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Volumn 16, Issue 12, 2005, Pages 5686-5698

Zonula occludens-1 alters connexin43 gap junction size and organization by influencing channel accretion

Author keywords

[No Author keywords available]

Indexed keywords

CONNEXIN 43; PROTEIN INHIBITOR; PROTEIN ZO1;

EID: 28644434657     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E05-08-0737     Document Type: Article
Times cited : (314)

References (69)
  • 1
    • 0030113804 scopus 로고    scopus 로고
    • Cell signalling: MAGUK magic
    • Anderson, J. M. (1996). Cell signalling: MAGUK magic. Curr. Biol. 6, 382-384.
    • (1996) Curr. Biol. , vol.6 , pp. 382-384
    • Anderson, J.M.1
  • 2
    • 0037155043 scopus 로고    scopus 로고
    • Increased association of ZO-1 with connexin43 during remodeling of cardiac gap junctions
    • Barker, R. J., Price, R. L., and Gourdie, R. G. (2002). Increased association of ZO-1 with connexin43 during remodeling of cardiac gap junctions. Circ. Res. 90, 317-324.
    • (2002) Circ. Res. , vol.90 , pp. 317-324
    • Barker, R.J.1    Price, R.L.2    Gourdie, R.G.3
  • 3
    • 0032555956 scopus 로고    scopus 로고
    • Rapid turnover of connexin43 in the adult rat heart
    • Beardslee, M. A., Laing, J. G., Beyer, E. C., and Saffitz, J. E. (1998). Rapid turnover of connexin43 in the adult rat heart. Circ. Res. 83, 629-635.
    • (1998) Circ. Res. , vol.83 , pp. 629-635
    • Beardslee, M.A.1    Laing, J.G.2    Beyer, E.C.3    Saffitz, J.E.4
  • 4
  • 6
    • 0034801820 scopus 로고    scopus 로고
    • Disruption of gap junctional intercellular communication by lindane is associated with aberrant localization of connexin43 and zonula occludens-1 in 42GPA9 Sertoli cells
    • Defamie, N., Mograbi, B., Roger, C., Cronier, L., Malassine, A., Brucker-Davis, F., Fenichel, P., Segretain, D., and Pointis, G. (2001). Disruption of gap junctional intercellular communication by lindane is associated with aberrant localization of connexin43 and zonula occludens-1 in 42GPA9 Sertoli cells. Carcinogenesis 22, 1537-1542.
    • (2001) Carcinogenesis , vol.22 , pp. 1537-1542
    • Defamie, N.1    Mograbi, B.2    Roger, C.3    Cronier, L.4    Malassine, A.5    Brucker-Davis, F.6    Fenichel, P.7    Segretain, D.8    Pointis, G.9
  • 9
    • 0035991948 scopus 로고    scopus 로고
    • Gap junctions: Structure and function
    • Evans, W. H., and Martin, P. E. (2002). Gap junctions: structure and function (Review). Mol. Membr. Biol. 19, 121-136.
    • (2002) Mol. Membr. Biol. , vol.19 , pp. 121-136
    • Evans, W.H.1    Martin, P.E.2
  • 10
    • 0031001091 scopus 로고    scopus 로고
    • Cell-free synthesis and assembly of connexins into functional gap junction membrane channels
    • Falk, M. M., Buehler, L. K., Kumar, N. M., and Gilula, N. B. (1997). Cell-free synthesis and assembly of connexins into functional gap junction membrane channels. EMBO J. 16, 2703-2716.
    • (1997) EMBO J. , vol.16 , pp. 2703-2716
    • Falk, M.M.1    Buehler, L.K.2    Kumar, N.M.3    Gilula, N.B.4
  • 11
    • 0019603292 scopus 로고
    • Five-hour half-life of mouse liver gap-junction protein
    • Fallon, R. F., and Goodenough, D. A. (1981). Five-hour half-life of mouse liver gap-junction protein. J. Cell Biol. 90, 521-526.
