mimic nutrient/growth signals to activate the mTOR pathway for viral replication. EMBO J. 24:1211- 1221.
    • (2005) EMBO J , vol.24 , pp. 1211-1221
    • O'Shea, C.1
  • 83
    • 33845472291 scopus 로고    scopus 로고
    • Scrib controls Cdc42 localization and activity to promote cell polarization during astrocyte migration
    • Osmani, N., N. Vitale, J. P. Borg, and S. Etienne-Manneville. 2006. Scrib controls Cdc42 localization and activity to promote cell polarization during astrocyte migration. Curr. Biol. 16:2395-2405.
    • (2006) Curr. Biol. , vol.16 , pp. 2395-2405
    • Osmani, N.1    Vitale, N.2    Borg, J.P.3    Etienne-Manneville, S.4
  • 84
    • 0037119361 scopus 로고    scopus 로고
    • Interaction of two actin-binding proteins, synaptopodin and alphaactinin-4, with the tight junction protein MAGI-1
    • Patrie, K. M., A. J. Drescher, A. Welihinda, P. Mundel, and B. Margolis. 2002. Interaction of two actin-binding proteins, synaptopodin and alphaactinin-4, with the tight junction protein MAGI-1. J. Biol. Chem. 277: 30183-30190.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30183-30190
    • Patrie, K.M.1    Drescher, A.J.2    Welihinda, A.3    Mundel, P.4    Margolis, B.5
  • 85
    • 63049134547 scopus 로고    scopus 로고
    • Human Discs Large is a new negative regulator of human immunodeficiency virus-1 infectivity
    • Perugi, F., et al. 2009. Human Discs Large is a new negative regulator of human immunodeficiency virus-1 infectivity. Mol. Biol. Cell 20:498-508.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 498-508
    • Perugi, F.1
  • 86
    • 79954546158 scopus 로고    scopus 로고
    • Protein complexes that control renal epithelial polarity
    • Pieczynski, J., and B. Margolis. 2011. Protein complexes that control renal epithelial polarity. Am. J. Physiol. Renal Physiol. 300:F589-F601.
    • (2011) Am. J. Physiol. Renal Physiol. , vol.300
    • Pieczynski, J.1    Margolis, B.2
  • 87
    • 70349269128 scopus 로고    scopus 로고
    • The human papillomavirus (HPV) E6* proteins from high-risk, mucosal HPVs can direct degradation of cellular proteins in the absence of full-length E6 protein
    • Pim, D., V. Tomaic, and L. Banks. 2009. The human papillomavirus (HPV) E6* proteins from high-risk, mucosal HPVs can direct degradation of cellular proteins in the absence of full-length E6 protein. J. Virol. 83:9863- 9874.
    • (2009) J. Virol. , vol.83 , pp. 9863-9874
    • Pim, D.1    Tomaic, V.2    Banks, L.3
  • 88
    • 77952302814 scopus 로고    scopus 로고
    • Attenuation of rabies virulence: takeover by the cytoplasmic domain of its envelope protein
    • Préhaud, C., et al. 2010. Attenuation of rabies virulence: takeover by the cytoplasmic domain of its envelope protein. Sci. Signal. 3:ra5.
    • (2010) Sci. Signal. , vol.3
    • Préhaud, C.1
  • 89
    • 76149102896 scopus 로고    scopus 로고
    • Interaction of hepatitis B virus core protein with human GIPC1
    • Razanskas, R., and K. Sasnauskas. 2010. Interaction of hepatitis B virus core protein with human GIPC1. Arch. Virol. 155:247-250.
    • (2010) Arch. Virol. , vol.155 , pp. 247-250
    • Razanskas, R.1    Sasnauskas, K.2
  • 90
    • 34247495936 scopus 로고    scopus 로고
    • Dlgh1 and Carma1 MAGUK proteins contribute to signal specificity downstream of TCR activation
    • Rebeaud, F., S. Hailfinger, and M. Thome. 2007. Dlgh1 and Carma1 MAGUK proteins contribute to signal specificity downstream of TCR activation. Trends Immunol. 28:196-200.
