메뉴 건너뛰기




Volumn 2012, Issue , 2012, Pages

Modulation of tight junction structure and function by kinases and phosphatases targeting occludin

Author keywords

[No Author keywords available]

Indexed keywords

BLK KINASE; CAVEOLIN 1; CLAUDIN; FGR KINASE; FOCAL ADHESION KINASE; GAMMA INTERFERON; GROWTH FACTOR; HEMATOPOIETIC CELL KINASE; LIPOPROTEIN RECEPTOR; MARVELD3 PROTEIN; MESSENGER RNA; MYOSIN LIGHT CHAIN; OCCLUDIN; PHOSPHATASE; PHOSPHOTRANSFERASE; PROTEIN KINASE LCK; PROTEIN KINASE LYN; PROTEIN KINASE YES; PROTEIN TYROSINE KINASE; PROTEIN ZO1; PROTEIN ZO2; SYMPLEKIN; TETRASPANIN; THIOL; TIGHT JUNCTION ASSOCIATED MARVEL PROTEIN; TRANSCRIPTION FACTOR MASH1; TRICELLULIN; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG; UNINDEXED DRUG; ZONAB PROTEIN; MEMBRANE PROTEIN;

EID: 84858146983     PISSN: 11107243     EISSN: 11107251     Source Type: Journal    
DOI: 10.1155/2012/807356     Document Type: Review
Times cited : (140)

References (114)
  • 1
    • 0015846194 scopus 로고
    • Further observations on the fine structure of freeze cleaved tight junctions
    • Staehelin L. A., Further observations on the fine structure of freeze cleaved tight junctions Journal of Cell Science 1973 13 3 763 786
    • (1973) Journal of Cell Science , vol.13 , Issue.3 , pp. 763-786
    • Staehelin, L.A.1
  • 3
    • 70449107587 scopus 로고    scopus 로고
    • Two-path impedance spectroscopy for measuring paracellular and transcellular epithelial resistance
    • Krug S. M., Fromm M., Gnzel D., Two-path impedance spectroscopy for measuring paracellular and transcellular epithelial resistance Biophysical Journal 2009 97 8 2202 2211
    • (2009) Biophysical Journal , vol.97 , Issue.8 , pp. 2202-2211
    • Krug, S.M.1    Fromm, M.2    Gnzel, D.3
  • 4
    • 0035320037 scopus 로고    scopus 로고
    • Multifunctional strands in tight junctions
    • DOI 10.1038/35067088
    • Tsukita S., Furuse M., Itoh M., Multifunctional strands in tight junctions Nature Reviews Molecular Cell Biology 2001 2 4 285 293 (Pubitemid 33676971)
    • (2001) Nature Reviews Molecular Cell Biology , vol.2 , Issue.4 , pp. 285-293
    • Tsukita, S.1    Furuse, M.2    Itoh, M.3
  • 6
    • 7244219999 scopus 로고    scopus 로고
    • Establishment and characterization of cultured epithelial cells lacking expression of ZO-1
    • DOI 10.1074/jbc.M406563200
    • Umeda K., Matsui T., Nakayama M., Furuse E., Sasaki H., Furuse M., Tsukita S., Establishment and characterization of cultured epithelial cells lacking expression of ZO-1 Journal of Biological Chemistry 2004 279 43 44785 44794 (Pubitemid 39430889)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.43 , pp. 44785-44794
    • Umeda, K.1    Matsui, T.2    Nakayama, M.3    Furuse, E.4    Sasaki, H.5    Furuse, M.6    Tsukita, S.7
  • 7
    • 40749084863 scopus 로고    scopus 로고
    • Early embryonic lethality of mice lacking ZO-2, but not ZO-3, reveals critical and nonredundant roles for individual zonula occludens proteins in mammalian development
    • Xu J., Kausalya P. J., Phua D. C. Y., Ali S. M., Hossain Z., Hunziker W., Early embryonic lethality of mice lacking ZO-2, but not ZO-3, reveals critical and nonredundant roles for individual zonula occludens proteins in mammalian development Molecular and Cellular Biology 2008 28 5 1669 1678
    • (2008) Molecular and Cellular Biology , vol.28 , Issue.5 , pp. 1669-1678
    • Xu, J.1    Kausalya, P.J.2    Phua, D.C.Y.3    Ali, S.M.4    Hossain, Z.5    Hunziker, W.6
  • 8
    • 33747155076 scopus 로고    scopus 로고
    • ZO-1 and ZO-2 Independently Determine Where Claudins Are Polymerized in Tight-Junction Strand Formation
    • DOI 10.1016/j.cell.2006.06.043, PII S0092867406009603
    • Umeda K., Ikenouchi J., Katahira-Tayama S., Furuse K., Sasaki H., Nakayama M., Matsui T., Tsukita S., Furuse M., Tsukita S., ZO-1 and ZO-2 independently determine where claudins are polymerized in tight-junction strand formation Cell 2006 126 4 741 754 (Pubitemid 44233624)
    • (2006) Cell , vol.126 , Issue.4 , pp. 741-754
    • Umeda, K.1    Ikenouchi, J.2    Katahira-Tayama, S.3    Furuse, K.4    Sasaki, H.5    Nakayama, M.6    Matsui, T.7    Tsukita, S.8    Furuse, M.9    Tsukita, S.10
  • 9
    • 39849103311 scopus 로고    scopus 로고
    • The cytoplasmic plaque of tight junctions: A scaffolding and signalling center
    • DOI 10.1016/j.bbamem.2007.09.032, PII S0005273607003926
    • Guillemot L., Paschoud S., Pulimeno P., Foglia A., Citi S., The cytoplasmic plaque of tight junctions: a scaffolding and signalling center Biochimica et Biophysica Acta 2008 1778 3 601 613 (Pubitemid 351317804)
    • (2008) Biochimica et Biophysica Acta - Biomembranes , vol.1778 , Issue.3 , pp. 601-613
    • Guillemot, L.1    Paschoud, S.2    Pulimeno, P.3    Foglia, A.4    Citi, S.5
  • 12
    • 33645747414 scopus 로고    scopus 로고
    • Claudins in occluding junctions of humans and flies
    • Furuse M., Tsukita S., Claudins in occluding junctions of humans and flies Trends in Cell Biology 2006 16 4 181 188