    • (1981) J. Cell Biol. , vol.90 , pp. 521-526
    • Fallon, R.F.1    Goodenough, D.A.2
  • 13
    • 0036498359 scopus 로고    scopus 로고
    • Upregulation in astrocytic connexin 43 gap junction levels may exacerbate generalized seizures in mesial temporal lobe epilepsy
    • Fonseca, C. G., Green, C. R., and Nicholson, L. F. (2002). Upregulation in astrocytic connexin 43 gap junction levels may exacerbate generalized seizures in mesial temporal lobe epilepsy. Brain Res. 929, 105-116.
    • (2002) Brain Res. , vol.929 , pp. 105-116
    • Fonseca, C.G.1    Green, C.R.2    Nicholson, L.F.3
  • 15
    • 1942503184 scopus 로고    scopus 로고
    • Gap junctions and connexin-interacting proteins
    • Giepmans, B. N. (2004). Gap junctions and connexin-interacting proteins. Cardiovasc. Res. 62, 233-245.
    • (2004) Cardiovasc. Res. , vol.62 , pp. 233-245
    • Giepmans, B.N.1
  • 16
    • 0035896527 scopus 로고    scopus 로고
    • Interaction of c-Src with gap junction protein connexin-43. Role in the regulation of cell-cell communication
    • Giepmans, B. N., Hengeveld, T., Postma, F. R., and Moolenaar, W. H. (2001a). Interaction of c-Src with gap junction protein connexin-43. Role in the regulation of cell-cell communication. J. Biol. Chem. 276, 8544-8549.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8544-8549
    • Giepmans, B.N.1    Hengeveld, T.2    Postma, F.R.3    Moolenaar, W.H.4
  • 17
    • 13144252170 scopus 로고    scopus 로고
    • The gap junction protein connexin43 interacts with the second PDZ domain of the zona occludens-1 protein
    • Giepmans, B. N., and Moolenaar, W. H. (1998). The gap junction protein connexin43 interacts with the second PDZ domain of the zona occludens-1 protein. Curr. Biol. 8, 931-934.
    • (1998) Curr. Biol. , vol.8 , pp. 931-934
    • Giepmans, B.N.1    Moolenaar, W.H.2
  • 18
    • 0035754494 scopus 로고    scopus 로고
    • Connexin-43 interactions with ZO-1 and α- and β-tubulin
    • Giepmans, B. N., Verlaan, I., and Moolenaar, W. H. (2001b). Connexin-43 interactions with ZO-1 and α- and β-tubulin. Cell Commun. Adhes. 8, 219-223.
    • (2001) Cell Commun. Adhes. , vol.8 , pp. 219-223
    • Giepmans, B.N.1    Verlaan, I.2    Moolenaar, W.H.3
  • 19
    • 0030013202 scopus 로고    scopus 로고
    • Connexins, connexons, and intercellular communication
    • Goodenough, D. A., Goliger, J. A., and Paul, D. L. (1996). Connexins, connexons, and intercellular communication. Annu. Rev. Biochem. 65, 475-502.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 475-502
    • Goodenough, D.A.1    Goliger, J.A.2    Paul, D.L.3
  • 20
    • 0037382614 scopus 로고    scopus 로고
    • Beyond the gap: Functions of unpaired connexon channels
    • Goodenough, D. A., and Paul, D. L. (2003). Beyond the gap: functions of unpaired connexon channels. Nat. Rev. Mol. Cell. Biol. 4, 285-294.
    • (2003) Nat. Rev. Mol. Cell. Biol. , vol.4 , pp. 285-294
    • Goodenough, D.A.1    Paul, D.L.2
  • 21
    • 0027169427 scopus 로고
    • Validation of immunohistochemical quantification in confocal scanning laser microscopy: A comparative assessment of gap junction size with confocal and ultrastructural techniques
    • Green, C. R., Peters, N. S., Gourdie, R. G., Rothery, S., and Severs, N. J. (1993). Validation of immunohistochemical quantification in confocal scanning laser microscopy: a comparative assessment of gap junction size with confocal and ultrastructural techniques. J. Histochem. Cytochem. 41, 1339-1349.
    • (1993) J. Histochem. Cytochem. , vol.41 , pp. 1339-1349
    • Green, C.R.1    Peters, N.S.2    Gourdie, R.G.3    Rothery, S.4    Severs, N.J.5
  • 22
    • 0029083743 scopus 로고
    • Spatial organization of cardiac gap junctions can affect access resistance
    • Hall, J. E., and Gourdie, R. G. (1995). Spatial organization of cardiac gap junctions can affect access resistance. Microsc. Res. Tech. 31, 446-451.