    • (2007) Trends Immunol , vol.28 , pp. 196-200
    • Rebeaud, F.1    Hailfinger, S.2    Thome, M.3
  • 91
    • 0034721765 scopus 로고    scopus 로고
    • The PDZ protein TIP-1 interacts with the Rho effector rhotekin and is involved in Rho signaling to the serum response element
    • Reynaud, C., S. Fabre, and P. Jalinot. 2000. The PDZ protein TIP-1 interacts with the Rho effector rhotekin and is involved in Rho signaling to the serum response element. J. Biol. Chem. 275:33962-33968.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33962-33968
    • Reynaud, C.1    Fabre, S.2    Jalinot, P.3
  • 92
    • 33846481303 scopus 로고    scopus 로고
    • Choreography of MAGUKs during T cell activation
    • Rincón, M., and R. J. Davis. 2007. Choreography of MAGUKs during T cell activation. Nat. Immunol. 8:126-127.
    • (2007) Nat. Immunol. , vol.8 , pp. 126-127
    • Rincón, M.1    Davis, R.J.2
  • 93
    • 40949092762 scopus 로고    scopus 로고
    • Human adenovirus Ad-36 induces adipogenesis via its E4 orf-1 gene
    • Rogers, P. M., et al. 2008. Human adenovirus Ad-36 induces adipogenesis via its E4 orf-1 gene. Int. J. Obes. 32:397-406.
    • (2008) Int. J. Obes. , vol.32 , pp. 397-406
    • Rogers, P.M.1
  • 94
    • 33846514807 scopus 로고    scopus 로고
    • Scaffold protein Dlgh1 coordinates alternative p38 kinase activation, directing T cell receptor signals toward NFAT but not NF-kappaB transcription factors
    • Round, J. L., et al. 2007. Scaffold protein Dlgh1 coordinates alternative p38 kinase activation, directing T cell receptor signals toward NFAT but not NF-kappaB transcription factors. Nat. Immunol. 8:154-161.
    • (2007) Nat. Immunol. , vol.8 , pp. 154-161
    • Round, J.L.1
  • 95
    • 13644268540 scopus 로고    scopus 로고
    • Dlgh1 coordinates actin polymerization, synaptic T cell receptor and lipid raft aggregation, and effector function in T cells
    • Round, J. L., et al. 2005. Dlgh1 coordinates actin polymerization, synaptic T cell receptor and lipid raft aggregation, and effector function in T cells. J. Exp. Med. 201:419-430.
    • (2005) J. Exp. Med. , vol.201 , pp. 419-430
    • Round, J.L.1
  • 96
    • 0032485028 scopus 로고    scopus 로고
    • The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction with the PDZ domain of cellular proteins
    • Rousset, R., S. Fabre, C. Desbois, F. Bantignies, and P. Jalinot. 1998. The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction with the PDZ domain of cellular proteins. Oncogene 16:643-654.
    • (1998) Oncogene , vol.16 , pp. 643-654
    • Rousset, R.1    Fabre, S.2    Desbois, C.3    Bantignies, F.4    Jalinot, P.5
  • 97
    • 33847743738 scopus 로고    scopus 로고
    • The human papillomavirus E6 oncogene dysregulates the cell cycle and contributes to cervical carcinogenesis through two independent activities
    • Shai, A., T. Brake, C. Somoza, and P. F. Lambert. 2007. The human papillomavirus E6 oncogene dysregulates the cell cycle and contributes to cervical carcinogenesis through two independent activities. Cancer Res. 67:1626-1635.
    • (2007) Cancer Res , vol.67 , pp. 1626-1635
    • Shai, A.1    Brake, T.2    Somoza, C.3    Lambert, P.F.4
  • 98
    • 42349097865 scopus 로고    scopus 로고
    • p53 loss synergizes with estrogen and papillomaviral oncogenes to induce cervical and breast cancers
    • Shai, A., H. C. Pitot, and P. F. Lambert. 2008. p53 loss synergizes with estrogen and papillomaviral oncogenes to induce cervical and breast cancers. Cancer Res. 68:2622-2631.