    • (2006) Trends in Cell Biology , vol.16 , Issue.4 , pp. 181-188
    • Furuse, M.1    Tsukita, S.2
  • 15
    • 2942722817 scopus 로고    scopus 로고
    • MARVEL: A conserved domain involved in membrane apposition events
    • DOI 10.1016/S0968-0004(02)02229-6, PII S0968000402022296
    • Snchez-Pulido L., Martn-Belmonte F., Valencia A., Alonso M. A., MARVEL: a conserved domain involved in membrane apposition events Trends in Biochemical Sciences 2002 27 12 599 601 (Pubitemid 35435304)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.12 , pp. 599-601
    • Sanchez-Pulido, L.1    Martin-Belmonte, F.2    Valencia, A.3    Alonso, M.A.4
  • 17
    • 29144533473 scopus 로고    scopus 로고
    • Tricellulin constitutes a novel barrier at tricellular contacts of epithelial cells
    • DOI 10.1083/jcb.200510043
    • Ikenouchi J., Furuse M., Furuse K., Sasaki H., Tsukita S., Tsukita S., Tricellulin constitutes a novel barrier at tricellular contacts of epithelial cells Journal of Cell Biology 2005 171 6 939 945 (Pubitemid 41815826)
    • (2005) Journal of Cell Biology , vol.171 , Issue.6 , pp. 939-945
    • Ikenouchi, J.1    Furuse, M.2    Furuse, K.3    Sasaki, H.4    Tsukita, S.5    Tsukita, S.6
  • 19
    • 74549219792 scopus 로고    scopus 로고
    • Identification of MarvelD3 as a tight junction-associated transmembrane protein of the occludin family
    • Steed E., Rodrigues N. T. L., Balda M. S., Matter K., Identification of MarvelD3 as a tight junction-associated transmembrane protein of the occludin family BMC Cell Biology 2009 10, article 95
    • (2009) BMC Cell Biology , vol.1095
    • Steed, E.1    Rodrigues, N.T.L.2    Balda, M.S.3    Matter, K.4
  • 21
    • 0141644213 scopus 로고    scopus 로고
    • The JAM family of junctional adhesion molecules
    • DOI 10.1016/S0955-0674(03)00104-2
    • Bazzoni G., The JAM family of junctional adhesion molecules Current Opinion in Cell Biology 2003 15 5 525 530 (Pubitemid 37176960)
    • (2003) Current Opinion in Cell Biology , vol.15 , Issue.5 , pp. 525-530
    • Bazzoni, G.1
  • 22
    • 79960756426 scopus 로고    scopus 로고
    • Pathobiology of junctional adhesion molecules
    • Bazzoni G., Pathobiology of junctional adhesion molecules Antioxidants and Redox Signaling 2011 15 5 1221 1234
    • (2011) Antioxidants and Redox Signaling , vol.15 , Issue.5 , pp. 1221-1234
    • Bazzoni, G.1
  • 27
    • 0030043414 scopus 로고    scopus 로고
    • Overexpression of occludin, a tight junction-associated integral membrane protein, induces the formation of intracellular multilamellar bodies bearing tight junction-like structures
    • Furuse M., Fujimoto K., Sato N., Hirase T., Tsukita S., Tsukita S., Overexpression of occludin, a tight junction-associated integral membrane protein, induces the formation of intracellular multilamellar bodies bearing tight junction-like structures Journal of Cell Science 1996 109 2 429 435 (Pubitemid 26057662)
    • (1996) Journal of Cell Science , vol.109 , Issue.2 , pp. 429-435
    • Furuse, M.1    Fujimoto, K.2    Sato, N.3    Hirase, T.4    Tsukita, S.5    Tsukita, S.6
  • 28
    • 0029799520 scopus 로고    scopus 로고
    • Functional dissociation of paracellular permeability and transepithelial electrical resistance and disruption of the apical-basolateral intramembrane diffusion barrier by expression of a mutant tight junction membrane protein
    • Balda M. S., Whitney J. A., Flores C., Gonzlez S., Cereijido M., Matter K., Functional dissociation of paracellular permeability and transepithelial electrical resistance and disruption of the apical-basolateral intramembrane diffusion barrier by expression of a mutant tight junction membrane protein Journal of Cell Biology 1996 134 4 1031 1049 (Pubitemid 26278226)
    • (1996) Journal of Cell Biology , vol.134 , Issue.4 , pp. 1031-1049
    • Balda, M.S.1    Whitney, J.A.2    Flores, C.3    Gonzalez, S.4    Cereijido, M.5    Matter, K.6
  • 31
    • 0034038626 scopus 로고    scopus 로고
    • Multiple domains of occludin are involved in the regulation of paracellular permeability
    • DOI 10.1002/(SICI)1097-4644(20000701)78:1<85::AID-JCB8>3.0.CO;2-F
    • Balda M. S., Flores-Maldonado C., Cereijido M., Matter K., Multiple domains of occludin are involved in the regulation of paracellular permeability Journal of Cellular Biochemistry 2000 78 1 85 96 (Pubitemid 30346385)
    • (2000) Journal of Cellular Biochemistry , vol.78 , Issue.1 , pp. 85-96
    • Balda, M.S.1    Flores-Maldonado, C.2    Cereijido, M.3    Matter, K.4
  • 34
    • 0032577975 scopus 로고    scopus 로고
    • Claudin-1 and -2: Novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin
    • DOI 10.1083/jcb.141.7.1539
    • Furuse M., Fujita K., Hiiragi T., Fujimoto K., Tsukita S., Claudin-1 and -2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin Journal of Cell Biology 1998 141 7 1539 1550 (Pubitemid 28309169)
    • (1998) Journal of Cell Biology , vol.141 , Issue.7 , pp. 1539-1550
    • Furuse, M.1    Fujita, K.2    Hiiragi, T.3    Fujimoto, K.4    Tsukita, S.5