    • (1995) Microsc. Res. Tech. , vol.31 , pp. 446-451
    • Hall, J.E.1    Gourdie, R.G.2
  • 23
    • 0025949276 scopus 로고
    • Mechanisms of plasma membrane protein degradation: Recycling proteins are degraded more rapidly than those confined to the cell surface
    • Hare, J. F., and Taylor, K. (1991). Mechanisms of plasma membrane protein degradation: recycling proteins are degraded more rapidly than those confined to the cell surface. Proc. Natl. Acad. Sci. USA 88, 5902-5906.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5902-5906
    • Hare, J.F.1    Taylor, K.2
  • 24
    • 0030053566 scopus 로고    scopus 로고
    • N-cadherin in adult rat cardiomyocytes in culture. H. Spatio-temporal appearance of proteins involved in cell-cell contact and communication. Formation of two distinct N-cadherin/catenin complexes
    • Hertig, C. M., Butz, S., Koch, S., Eppenberger-Eberhardt, M., Kemler, R., and Eppenberger, H. M. (1996). N-cadherin in adult rat cardiomyocytes in culture. H. Spatio-temporal appearance of proteins involved in cell-cell contact and communication. Formation of two distinct N-cadherin/catenin complexes. J. Cell Sci. 109, 11-20.
    • (1996) J. Cell Sci. , vol.109 , pp. 11-20
    • Hertig, C.M.1    Butz, S.2    Koch, S.3    Eppenberger-Eberhardt, M.4    Kemler, R.5    Eppenberger, H.M.6
  • 25
    • 0346496133 scopus 로고    scopus 로고
    • Fusion of GFP to the carboxyl terminus of connexin43 increases gap junction size in HeLa cells
    • Hunter, A. W., Jourdan, J., and Gourdie, R. G. (2003). Fusion of GFP to the carboxyl terminus of connexin43 increases gap junction size in HeLa cells. Cell Commun. Adhes. 10, 211-214.
    • (2003) Cell Commun. Adhes. , vol.10 , pp. 211-214
    • Hunter, A.W.1    Jourdan, J.2    Gourdie, R.G.3
  • 26
    • 0030748548 scopus 로고    scopus 로고
    • Involvement of ZO-1 in cadherin-based cell adhesion through its direct binding to a catenin and actin filaments
    • Itoh, M., Nagafuchi, A., Moroi, S., and Tsukita, S. (1997). Involvement of ZO-1 in cadherin-based cell adhesion through its direct binding to a catenin and actin filaments. J. Cell Biol. 138, 181-192.
    • (1997) J. Cell Biol. , vol.138 , pp. 181-192
    • Itoh, M.1    Nagafuchi, A.2    Moroi, S.3    Tsukita, S.4
  • 27
    • 0034097698 scopus 로고    scopus 로고
    • Identification of connexin-interacting proteins: Application of the yeast two-hybrid screen
    • Jin, C., Lau, A. F., and Martyn, K. D. (2000). Identification of connexin-interacting proteins: application of the yeast two-hybrid screen. Methods 20, 219-231.
    • (2000) Methods , vol.20 , pp. 219-231
    • Jin, C.1    Lau, A.F.2    Martyn, K.D.3
  • 29
    • 0033012698 scopus 로고    scopus 로고
    • Trafficking, assembly, and function of a connexin43-green fluorescent protein chimera in live mammalian cells
    • Jordan, K., Solan, J. L., Dominguez, M., Sia, M., Hand, A., Lampe, P. D., and Laird, D. W. (1999). Trafficking, assembly, and function of a connexin43-green fluorescent protein chimera in live mammalian cells. Mol. Biol. Cell 10, 2033-2050.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2033-2050
    • Jordan, K.1    Solan, J.L.2    Dominguez, M.3    Sia, M.4    Hand, A.5    Lampe, P.D.6    Laird, D.W.7
  • 30
    • 0035823043 scopus 로고    scopus 로고
    • Connexin45 directly binds to ZO-1 and localizes to the tight junction region in epithelial MDCK cells
    • Kausalya, P. J., Reichert, M., and Hunziker, W. (2001). Connexin45 directly binds to ZO-1 and localizes to the tight junction region in epithelial MDCK cells. FEBS Lett. 505, 92-96.