    • (2008) Cancer Res , vol.68 , pp. 2622-2631
    • Shai, A.1    Pitot, H.C.2    Lambert, P.F.3
  • 99
    • 14744275517 scopus 로고    scopus 로고
    • PATJ regulates tight junction formation and polarity in mammalian epithelial cells
    • Shin, K., S. Straight, and B. Margolis. 2005. PATJ regulates tight junction formation and polarity in mammalian epithelial cells. J. Cell Biol. 168:705- 711.
    • (2005) J. Cell Biol. , vol.168 , pp. 705-711
    • Shin, K.1    Straight, S.2    Margolis, B.3
  • 100
    • 33947268014 scopus 로고    scopus 로고
    • PATJ regulates directional migration of mammalian epithelial cells
    • Shin, K., Q. Wang, and B. Margolis. 2007. PATJ regulates directional migration of mammalian epithelial cells. EMBO Rep. 8:158-164.
    • (2007) EMBO Rep , vol.8 , pp. 158-164
    • Shin, K.1    Wang, Q.2    Margolis, B.3
  • 101
    • 33947142869 scopus 로고    scopus 로고
    • Microtubule-induced cortical cell polarity
    • Siegrist, S. E., and C. Q. Doe. 2007. Microtubule-induced cortical cell polarity. Genes Dev. 21:483-496.
    • (2007) Genes Dev , vol.21 , pp. 483-496
    • Siegrist, S.E.1    Doe, C.Q.2
  • 102
    • 0032820577 scopus 로고    scopus 로고
    • Increased tight junctional permeability is associated with the development of colon cancer
    • Soler, A. P., et al. 1999. Increased tight junctional permeability is associated with the development of colon cancer. Carcinogenesis. 20:1425-1431.
    • (1999) Carcinogenesis , vol.20 , pp. 1425-1431
    • Soler, A.P.1
  • 103
    • 69449095413 scopus 로고    scopus 로고
    • Tax1 enhances cancer cell proliferation via Ras-Raf-MEK-ERK signaling pathway
    • Song, C., W. Wang, M. Li, Y. Liu, and D. Zheng. 2009. Tax1 enhances cancer cell proliferation via Ras-Raf-MEK-ERK signaling pathway. IUBMB Life 61:685-692.
    • (2009) IUBMB Life , vol.61 , pp. 685-692
    • Song, C.1    Wang, W.2    Li, M.3    Liu, Y.4    Zheng, D.5
  • 104
    • 77953303859 scopus 로고    scopus 로고
    • Species-specific contribution of the four C-terminal amino acids of influenza A virus NS1 protein to virulence
    • Soubies, S. M., et al. 2010. Species-specific contribution of the four C-terminal amino acids of influenza A virus NS1 protein to virulence. J. Virol. 84:6733-6747.
    • (2010) J. Virol. , vol.84 , pp. 6733-6747
    • Soubies, S.M.1
  • 105
    • 39049128059 scopus 로고    scopus 로고
    • Act globally, think locally: systems biology addresses the PDZ domain
    • Spaller, M. R. 2006. Act globally, think locally: systems biology addresses the PDZ domain. ACS Chem. Biol. 1:207-210.
    • (2006) ACS Chem. Biol. , vol.1 , pp. 207-210
    • Spaller, M.R.1
  • 106
    • 39149088346 scopus 로고    scopus 로고
    • Deletion of the PDZ motif of HPV16 E6 preventing immortalization and anchorage-independent growth in human tonsil epithelial cells
    • Spanos, W. C., et al. 2008. Deletion of the PDZ motif of HPV16 E6 preventing immortalization and anchorage-independent growth in human tonsil epithelial cells. Head Neck 30:139-147.