  • 35
    • 0032547833 scopus 로고    scopus 로고
    • A single gene product, claudin-1 or -2, reconstitutes tight junction strands and recruits occludin in fibroblasts
    • DOI 10.1083/jcb.143.2.391
    • Furuse M., Sasaki H., Fujimoto K., Tsukita S., A single gene product, claudin-1 or -2, reconstitutes tight junction strands and recruits occludin in fibroblasts Journal of Cell Biology 1998 143 2 391 401 (Pubitemid 28487858)
    • (1998) Journal of Cell Biology , vol.143 , Issue.2 , pp. 391-401
    • Furuse, M.1    Sasaki, H.2    Fujimoto, K.3    Tsukita, S.4
  • 38
    • 77955992054 scopus 로고    scopus 로고
    • Occludin is required for cytokine-induced regulation of tight junction barriers
    • van Itallie C. M., Fanning A. S., Holmes J., Anderson J. M., Occludin is required for cytokine-induced regulation of tight junction barriers Journal of Cell Science 2010 123 16 2844 2852
    • (2010) Journal of Cell Science , vol.123 , Issue.16 , pp. 2844-2852
    • Van Itallie, C.M.1    Fanning, A.S.2    Holmes, J.3    Anderson, J.M.4
  • 40
  • 41
    • 55949121106 scopus 로고    scopus 로고
    • Inventions designed to enhance drug delivery across epithelial and endothelial cells through tha paracellular pathway
    • Gonzlez-Mariscal L., Hernndez S., Vega J., Inventions designed to enhance drug delivery across epithelial and endothelial cells through tha paracellular pathway Recent Patents on Drug Delivery and Formulation 2008 2 2 145 176
    • (2008) Recent Patents on Drug Delivery and Formulation , vol.2 , Issue.2 , pp. 145-176
    • Gonzlez-Mariscal, L.1    Hernndez, S.2    Vega, J.3
  • 42
    • 24644496823 scopus 로고    scopus 로고
    • Mammalian tight junctions in the regulation of epithelial differentiation and proliferation
    • DOI 10.1016/j.ceb.2005.08.003, PII S0955067405001067
    • Matter K., Aijaz S., Tsapara A., Balda M. S., Mammalian tight junctions in the regulation of epithelial differentiation and proliferation Current Opinion in Cell Biology 2005 17 5 453 458 (Pubitemid 41267158)
    • (2005) Current Opinion in Cell Biology , vol.17 , Issue.5 SPEC. ISS. , pp. 453-458
    • Matter, K.1    Aijaz, S.2    Tsapara, A.3    Balda, M.S.4
  • 43
    • 0037336565 scopus 로고    scopus 로고
    • Signalling to and from tight junctions
    • DOI 10.1038/nrm1055
    • Matter K., Balda M. S., Signalling to and from tight junctions Nature Reviews Molecular Cell Biology 2003 4 3 225 236 (Pubitemid 36288044)
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.3 , pp. 225-236
    • Matter, K.1    Balda, M.S.2
  • 45
    • 63849237020 scopus 로고    scopus 로고
    • Regulation of epithelial apical junctional complex by Rho family GTPases
    • Samarin S., Nusrat A., Regulation of epithelial apical junctional complex by Rho family GTPases Frontiers in Bioscience 2009 14 1129 1142
    • (2009) Frontiers in Bioscience , vol.14 , pp. 1129-1142
    • Samarin, S.1    Nusrat, A.2
  • 46
    • 79551612886 scopus 로고    scopus 로고
    • Spatially restricted activation of RhoA signalling at epithelial junctions by p114RhoGEF drives junction formation and morphogenesis
    • Terry S. J., Zihni C., Elbediwy A., Vitiello E., Leefa Chong San I. V., Balda M. S., Matter K., Spatially restricted activation of RhoA signalling at epithelial junctions by p114RhoGEF drives junction formation and morphogenesis Nature Cell Biology 2011 13 2 159 166
    • (2011) Nature Cell Biology , vol.13 , Issue.2 , pp. 159-166
    • Terry, S.J.1    Zihni, C.2    Elbediwy, A.3    Vitiello, E.4    Leefa Chong San, I.V.5    Balda, M.S.6    Matter, K.7
  • 47
    • 17844402719 scopus 로고    scopus 로고
    • Binding of GEF-H1 to the tight junction-associated adaptor cingulin results in inhibition of Rho signaling and G1/S phase transition
    • DOI 10.1016/j.devcel.2005.03.003, PII S1534580705000869
    • Aijaz S., D'Atri F., Citi S., Balda M. S., Matter K., Binding of GEF-H1 to the tight junction-associated adaptor cingulin results in inhibition of Rho signaling and G1/S phase transition Developmental Cell 2005 8 5 777 786 (Pubitemid 40585299)
    • (2005) Developmental Cell , vol.8 , Issue.5 , pp. 777-786
    • Aijaz, S.1    D'Atri, F.2    Citi, S.3    Balda, M.S.4    Matter, K.5
  • 48
    • 0038021222 scopus 로고    scopus 로고
    • Epithelial cell adhesion and the regulation of gene expression
    • DOI 10.1016/S0962-8924(03)00105-3
    • Balda M. S., Matter K., Epithelial cell adhesion and the regulation of gene expression Trends in Cell Biology 2003 13 6 310 318 (Pubitemid 36638798)
    • (2003) Trends in Cell Biology , vol.13 , Issue.6 , pp. 310-318
    • Balda, M.S.1    Matter, K.2
  • 49
    • 34249732713 scopus 로고    scopus 로고
    • Epithelial tight junctions, gene expression and nucleo-junctional interplay
    • DOI 10.1242/jcs.005975
    • Matter K., Balda M. S., Epithelial tight junctions, gene expression and nucleo-junctional interplay Journal of Cell Science 2007 120 9 1505 1511 (Pubitemid 46831780)
    • (2007) Journal of Cell Science , vol.120 , Issue.9 , pp. 1505-1511