    • (2001) FEBS Lett. , vol.505 , pp. 92-96
    • Kausalya, P.J.1    Reichert, M.2    Hunziker, W.3
  • 31
    • 21044444186 scopus 로고    scopus 로고
    • ZO-1 alters the plasma membrane localization and function of Cx43 in osteoblastic cells
    • Laing, J. G., Chou, B. C., and Steinberg, T. H. (2005). ZO-1 alters the plasma membrane localization and function of Cx43 in osteoblastic cells. J. Cell Sci. 118, 2167-2176.
    • (2005) J. Cell Sci. , vol.118 , pp. 2167-2176
    • Laing, J.G.1    Chou, B.C.2    Steinberg, T.H.3
  • 32
    • 0035933764 scopus 로고    scopus 로고
    • Connexin45 interacts with zonula occludens-1 and connexin43 in osteoblastic cells
    • Laing, J. G., Manley-Markowski, R. N., Koval, M., Civitelli, R., and Steinberg, T. H. (2001). Connexin45 interacts with zonula occludens-1 and connexin43 in osteoblastic cells. J. Biol. Chem, 276, 23051-23055.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23051-23055
    • Laing, J.G.1    Manley-Markowski, R.N.2    Koval, M.3    Civitelli, R.4    Steinberg, T.H.5
  • 33
    • 0029176855 scopus 로고
    • Gap junction turnover, intracellular trafficking, and phosphorylation of connexin43 in brefeldin A-treated rat mammary tumor cells
    • Laird, D. W., Castillo, M., and Kasprzak, L. (1995). Gap junction turnover, intracellular trafficking, and phosphorylation of connexin43 in brefeldin A-treated rat mammary tumor cells. J. Cell Biol. 131, 1193-1203.
    • (1995) J. Cell Biol. , vol.131 , pp. 1193-1203
    • Laird, D.W.1    Castillo, M.2    Kasprzak, L.3
  • 34
    • 0035229297 scopus 로고    scopus 로고
    • Expression and imaging of connexin-GFP chimeras in live mammalian cells
    • Laird, D. W., Jordan, K., and Shao, Q. (2001). Expression and imaging of connexin-GFP chimeras in live mammalian cells. Methods Mol. Biol. 154, 135-142.
    • (2001) Methods Mol. Biol. , vol.154 , pp. 135-142
    • Laird, D.W.1    Jordan, K.2    Shao, Q.3
  • 35
    • 0026025267 scopus 로고
    • Turnover and phosphorylation dynamics of connexin43 gap junction protein in cultured cardiac myocytes
    • Laird, D. W., Puranam, K. L., and Revel, J. P. (1991). Turnover and phosphorylation dynamics of connexin43 gap junction protein in cultured cardiac myocytes. Biochem. J. 273, 67-72.
    • (1991) Biochem. J. , vol.273 , pp. 67-72
    • Laird, D.W.1    Puranam, K.L.2    Revel, J.P.3
  • 36
    • 0036677449 scopus 로고    scopus 로고
    • Dynamic trafficking and delivery of connexons to the plasma membrane and accretion to gap junctions in living cells
    • Lauf, U., Giepmans, B. N., Lopez, P., Braconnot, S., Chen, S. C., and Falk, M. M. (2002). Dynamic trafficking and delivery of connexons to the plasma membrane and accretion to gap junctions in living cells. Proc. Natl. Acad. Sci. USA 99, 10446-10451.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10446-10451
    • Lauf, U.1    Giepmans, B.N.2    Lopez, P.3    Braconnot, S.4    Chen, S.C.5    Falk, M.M.6
  • 37
    • 0035370120 scopus 로고    scopus 로고
    • Expression of fluorescently tagged connexins: A novel approach to rescue function of oligomeric DsRed-tagged proteins
    • Lauf, U., Lopez, P., and Falk, M. M. (2001). Expression of fluorescently tagged connexins: a novel approach to rescue function of oligomeric DsRed-tagged proteins. FEBS Lett. 498, 11-15.