    • (2008) Head Neck , vol.30 , pp. 139-147
    • Spanos, W.C.1
  • 107
    • 39749192555 scopus 로고    scopus 로고
    • The PDZ binding motif of human papillomavirus type 16 E6 induces PTPN13 loss, which allows anchorage-independent growth and synergizes with Ras for invasive growth
    • Spanos, W. C., et al. 2008. The PDZ binding motif of human papillomavirus type 16 E6 induces PTPN13 loss, which allows anchorage-independent growth and synergizes with Ras for invasive growth. J. Virol. 82:2493-2500.
    • (2008) J. Virol. , vol.82 , pp. 2493-2500
    • Spanos, W.C.1
  • 108
    • 34247153072 scopus 로고    scopus 로고
    • PATJ, a tight junction-associated PDZ protein, is a novel degradation target of high-risk human papillomavirus E6 and the alternatively spliced isoform 18 E6
    • Storrs, C. H., and S. J. Silverstein. 2007. PATJ, a tight junction-associated PDZ protein, is a novel degradation target of high-risk human papillomavirus E6 and the alternatively spliced isoform 18 E6. J. Virol. 81:4080-4090.
    • (2007) J. Virol. , vol.81 , pp. 4080-4090
    • Storrs, C.H.1    Silverstein, S.J.2
  • 109
    • 34248143390 scopus 로고    scopus 로고
    • The MAGUK protein MPP7 binds to the polarity protein hDlg1 and facilitates epithelial tight junction formation
    • Stucke, V. M., E. Timmerman, J. Vandekerckhove, K. Gevaert, and A. Hall. 2007. The MAGUK protein MPP7 binds to the polarity protein hDlg1 and facilitates epithelial tight junction formation. Mol. Biol. Cell 18:1744-1755.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 1744-1755
    • Stucke, V.M.1    Timmerman, E.2    Vandekerckhove, J.3    Gevaert, K.4    Hall, A.5
  • 110
    • 0033613411 scopus 로고    scopus 로고
    • Tax oncoprotein of HTLV-1 binds to the human homologue of Drosophila discs large tumor suppressor protein, hDLG, and perturbs its function in cell growth control
    • Suzuki, T., Y. Ohsugi, M. Uchida-Toita, T. Akiyama, and M. Yoshida. 1999. Tax oncoprotein of HTLV-1 binds to the human homologue of Drosophila discs large tumor suppressor protein, hDLG, and perturbs its function in cell growth control. Oncogene 18:5967-5972.
    • (1999) Oncogene , vol.18 , pp. 5967-5972
    • Suzuki, T.1    Ohsugi, Y.2    Uchida-Toita, M.3    Akiyama, T.4    Yoshida, M.5
  • 111
    • 56749139682 scopus 로고    scopus 로고
    • The epithelial polarity program: machineries involved and their hijacking by cancer
    • Tanos, B., and E. Rodriguez-Boulan. 2008. The epithelial polarity program: machineries involved and their hijacking by cancer. Oncogene 27:6939- 6957.
    • (2008) Oncogene , vol.27 , pp. 6939-6957
    • Tanos, B.1    Rodriguez-Boulan, E.2
  • 112
    • 78649684164 scopus 로고    scopus 로고
    • The SARS coronavirus E protein interacts with PALS1 and alters tight junction formation and epithelial morphogenesis
    • Teoh, K. T., et al. 2010. The SARS coronavirus E protein interacts with PALS1 and alters tight junction formation and epithelial morphogenesis. Mol. Biol. Cell 21:3838-3852.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 3838-3852
    • Teoh, K.T.1
  • 113
    • 0035817789 scopus 로고    scopus 로고
    • HPV E6 and MAGUK protein interactions: determination of the molecular basis for specific protein recognition and degradation
    • Thomas, M., B. Glaunsinger, D. Pim, R. Javier, and L. Banks. 2001. HPV E6 and MAGUK protein interactions: determination of the molecular basis for specific protein recognition and degradation. Oncogene 20:5431-5439.