    • Matter, K.1    Balda, M.S.2
  • 51
    • 0035933894 scopus 로고    scopus 로고
    • Reassembly of the tight junction after oxidative stress depends on tyrosine kinase activity
    • Meyer T. N., Schwesinger C., Ye J., Denker B. M., Nigam S. K., Reassembly of the tight junction after oxidative stress depends on tyrosine kinase activity Journal of Biological Chemistry 2001 276 25 22048 22055
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.25 , pp. 22048-22055
    • Meyer, T.N.1    Schwesinger, C.2    Ye, J.3    Denker, B.M.4    Nigam, S.K.5
  • 52
    • 0034099223 scopus 로고    scopus 로고
    • Restoration of tight junction structure and barrier function by down- regulation of the mitogen-activated protein kinase pathway in Ras-transformed Madin-Darby canine kidney cells
    • Chen Y. H., Lu Q., Schneeberger E. E., Goodenough D. A., Restoration of tight junction structure and barrier function by down-regulation of the mitogen-activated protein kinase pathway in Ras-transformed Madin-Darby canine kidney cells Molecular Biology of the Cell 2000 11 3 849 862 (Pubitemid 30159306)
    • (2000) Molecular Biology of the Cell , vol.11 , Issue.3 , pp. 849-862
    • Chen, Y.-H.1    Lu, Q.2    Schneeberger, E.E.3    Goodenough, D.A.4
  • 53
    • 0034703027 scopus 로고    scopus 로고
    • The coiled-coil domain of occludin can act to organize structural and functional elements of the epithelial tight junction
    • DOI 10.1074/jbc.M002450200
    • Nusrat A., Chen J. A., Foley C. S., Liang T. W., Tom J., Cromwell M., Quan C., Mrsny R. J., The coiled-coil domain of occludin can act to organize structural and functional elements of the epithelial tight junction Journal of Biological Chemistry 2000 275 38 29816 29822 (Pubitemid 32043866)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.38 , pp. 29816-29822
    • Nusrat, A.1    Chen, J.A.2    Foley, C.S.3    Liang, T.W.4    Tom, J.5    Cromwell, M.6    Quan, C.7    Mrsny, R.J.8
  • 54
    • 79952100337 scopus 로고    scopus 로고
    • C-Yes regulates cell adhesion at the blood-testis barrier and the apical ectoplasmic specialization in the seminiferous epithelium of rat testes
    • Xiao X., Mruk D. D., Lee W. M., Cheng C. Y., c-Yes regulates cell adhesion at the blood-testis barrier and the apical ectoplasmic specialization in the seminiferous epithelium of rat testes International Journal of Biochemistry and Cell Biology 2011 43 4 651 665
    • (2011) International Journal of Biochemistry and Cell Biology , vol.43 , Issue.4 , pp. 651-665
    • Xiao, X.1    Mruk, D.D.2    Lee, W.M.3    Cheng, C.Y.4
  • 55
    • 0038146915 scopus 로고    scopus 로고
    • Expression of kinase-inactive c-Src delays oxidative stress-induced disassembly and accelerates calcium-mediated reassembly of tight junctions in the Caco-2 cell monolayer
    • DOI 10.1074/jbc.M211710200
    • Basuroy S., Sheth P., Kuppuswamy D., Balasubramanian S., Ray R. M., Rao R. K., Expression of kinase-inactive c-Src delays oxidative stress-induced disassembly and accelerates calcium-mediated reassembly of tight junctions in the Caco-2 cell monolayer Journal of Biological Chemistry 2003 278 14 11916 11924 (Pubitemid 36800164)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.14 , pp. 11916-11924
    • Basuroy, S.1    Sheth, P.2    Kuppuswamy, D.3    Balasubramanian, S.4    Ray, R.M.5    Rao, R.K.6
  • 56
    • 0037428288 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of occludin attenuates its interactions with ZO-1, ZO-2, and ZO-3
    • DOI 10.1016/S0006-291X(03)00167-0
    • Kale G., Naren A. P., Sheth P., Rao R. K., Tyrosine phosphorylation of occludin attenuates its interactions with ZO-1, ZO-2, and ZO-3 Biochemical and Biophysical Research Communications 2003 302 2 324 329 (Pubitemid 36397924)
    • (2003) Biochemical and Biophysical Research Communications , vol.302 , Issue.2 , pp. 324-329
    • Kale, G.1    Naren, A.P.2    Sheth, P.3    Rao, R.K.4
  • 59
    • 1542677112 scopus 로고    scopus 로고
    • Role of phosphatidylinositol 3-kinase in oxidative stress-induced disruption of tight junctions
    • Sheth P., Basuroy S., Li C., Naren A. P., Rao R. K., Role of phosphatidylinositol 3-kinase in oxidative stress-induced disruption of tight junctions The Journal of Biological Chemistry 2003 278 49 49239 49245
    • (2003) The Journal of Biological Chemistry , vol.278 , Issue.49 , pp. 49239-49245
    • Sheth, P.1    Basuroy, S.2    Li, C.3    Naren, A.P.4    Rao, R.K.5
  • 60
    • 77951184829 scopus 로고    scopus 로고
    • Cellular functions of FAK kinases: Insight into molecular mechanisms and novel functions
    • Schaller M. D., Cellular functions of FAK kinases: insight into molecular mechanisms and novel functions Journal of Cell Science 2010 123 7 1007 1013
    • (2010) Journal of Cell Science , vol.123 , Issue.7 , pp. 1007-1013
    • Schaller, M.D.1
  • 61
    • 82955162793 scopus 로고    scopus 로고
    • Focal adhesion kinase regulation of mechanotransduction and its impact on endothelial cell functions