    • (2001) FEBS Lett. , vol.498 , pp. 11-15
    • Lauf, U.1    Lopez, P.2    Falk, M.M.3
  • 38
    • 2342567031 scopus 로고    scopus 로고
    • Neuronal connexin36 association with zonula occludens-1 protein (ZO-I) in mouse brain and interaction with the first PDZ domain of ZO-1
    • Li, X., Olson, C., Lu, S., Kamasawa, N., Yasumura, T., Rash, J. E., and Nagy, J. I. (2004). Neuronal connexin36 association with zonula occludens-1 protein (ZO-I) in mouse brain and interaction with the first PDZ domain of ZO-1. Eur. J. Neurosci. 39, 2132-2146.
    • (2004) Eur. J. Neurosci. , vol.39 , pp. 2132-2146
    • Li, X.1    Olson, C.2    Lu, S.3    Kamasawa, N.4    Yasumura, T.5    Rash, J.E.6    Nagy, J.I.7
  • 40
    • 0027172696 scopus 로고
    • A structural basis for the unequal sensitivity of the major cardiac and liver gap junctions to intracellular acidification: The carboxyl tail length
    • Liu, S., Taffet, S., Stoner, L., Delmar, M., Vallano, M. L., and Jalife, J. (1993). A structural basis for the unequal sensitivity of the major cardiac and liver gap junctions to intracellular acidification: the carboxyl tail length. Biophys. J. 64, 1422-1433.
    • (1993) Biophys. J. , vol.64 , pp. 1422-1433
    • Liu, S.1    Taffet, S.2    Stoner, L.3    Delmar, M.4    Vallano, M.L.5    Jalife, J.6
  • 42
    • 20444387943 scopus 로고    scopus 로고
    • Defining a minimal motif required to prevent connexin oligomerization in the endoplasmic reticulum
    • Maza, J., Das Sarma, J., and Koval, M. (2005). Defining a minimal motif required to prevent connexin oligomerization in the endoplasmic reticulum. J. Biol. Chem. 280, 21115-21121.
    • (2005) J. Biol. Chem. , vol.280 , pp. 21115-21121
    • Maza, J.1    Das Sarma, J.2    Koval, M.3
  • 43
    • 0026671599 scopus 로고
    • Inhibition of gap junction and adherens junction assembly by connexin and A-CAM antibodies
    • Meyer, R. A., Laird, D. W., Revel, J. P., and Johnson, R. G. (1992). Inhibition of gap junction and adherens junction assembly by connexin and A-CAM antibodies. J. Cell Biol. 119, 179-189.
    • (1992) J. Cell Biol. , vol.119 , pp. 179-189
    • Meyer, R.A.1    Laird, D.W.2    Revel, J.P.3    Johnson, R.G.4
  • 44
    • 0025155347 scopus 로고
    • Differential phosphorylation of the gap junction protein connexin43 in junctional communication-competent and -deficient cell lines
    • Musil, L. S., Cunningham, B. A., Edelman, G. M., and Goodenough, D. A. (1990). Differential phosphorylation of the gap junction protein connexin43 in junctional communication-competent and -deficient cell lines. J. Cell Biol. 111, 2077-2088.
    • (1990) J. Cell Biol. , vol.111 , pp. 2077-2088
    • Musil, L.S.1    Cunningham, B.A.2    Edelman, G.M.3    Goodenough, D.A.4
  • 45
    • 0025789648 scopus 로고
    • Biochemical analysis of connexin43 intracellular transport, phosphorylation, and assembly into gap junctional plaques
    • Musil, L. S., and Goodenough, D. A. (1991). Biochemical analysis of connexin43 intracellular transport, phosphorylation, and assembly into gap junctional plaques. J. Cell Biol. 115, 1357-1374.
    • (1991) J. Cell Biol. , vol.115 , pp. 1357-1374
    • Musil, L.S.1    Goodenough, D.A.2
  • 46
    • 0027364529 scopus 로고
    • Multisubunit assembly of an integral plasma membrane channel protein, gap junction connexin43, occurs after exit from the ER
    • Musil, L. S., and Goodenough, D. A. (1993). Multisubunit assembly of an integral plasma membrane channel protein, gap junction connexin43, occurs after exit from the ER. Cell 74, 1065-1077.