    • (2001) Oncogene , vol.20 , pp. 5431-5439
    • Thomas, M.1    Glaunsinger, B.2    Pim, D.3    Javier, R.4    Banks, L.5
  • 114
    • 78651504041 scopus 로고    scopus 로고
    • Analysis of the PDZ binding specificities of Influenza A virus NS1 proteins
    • Thomas, M., C. Kranjec, K. Nagasaka, G. Matlashewski, and L. Banks. 2011. Analysis of the PDZ binding specificities of Influenza A virus NS1 proteins. Virol. J. 8:25.
    • (2011) Virol. J. , vol.8 , pp. 25
    • Thomas, M.1    Kranjec, C.2    Nagasaka, K.3    Matlashewski, G.4    Banks, L.5
  • 115
    • 0036676836 scopus 로고    scopus 로고
    • Oncogenic human papillomavirus E6 proteins target the MAGI-2 and MAGI-3 proteins for degradation
    • Thomas, M., et al. 2002. Oncogenic human papillomavirus E6 proteins target the MAGI-2 and MAGI-3 proteins for degradation. Oncogene 21: 5088-5096.
    • (2002) Oncogene , vol.21 , pp. 5088-5096
    • Thomas, M.1
  • 116
    • 30544452459 scopus 로고    scopus 로고
    • The hScrib/Dlg apico-basal control complex is differentially targeted by HPV-16 and HPV-18 E6 proteins
    • Thomas, M., P. Massimi, C. Navarro, J. P. Borg, and L. Banks. 2005. The hScrib/Dlg apico-basal control complex is differentially targeted by HPV-16 and HPV-18 E6 proteins. Oncogene 24:6222-6230.
    • (2005) Oncogene , vol.24 , pp. 6222-6230
    • Thomas, M.1    Massimi, P.2    Navarro, C.3    Borg, J.P.4    Banks, L.5
  • 117
    • 56749095769 scopus 로고    scopus 로고
    • Human papillomaviruses, cervical cancer and cell polarity
    • Thomas, M., et al. 2008. Human papillomaviruses, cervical cancer and cell polarity. Oncogene 27:7018-7030.
    • (2008) Oncogene , vol.27 , pp. 7018-7030
    • Thomas, M.1
  • 118
    • 58149359224 scopus 로고    scopus 로고
    • Human and primate tumour viruses use PDZ binding as an evolutionarily conserved mechanism of targeting cell polarity regulators
    • Tomaić, V., et al. 2009. Human and primate tumour viruses use PDZ binding as an evolutionarily conserved mechanism of targeting cell polarity regulators. Oncogene 28:1-8.
    • (2009) Oncogene , vol.28 , pp. 1-8
    • Tomaić, V.1
  • 119
    • 54749086397 scopus 로고    scopus 로고
    • A specificity map for the PDZ domain family
    • Tonikian, R., et al. 2008. A specificity map for the PDZ domain family. PLoS Biol. 6:e239.
    • (2008) PLoS Biol , vol.6
    • Tonikian, R.1
  • 120
    • 36249022050 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase H1 is a target of the E6 oncoprotein of high-risk genital human papillomaviruses
    • Töpffer, S., A. Muller-Schiffmann, K. Matentzoglu, M. Scheffner, and G. Steger. 2007. Protein tyrosine phosphatase H1 is a target of the E6 oncoprotein of high-risk genital human papillomaviruses. J. Gen. Virol. 88: 2956-2965.
    • (2007) J. Gen. Virol. , vol.88 , pp. 2956-2965
    • Töpffer, S.1    Muller-Schiffmann, A.2    Matentzoglu, K.3    Scheffner, M.4    Steger, G.5
  • 121
    • 27344432181 scopus 로고    scopus 로고
    • PDZ domain-binding motif of human T-cell leukemia virus type 1 Tax oncoprotein is essential for the interleukin 2 independent growth induction of a T-cell line
    • Tsubata, C., et al. 2005. PDZ domain-binding motif of human T-cell leukemia virus type 1 Tax oncoprotein is essential for the interleukin 2 independent growth induction of a T-cell line. Retrovirology 2:46.