    • Zebda N., Dubrovskyi O., Birukov K. G., Focal adhesion kinase regulation of mechanotransduction and its impact on endothelial cell functions Microvascular Research 2012 83 1 71 81
    • (2012) Microvascular Research , vol.83 , Issue.1 , pp. 71-81
    • Zebda, N.1    Dubrovskyi, O.2    Birukov, K.G.3
  • 62
    • 22544451542 scopus 로고    scopus 로고
    • Acetaldehyde disrupts tight junctions and adherens junctions in human colonic mucosa: Protection by EGF and L-glutamine
    • Basuroy S., Sheth P., Mansbach C. M., Rao R. K., Acetaldehyde disrupts tight junctions and adherens junctions in human colonic mucosa: protection by EGF and L-glutamine American Journal of Physiology 2005 289 2 G367 G375
    • (2005) American Journal of Physiology , vol.289 , Issue.2
    • Basuroy, S.1    Sheth, P.2    Mansbach, C.M.3    Rao, R.K.4
  • 64
    • 78149353346 scopus 로고    scopus 로고
    • Rho-kinase/ROCK: A key regulator of the cytoskeleton and cell polarity
    • Amano M., Nakayama M., Kaibuchi K., Rho-kinase/ROCK: a key regulator of the cytoskeleton and cell polarity Cytoskeleton 2010 67 9 545 554
    • (2010) Cytoskeleton , vol.67 , Issue.9 , pp. 545-554
    • Amano, M.1    Nakayama, M.2    Kaibuchi, K.3
  • 65
    • 0031695576 scopus 로고    scopus 로고
    • Rho GTPase signaling regulates tight junction assembly and protects tight junctions during ATP depletion
    • Gopalakrishnan S., Raman N., Atkinson S. J., Marrs J. A., Rho GTPase signaling regulates tight junction assembly and protects tight junctions during ATP depletion American Journal of Physiology 1998 275 3 C798 C809
    • (1998) American Journal of Physiology , vol.275 , Issue.3
    • Gopalakrishnan, S.1    Raman, N.2    Atkinson, S.J.3    Marrs, J.A.4
  • 68
    • 33745094734 scopus 로고    scopus 로고
    • Rho-mediated regulation of tight junctions during monocyte migration across the blood-brain barrier in HIV-1 encephalitis (HIVE)
    • DOI 10.1182/blood-2005-11-4721
    • Persidsky Y., Heilman D., Haorah J., Zelivyanskaya M., Persidsky R., Weber G. A., Shimokawa H., Kaibuchi K., Ikezu T., Rho-mediated regulation of tight junctions during monocyte migration across the blood-brain barrier in HIV-1 encephalitis (HIVE) Blood 2006 107 12 4770 4780 (Pubitemid 43882628)
    • (2006) Blood , vol.107 , Issue.12 , pp. 4770-4780
    • Persidsky, Y.1    Heilman, D.2    Haorah, J.3    Zelivyanskaya, M.4    Persidsky, R.5    Weber, G.A.6    Shimokawa, H.7    Kaibuchi, K.8    Ikezu, T.9
  • 70
    • 76749088358 scopus 로고    scopus 로고
    • Pathological roles of MAPK signaling pathways in human diseases
    • Kim E. K., Choi E. J., Pathological roles of MAPK signaling pathways in human diseases Biochimica et Biophysica Acta 2010 1802 4 396 405
    • (2010) Biochimica et Biophysica Acta , vol.1802 , Issue.4 , pp. 396-405
    • Kim, E.K.1    Choi, E.J.2
  • 72
    • 0344688189 scopus 로고    scopus 로고
    • Activation of ERK1/2 MAP kinase pathway induces tight junction disruption in human corneal epithelial cells
    • DOI 10.1016/j.exer.2003.09.002
    • Wang Y., Zhang J., Yi X. J., Yu F. S., Activation of ERK1/2 MAP kinase pathway induces tight junction disruption in human corneal epithelial cells Experimental Eye Research 2004 78 1 125 136 (Pubitemid 37518251)
    • (2004) Experimental Eye Research , vol.78 , Issue.1 , pp. 125-136
    • Wang, Y.1    Zhang, J.2    Yi, X.-J.3    Yu, F.-S.X.4
  • 73
    • 0034695923 scopus 로고    scopus 로고
    • Oncogenic Raf-1 disrupts epithelial tight junctions via downregulation of occludin
    • Li D., Mrsny R. J., Oncogenic Raf-1 disrupts epithelial tight junctions via downregulation of occludin Journal of Cell Biology 2000 148 4 791 800
    • (2000) Journal of Cell Biology , vol.148 , Issue.4 , pp. 791-800
    • Li, D.1    Mrsny, R.J.2
  • 74
    • 30044442771 scopus 로고    scopus 로고
    • MAPK interacts with occludin and mediates EGF-induced prevention of tight junction disruption by hydrogen peroxide
    • DOI 10.1042/BJ20050959
    • Basuroy S., Seth A., Elias B., Naren A. P., Rao R., MAPK interacts with occludin and mediates EGF-induced prevention of tight junction disruption by hydrogen peroxide Biochemical Journal 2006 393 1 69 77 (Pubitemid 43049303)
    • (2006) Biochemical Journal , vol.393 , Issue.1 , pp. 69-77
    • Basuroy, S.1    Seth, A.2    Elias, B.3    Naren, A.P.4    Rao, R.5
  • 75
    • 79551482121 scopus 로고    scopus 로고
    • Contrasting effects of ERK on tight junction integrity in differentiated and under-differentiated Caco-2 cell monolayers
    • Aggarwal S., Suzuki T., Taylor W. L., Bhargava A., Rao R. K., Contrasting effects of ERK on tight junction integrity in differentiated and under-differentiated Caco-2 cell monolayers Biochemical Journal 2011 433 1 51 63
    • (2011) Biochemical Journal , vol.433 , Issue.1 , pp. 51-63
    • Aggarwal, S.1    Suzuki, T.2    Taylor, W.L.3    Bhargava, A.4    Rao, R.K.5
  • 77
    • 79959813014 scopus 로고    scopus 로고
    • ERK is involved in EGF-mediated protection of tight junctions, but not adherens junctions, in acetaldehyde-treated Caco-2 cell monolayers