    • (1993) Cell , vol.74 , pp. 1065-1077
    • Musil, L.S.1    Goodenough, D.A.2
  • 47
    • 0034682799 scopus 로고    scopus 로고
    • Regulation of connexin degradation as a mechanism to increase gap junction assembly and function
    • Musil, L. S., Le, A. C., VanSlyke, J. K., and Roberts, L. M. (2000). Regulation of connexin degradation as a mechanism to increase gap junction assembly and function. J. Biol. Chem. 275, 25207-25215.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25207-25215
    • Musil, L.S.1    Le, A.C.2    VanSlyke, J.K.3    Roberts, L.M.4
  • 49
    • 0037064004 scopus 로고    scopus 로고
    • Molecular cloning, functional expression, and tissue distribution of a novel human gap junction-forming protein, connexin-31.9. Interaction with zona occludens protein-1
    • Nielsen, P. A., Beahm, D. L., Giepmans, B. N., Baruch, A., Hall, J. E., and Kumar, N. M. (2002). Molecular cloning, functional expression, and tissue distribution of a novel human gap junction-forming protein, connexin-31.9. Interaction with zona occludens protein-1. J. Biol. Chem. 277, 38272-38283.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38272-38283
    • Nielsen, P.A.1    Beahm, D.L.2    Giepmans, B.N.3    Baruch, A.4    Hall, J.E.5    Kumar, N.M.6
  • 50
    • 0034030506 scopus 로고    scopus 로고
    • Truncation mutants of the tight junction protein ZO-1 disrupt comeal epithelial cell morphology
    • Ryeom, S. W., Paul, D., and Goodenough, D. A. (2000). Truncation mutants of the tight junction protein ZO-1 disrupt comeal epithelial cell morphology. Mol. Biol. Cell 11, 1687-1696.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1687-1696
    • Ryeom, S.W.1    Paul, D.2    Goodenough, D.A.3
  • 51
    • 17344390158 scopus 로고    scopus 로고
    • Plasma membrane channels formed by connexins: Their regulation and functions
    • Saez, J. C., Berthoud, V. M., Branes, M. C., Martinez, A. D., and Beyer, E. C. (2003). Plasma membrane channels formed by connexins: their regulation and functions. Physiol. Rev. 83, 1359-1400.
    • (2003) Physiol. Rev. , vol.83 , pp. 1359-1400
    • Saez, J.C.1    Berthoud, V.M.2    Branes, M.C.3    Martinez, A.D.4    Beyer, E.C.5
  • 52
    • 0037036426 scopus 로고    scopus 로고
    • Targeted gap junction protein constructs reveal connexin-specific differences in oligomerization
    • Sarma, J. D., Wang, F., and Koval, M. (2002). Targeted gap junction protein constructs reveal connexin-specific differences in oligomerization. J. Biol. Chem. 277, 20911-20918.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20911-20918
    • Sarma, J.D.1    Wang, F.2    Koval, M.3
  • 53
    • 1642407845 scopus 로고    scopus 로고
    • Regulation of connexin biosynthesis, assembly, gap junction formation, and removal
    • Segretain, D., and Falk, M. M. (2004). Regulation of connexin biosynthesis, assembly, gap junction formation, and removal. Biochim. Biophys. Acta 1662, 3-21.
    • (2004) Biochim. Biophys. Acta , vol.1662 , pp. 3-21
    • Segretain, D.1    Falk, M.M.2
  • 54
    • 2942683207 scopus 로고    scopus 로고
    • A proposed role for ZO-1 in targeting connexin 43 gap junctions to the endocytic pathway
    • Segretain, D., Fiorini, C., Decrouy, X., Defamie, N., Prat, J. R., and Pointis, G. (2004). A proposed role for ZO-1 in targeting connexin 43 gap junctions to the endocytic pathway. Biochimie 86, 241-244.
    • (2004) Biochimie , vol.86 , pp. 241-244
    • Segretain, D.1    Fiorini, C.2    Decrouy, X.3    Defamie, N.4    Prat, J.R.5    Pointis, G.6
  • 55
    • 0029801693 scopus 로고    scopus 로고
    • Altered patterns of cardiac intercellular junction distribution in hypertrophic cardiomyopathy
    • Sepp, R., Severs, N. J., and Gourdie, R. G. (1996). Altered patterns of cardiac intercellular junction distribution in hypertrophic cardiomyopathy. Heart 76, 412-417.