    • (2005) Retrovirology , vol.2 , pp. 46
    • Tsubata, C.1
  • 122
    • 67249083873 scopus 로고    scopus 로고
    • Roles of ZO-1 and ZO-2 in establishment of the belt-like adherens and tight junctions with paracellular permselective barrier function
    • Tsukita, S., et al. 2009. Roles of ZO-1 and ZO-2 in establishment of the belt-like adherens and tight junctions with paracellular permselective barrier function. Ann. N. Y. Acad. Sci. 1165:44-52.
    • (2009) Ann. N. Y. Acad. Sci. , vol.1165 , pp. 44-52
    • Tsukita, S.1
  • 123
    • 33747155076 scopus 로고    scopus 로고
    • ZO- 1 and ZO-2 independently determine where claudins are polymerized in tight-junction strand formation
    • Umeda, K., et al. 2006. ZO-1 and ZO-2 independently determine where claudins are polymerized in tight-junction strand formation. Cell 126:741- 754.
    • (2006) Cell , vol.126 , pp. 741-754
    • Umeda, K.1
  • 124
    • 0036848432 scopus 로고    scopus 로고
    • Changes in expression of the human homologue of the Drosophila discs large tumour suppressor protein in high-grade premalignant cervical neoplasias
    • Watson, R. A., et al. 2002. Changes in expression of the human homologue of the Drosophila discs large tumour suppressor protein in high-grade premalignant cervical neoplasias. Carcinogenesis 23:1791-1796.
    • (2002) Carcinogenesis , vol.23 , pp. 1791-1796
    • Watson, R.A.1
  • 125
    • 0346252339 scopus 로고    scopus 로고
    • Activity of the human papillomavirus E6 PDZ-binding motif correlates with an enhanced morphological transformation of immortalized human keratinocytes
    • Watson, R. A., M. Thomas, L. Banks, and S. Roberts. 2003. Activity of the human papillomavirus E6 PDZ-binding motif correlates with an enhanced morphological transformation of immortalized human keratinocytes. J. Cell Sci. 116:4925-4934.
    • (2003) J. Cell Sci. , vol.116 , pp. 4925-4934
    • Watson, R.A.1    Thomas, M.2    Banks, L.3    Roberts, S.4
  • 126
    • 0030796307 scopus 로고    scopus 로고
    • A carboxy-terminal region required by the adenovirus type 9 E4 ORF1 oncoprotein for transformation mediates direct binding to cellular polypeptides
    • Weiss, R. S., and R. T. Javier. 1997. A carboxy-terminal region required by the adenovirus type 9 E4 ORF1 oncoprotein for transformation mediates direct binding to cellular polypeptides. J. Virol. 71:7873-7880.
    • (1997) J. Virol. , vol.71 , pp. 7873-7880
    • Weiss, R.S.1    Javier, R.T.2
  • 127
    • 38849166538 scopus 로고    scopus 로고
    • Tick-borne encephalitis virus NS5 associates with membrane protein scribble and impairs interferon-stimulated JAK-STAT signalling
    • Werme, K., M. Wigerius, and M. Johansson. 2008. Tick-borne encephalitis virus NS5 associates with membrane protein scribble and impairs interferon-stimulated JAK-STAT signalling. Cell Microbiol. 10:696-712.
    • (2008) Cell Microbiol , vol.10 , pp. 696-712
    • Werme, K.1    Wigerius, M.2    Johansson, M.3
  • 128
    • 0037295160 scopus 로고    scopus 로고
    • Binding of HTLV-1 tax oncoprotein to the precursor of interleukin-16, a T cell PDZ domain-containing protein
    • Wilson, K. C., D. M. Center, W. W. Cruikshank, and Y. Zhang. 2003. Binding of HTLV-1 tax oncoprotein to the precursor of interleukin-16, a T cell PDZ domain-containing protein. Virology 306:60-67.