    • Samak G., Aggarwal S., Rao R. K., ERK is involved in EGF-mediated protection of tight junctions, but not adherens junctions, in acetaldehyde-treated Caco-2 cell monolayers American Journal of Physiology 2011 301 1 G50 G59
    • (2011) American Journal of Physiology , vol.301 , Issue.1
    • Samak, G.1    Aggarwal, S.2    Rao, R.K.3
  • 78
    • 77956997586 scopus 로고    scopus 로고
    • C-Jun NH2-terminal kinase-2 mediates osmotic stress-induced tight junction disruption in the intestinal epithelium
    • Samak G., Suzuki T., Bhargava A., Rao R. K., c-Jun NH2-terminal kinase-2 mediates osmotic stress-induced tight junction disruption in the intestinal epithelium American Journal of Physiology 2010 299 3 G572 G584
    • (2010) American Journal of Physiology , vol.299 , Issue.3
    • Samak, G.1    Suzuki, T.2    Bhargava, A.3    Rao, R.K.4
  • 79
    • 55949109631 scopus 로고    scopus 로고
    • Structural basis of protein kinase C isoform function
    • Steinberg S. F., Structural basis of protein kinase C isoform function Physiological Reviews 2008 88 4 1341 1378
    • (2008) Physiological Reviews , vol.88 , Issue.4 , pp. 1341-1378
    • Steinberg, S.F.1
  • 82
    • 27744493501 scopus 로고    scopus 로고
    • Assembly of tight junction is regulated by the antagonism of conventional and novel protein kinase C isoforms
    • DOI 10.1016/j.biocel.2005.09.001, PII S1357272505002748
    • Andreeva A. Y., Piontek J., Blasig I. E., Utepbergenov D. I., Assembly of tight junction is regulated by the antagonism of conventional and novel protein kinase C isoforms International Journal of Biochemistry and Cell Biology 2006 38 2 222 233 (Pubitemid 41619451)
    • (2006) International Journal of Biochemistry and Cell Biology , vol.38 , Issue.2 , pp. 222-233
    • Andreeva, A.Y.1    Piontek, J.2    Blasig, I.E.3    Utepbergenov, D.I.4
  • 84
    • 79959736965 scopus 로고    scopus 로고
    • Protein kinase Czeta phosphorylates occludin and promotes assembly of epithelial tight junctions
    • Jain S., Suzuki T., Seth A., Samak G., Rao R., Protein kinase Czeta phosphorylates occludin and promotes assembly of epithelial tight junctions Biochemical Journal 2011 437 2 289 299
    • (2011) Biochemical Journal , vol.437 , Issue.2 , pp. 289-299
    • Jain, S.1    Suzuki, T.2    Seth, A.3    Samak, G.4    Rao, R.5
  • 86
    • 33645968728 scopus 로고    scopus 로고
    • Casein kinase i associates with and phosphorylates the tight junction protein occludin
    • McKenzie J. A. G., Riento K., Ridley A. J., Casein kinase I associates with and phosphorylates the tight junction protein occludin FEBS Letters 2006 580 9 2388 2394
    • (2006) FEBS Letters , vol.580 , Issue.9 , pp. 2388-2394
    • McKenzie, J.A.G.1    Riento, K.2    Ridley, A.J.3
  • 88
    • 70349336104 scopus 로고    scopus 로고
    • Protein kinase CK2 in health and disease: Cellular functions of protein kinase CK2: A dynamic affair
    • Filhol O., Cochet C., Protein kinase CK2 in health and disease: cellular functions of protein kinase CK2: a dynamic affair Cellular and Molecular Life Sciences 2009 66 11-12 1830 1839
    • (2009) Cellular and Molecular Life Sciences , vol.66 , Issue.1112 , pp. 1830-1839
    • Filhol, O.1    Cochet, C.2
  • 89
    • 70349186117 scopus 로고    scopus 로고
    • Protein kinase CK2 in health and disease: From birth to death: The role of protein kinase CK2 in the regulation of cell proliferation and survival
    • St-Denis N. A., Litchfield D. W., Protein kinase CK2 in health and disease: from birth to death: the role of protein kinase CK2 in the regulation of cell proliferation and survival Cellular and Molecular Life Sciences 2009 66 11-12 1817 1829
    • (2009) Cellular and Molecular Life Sciences , vol.66 , Issue.1112 , pp. 1817-1829
    • St-Denis, N.A.1    Litchfield, D.W.2
  • 90
    • 0033199904 scopus 로고    scopus 로고
    • Xenopus laevis occludin: Identification of in vitro phosphorylation sites by protein kinase CK2 and association with cingulin
    • DOI 10.1046/j.1432-1327.1999.00616.x
    • Cordenonsi M., Turco F., D'Atri F., Hammar E., Martinucci G., Meggio F., Citi S., Xenopus laevis occludin: identification of in vitro phosphorylation sites by protein kinase CK2 and association with cingulin European Journal of Biochemistry 1999 264 2 374 384 (Pubitemid 29424441)
    • (1999) European Journal of Biochemistry , vol.264 , Issue.2 , pp. 374-384
    • Cordenonsi, M.1    Turco, F.2    D'Atri, F.3    Hammar, E.4    Martinucci, G.5    Meggio, F.6    Citi, S.7
  • 91
    • 0038201989 scopus 로고    scopus 로고
    • Occludin phosphorylation: Identification of an occludin kinase in brain and cell extracts as CK2
    • DOI 10.1016/S0014-5793(03)00525-8
    • Smales C., Ellis M., Baumber R., Hussain N., Desmond H., Staddon J. M., Occludin phosphorylation: identification of an occludin kinase in brain and cell extracts as CK2 FEBS Letters 2003 545 2-3 161 166 (Pubitemid 36694694)
    • (2003) FEBS Letters , vol.545 , Issue.2-3 , pp. 161-166
    • Smales, C.1    Ellis, M.2    Baumber, R.3    Hussain, N.4    Desmond, H.5    Staddon, J.M.6
  • 95
    • 0032752371 scopus 로고    scopus 로고
    • Requirement for Ras and phosphatidylinositol 3-kinase signaling uncouples the glucocorticoid-induced junctional organization and transepithelial electrical resistance in mammary tumor cells
    • Woo P. L., Ching D., Guan Y., Firestone G. L., Requirement for Ras and phosphatidylinositol 3-kinase signaling uncouples the glucocorticoid-induced junctional organization and transepithelial electrical resistance in mammary tumor cells Journal of Biological Chemistry 1999 274 46 32818 32828 (Pubitemid 129535315)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.46 , pp. 32818-32828
    • Woo, P.L.1    Ching, D.2    Guan, Y.3    Firestone, G.L.4
  • 97
    • 47949089077 scopus 로고    scopus 로고
    • VEGF-targeted therapy: Mechanisms of anti-tumour activity
    • Ellis L. M., Hicklin D. J., VEGF-targeted therapy: mechanisms of anti-tumour activity Nature Reviews Cancer 2008 8 8 579 591
    • (2008) Nature Reviews Cancer , vol.8 , Issue.8 , pp. 579-591
    • Ellis, L.M.1    Hicklin, D.J.2
  • 98
    • 79957925832 scopus 로고    scopus 로고
    • Vascular endothelial growth factors and receptors: Anti-angiogenic therapy in the treatment of cancer
    • Tugues S., Koch S., Gualandi L., Li X., Claesson-Welsh L., Vascular endothelial growth factors and receptors: anti-angiogenic therapy in the treatment of cancer Molecular Aspects of Medicine 2011 32 2 88 111
    • (2011) Molecular Aspects of Medicine , vol.32 , Issue.2 , pp. 88-111
    • Tugues, S.1    Koch, S.2    Gualandi, L.3    Li, X.4    Claesson-Welsh, L.5
  • 99
    • 0033551811 scopus 로고    scopus 로고
    • Vascular endothelial growth factor induces rapid phosphorylation of tight junction proteins occludin and zonula occludens 1. A potential mechanism for vascular permeability in diabetic retinopathy and tumors
    • Antonetti D. A., Barber A. J., Hollinger L. A., Wolpert E. B., Gardner T. W., Vascular endothelial growth factor induces rapid phosphorylation of tight junction proteins occludin and zonula occludens 1. A potential mechanism for vascular permeability in diabetic retinopathy and tumors Journal of Biological Chemistry 1999 274 33 23463 23467
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.33 , pp. 23463-23467
    • Antonetti, D.A.1    Barber, A.J.2    Hollinger, L.A.3    Wolpert, E.B.4    Gardner, T.W.5
  • 101
    • 68949129005 scopus 로고    scopus 로고
    • Occludin phosphorylation and ubiquitination regulate tight junction trafficking and vascular endothelial growth factor-induced permeability
    • Murakami T., Felinski E. A., Antonetti D. A., Occludin phosphorylation and ubiquitination regulate tight junction trafficking and vascular endothelial growth factor-induced permeability Journal of Biological Chemistry 2009 284 31 21036 21046
    • (2009) Journal of Biological Chemistry , vol.284 , Issue.31 , pp. 21036-21046
    • Murakami, T.1    Felinski, E.A.2    Antonetti, D.A.3
  • 102
    • 0037155884 scopus 로고    scopus 로고
    • The tight junction-specific protein occludin is a functional target of the E3 ubiquitin-protein ligase itch
    • DOI 10.1074/jbc.M111384200
    • Traweger A., Fang D., Liu Y. C., Stelzhammer W., Krizbai I. A., Fresser F., Bauer H. C., Bauer H., The tight junction-specific protein occludin is a functional target of the E3 ubiquitin-protein ligase Itch Journal of Biological Chemistry 2002 277 12 10201 10208 (Pubitemid 34968134)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.12 , pp. 10201-10208
    • Traweger, A.1    Fang, D.2    Liu, Y.-C.3    Stelzhammer, W.4    Krizbai, I.A.5    Fresser, F.6    Bauer, H.-C.7    Bauer, H.8
  • 103
    • 70350340056 scopus 로고    scopus 로고
    • Serine/threonine phosphatases: Mechanism through structure
    • Shi Y., Serine/threonine phosphatases: mechanism through structure Cell 2009 139 3 468 484
    • (2009) Cell , vol.139 , Issue.3 , pp. 468-484
    • Shi, Y.1
  • 104
    • 61849136595 scopus 로고    scopus 로고
    • CD45, CD148, and Lyp/Pep: Critical phosphatases regulating Src family kinase signaling networks in immune cells
    • Hermiston M. L., Zikherman J., Zhu J. W., CD45, CD148, and Lyp/Pep: critical phosphatases regulating Src family kinase signaling networks in immune cells Immunological Reviews 2009 228 1 288 311
    • (2009) Immunological Reviews , vol.228 , Issue.1 , pp. 288-311
    • Hermiston, M.L.1    Zikherman, J.2    Zhu, J.W.3
  • 105
    • 0033491912 scopus 로고    scopus 로고
    • Occludin proteolysis and increased permeability in endothelial cells through tyrosine phosphatase inhibition
    • Wachtel M., Frei K., Ehler E., Fontana A., Winterhalter K., Gloor S. M., Occludin proteolysis and increased permeability in endothelial cells through tyrosine phosphatase inhibition Journal of Cell Science 1999 112 23 4347 4356 (Pubitemid 30122026)
    • (1999) Journal of Cell Science , vol.112 , Issue.23 , pp. 4347-4356