    • (2003) Virology , vol.306 , pp. 60-67
    • Wilson, K.C.1    Center, D.M.2    Cruikshank, W.W.3    Zhang, Y.4
  • 129
    • 4444382955 scopus 로고    scopus 로고
    • Discs large (Dlg1) complexes in lymphocyte activation
    • Xavier, R., et al. 2004. Discs large (Dlg1) complexes in lymphocyte activation. J. Cell Biol. 166:173-178.
    • (2004) J. Cell Biol. , vol.166 , pp. 173-178
    • Xavier, R.1
  • 130
    • 33344455151 scopus 로고    scopus 로고
    • PDZ binding motif of HTLV-1 Tax promotes virus-mediated T-cell proliferation in vitro and persistence in vivo
    • Xie, L., B. Yamamoto, A. Haoudi, O. J. Semmes, and P. L. Green. 2006. PDZ binding motif of HTLV-1 Tax promotes virus-mediated T-cell proliferation in vitro and persistence in vivo. Blood 107:1980-1988.
    • (2006) Blood , vol.107 , pp. 1980-1988
    • Xie, L.1    Yamamoto, B.2    Haoudi, A.3    Semmes, O.J.4    Green, P.L.5
  • 131
    • 66149089133 scopus 로고    scopus 로고
    • PDLIM2 suppresses human T-cell leukemia virus type I Tax-mediated tumorigenesis by targeting Tax into the nuclear matrix for proteasomal degradation
    • Yan, P., et al. 2009. PDLIM2 suppresses human T-cell leukemia virus type I Tax-mediated tumorigenesis by targeting Tax into the nuclear matrix for proteasomal degradation. Blood 113:4370-4380.
    • (2009) Blood , vol.113 , pp. 4370-4380
    • Yan, P.1
  • 132
    • 45549084954 scopus 로고    scopus 로고
    • Knockdown of synapse-associated protein Dlg1 reduces syncytium formation induced by human T-cell leukemia virus type1
    • Yoshida, S., et al. 2008. Knockdown of synapse-associated protein Dlg1 reduces syncytium formation induced by human T-cell leukemia virus type1. Virus Genes 37:9-15.
    • (2008) Virus Genes , vol.37 , pp. 9-15
    • Yoshida, S.1
  • 133
    • 79956374417 scopus 로고    scopus 로고
    • PDlim2 selectively interacts with the PDZ binding motif of highly pathogenic avian H5N1 influenza A virus NS1
    • Yu, J., et al. 2011. PDlim2 selectively interacts with the PDZ binding motif of highly pathogenic avian H5N1 influenza A virus NS1. PLoS One 6:e19511.
    • (2011) PLoS One , vol.6
    • Yu, J.1
  • 134
    • 33947412686 scopus 로고    scopus 로고
    • Structures of a human papillomavirus (HPV) E6 polypeptide bound to MAGUK proteins: mechanisms of targeting tumor suppressors by a high-risk HPV oncoprotein
    • Zhang, Y., et al. 2007. Structures of a human papillomavirus (HPV) E6 polypeptide bound to MAGUK proteins: mechanisms of targeting tumor suppressors by a high-risk HPV oncoprotein. J. Virol. 81:3618-3626.
    • (2007) J. Virol. , vol.81 , pp. 3618-3626
    • Zhang, Y.1
  • 135
    • 77957201252 scopus 로고    scopus 로고
    • Virulence determinants of avian H5N1 influenza A virus in mammalian and avian hosts: role of the C-terminal ESEV motif in the viral NS1 protein
    • Zielecki, F., et al. 2010. Virulence determinants of avian H5N1 influenza A virus in mammalian and avian hosts: role of the C-terminal ESEV motif in the viral NS1 protein. J. Virol. 84:10708-10718.
    • (2010) J. Virol. , vol.84 , pp. 10708-10718
    • Zielecki, F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.