    • Wachtel, M.1    Frei, K.2    Ehler, E.3    Fontana, A.4    Winterhalter, K.5    Gloor, S.M.6
  • 106
    • 0037009005 scopus 로고    scopus 로고
    • Protein phosphatase 2A associates with and regulates atypical PKC and the epithelial tight junction complex
    • DOI 10.1083/jcb.200206114
    • Nunbhakdi-Craig V., Machleidt T., Ogris E., Bellotto D., White III C. L., Sontag E., Protein phosphatase 2A associates with and regulates atypical PKC and the epithelial tight junction complex Journal of Cell Biology 2002 158 5 967 978 (Pubitemid 35001086)
    • (2002) Journal of Cell Biology , vol.158 , Issue.5 , pp. 967-978
    • Nunbhakdi-Craig, V.1    Machleidt, T.2    Ogris, E.3    Bellotto, D.4    White Iii, C.L.5    Sontag, E.6
  • 107
    • 77953232964 scopus 로고    scopus 로고
    • Hypoglycosylated E-cadherin promotes the assembly of tight junctions through the recruitment of PP2A to adherens junctions
    • Nita-Lazar M., Rebustini I., Walker J., Kukuruzinska M. A., Hypoglycosylated E-cadherin promotes the assembly of tight junctions through the recruitment of PP2A to adherens junctions Experimental Cell Research 2010 316 11 1871 1884
    • (2010) Experimental Cell Research , vol.316 , Issue.11 , pp. 1871-1884
    • Nita-Lazar, M.1    Rebustini, I.2    Walker, J.3    Kukuruzinska, M.A.4
  • 108
    • 33644989149 scopus 로고    scopus 로고
    • ErbB1 functions as a sensor of airway epithelial integrity by regulation of protein phosphatase 2A activity
    • Vermeer P. D., Panko L., Welsh M. J., Zabner J., ErbB1 functions as a sensor of airway epithelial integrity by regulation of protein phosphatase 2A activity Journal of Biological Chemistry 2006 281 3 1725 1730
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.3 , pp. 1725-1730
    • Vermeer, P.D.1    Panko, L.2    Welsh, M.J.3    Zabner, J.4
  • 109
    • 0037456842 scopus 로고    scopus 로고
    • Segregation of receptor and ligand regulates activation of epithelial growth factor receptor
    • DOI 10.1038/nature01440
    • Vermeer P. D., Einwalter L. A., Moninger T. O., Rokhlina T., Kern J. A., Zabner J., Welsh M. J., Segregation of receptor and ligand regulates activation of epithelial growth factor receptor Nature 2003 422 6929 322 326 (Pubitemid 36378360)
    • (2003) Nature , vol.422 , Issue.6929 , pp. 322-326
    • Vermeer, P.D.1    Einwalter, L.A.2    Moninger, T.O.3    Rokhlina, T.4    Kern, J.A.5    Zabner, J.6    Welsh, M.J.7
  • 110
    • 34249668828 scopus 로고    scopus 로고
    • Protein phosphatases 2A and 1 interact with occludin and negatively regulate the assembly of tight junctions in the CACO-2 cell monolayer
    • DOI 10.1074/jbc.M610597200
    • Seth A., Sheth P., Elias B. C., Rao R., Protein phosphatases 2A and 1 interact with occludin and negatively regulate the assembly of tight junctions in the CACO-2 cell monolayer Journal of Biological Chemistry 2007 282 15 11487 11498 (Pubitemid 47100808)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.15 , pp. 11487-11498
    • Seth, A.1    Sheth, P.2    Elias, B.C.3    Rao, R.4
  • 111
    • 0033853899 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli dephosphorylates and dissociates occludin from intestinal epithelial tight junctions
    • DOI 10.1046/j.1462-5822.2000.00055.x
    • Simonovic I., Rosenberg J., Koutsouris A., Hecht G., Enteropathogenic Escherichia coli dephosphorylates and dissociates occludin from intestinal epithelial tight junctions Cellular Microbiology 2000 2 4 305 315 (Pubitemid 30612940)
    • (2000) Cellular Microbiology , vol.2 , Issue.4 , pp. 305-315
    • Simonovic, I.1    Rosenberg, J.2    Koutsouris, A.3    Hecht, G.4
  • 112
    • 67649344470 scopus 로고    scopus 로고
    • Density-enhanced phosphatase 1 regulates phosphorylation of tight junction proteins and enhances barrier function of epithelial cells
    • Sallee J. L., Burridge K., Density-enhanced phosphatase 1 regulates phosphorylation of tight junction proteins and enhances barrier function of epithelial cells Journal of Biological Chemistry 2009 284 22 14997 15006
    • (2009) Journal of Biological Chemistry , vol.284 , Issue.22 , pp. 14997-15006
    • Sallee, J.L.1    Burridge, K.2
  • 114
    • 79955775557 scopus 로고    scopus 로고
    • AMP-activated protein kinase (AMPK) activation and glycogen synthase kinase-3 (GSK-3 ) inhibition induce Ca 2+ -independent deposition of tight junction components at the plasma membrane
    • Zhang L., Jouret F., Rinehart J., Sfakianos J., Mellman I., Lifton R. P., Young L. H., Caplan M. J., AMP-activated protein kinase (AMPK) activation and glycogen synthase kinase-3 (GSK-3 ) inhibition induce Ca 2+ -independent deposition of tight junction components at the plasma membrane Journal of Biological Chemistry 2011 286 19 16879 16890
    • (2011) Journal of Biological Chemistry , vol.286 , Issue.19 , pp. 16879-16890
    • Zhang, L.1    Jouret, F.2    Rinehart, J.3    Sfakianos, J.4    Mellman, I.5    Lifton, R.P.6    Young, L.H.7    Caplan, M.J.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.