    • (1996) Heart , vol.76 , pp. 412-417
    • Sepp, R.1    Severs, N.J.2    Gourdie, R.G.3
  • 57
    • 24044554201 scopus 로고    scopus 로고
    • Connexin 43 interacts with zona occludens-1 and -2 proteins in a cell cycle stage-specific manner
    • Singh, D., Solan, J. L., Taffet, S. M., Javier, R., and Lampe, P. D. (2005). Connexin 43 interacts with zona occludens-1 and -2 proteins in a cell cycle stage-specific manner. J. Biol. Chem. 280, 30416-30421.
    • (2005) J. Biol. Chem. , vol.280 , pp. 30416-30421
    • Singh, D.1    Solan, J.L.2    Taffet, S.M.3    Javier, R.4    Lampe, P.D.5
  • 58
    • 0025941699 scopus 로고
    • Altered patterns of gap junction distribution in ischemic heart disease. An immunohistochemical study of human myocardium using laser scanning confocal microscopy
    • Smith, J. H., Green, C. R., Peters, N. S., Rothery, S., and Severs, N. J. (1991). Altered patterns of gap junction distribution in ischemic heart disease. An immunohistochemical study of human myocardium using laser scanning confocal microscopy. Am. J. Pathol. 139, 801-821.
    • (1991) Am. J. Pathol. , vol.139 , pp. 801-821
    • Smith, J.H.1    Green, C.R.2    Peters, N.S.3    Rothery, S.4    Severs, N.J.5
  • 59
    • 0037672632 scopus 로고    scopus 로고
    • Connexin43 phosphorylation at S368 is acute during S and G2/M and in response to protein kinase C activation
    • Solan, J. L., Fry, M. D., TenBroek, E. M., and Lampe, P. D. (2003). Connexin43 phosphorylation at S368 is acute during S and G2/M and in response to protein kinase C activation. J. Cell Sci. 116, 2203-2211.
    • (2003) J. Cell Sci. , vol.116 , pp. 2203-2211
    • Solan, J.L.1    Fry, M.D.2    Tenbroek, E.M.3    Lampe, P.D.4
  • 60
    • 11144230049 scopus 로고    scopus 로고
    • Structural changes in the carboxyl terminus of the gap junction protein connexin43 indicates signaling between binding domains for c-Src and zonula occludens-1
    • Sorgen, P. L., Duffy, H. S., Sahoo, P., Coombs, W., Delmar, M., and Spray, D. C. (2004). Structural changes in the carboxyl terminus of the gap junction protein connexin43 indicates signaling between binding domains for c-Src and zonula occludens-1. J. Biol. Chem. 279, 54695-54701.
    • (2004) J. Biol. Chem. , vol.279 , pp. 54695-54701
    • Sorgen, P.L.1    Duffy, H.S.2    Sahoo, P.3    Coombs, W.4    Delmar, M.5    Spray, D.C.6
  • 62
    • 0023030826 scopus 로고
    • Identification of ZO-1, a high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia
    • Stevenson, B. R., Siliciano, J. D., Mooseker, M. S., and Goodenough, D. A. (1986). Identification of ZO-1, a high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia. J. Cell Biol. 103, 755-766.
    • (1986) J. Cell Biol. , vol.103 , pp. 755-766
    • Stevenson, B.R.1    Siliciano, J.D.2    Mooseker, M.S.3    Goodenough, D.A.4
  • 63
    • 0035910415 scopus 로고    scopus 로고
    • c-Src regulates the interaction between connexin-43 and ZO-1 in cardiac myocytes
    • Toyofuku, T., Akamatsu, Y., Zhang, H., Kuzuya, T., Tada, M., and Hori, M. (2001). c-Src regulates the interaction between connexin-43 and ZO-1 in cardiac myocytes. J. Biol. Chem. 276, 1780-1788.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1780-1788
    • Toyofuku, T.1    Akamatsu, Y.2    Zhang, H.3    Kuzuya, T.4    Tada, M.5    Hori, M.6
  • 64
    • 0032557460 scopus 로고    scopus 로고
    • Direct association of the gap junction protein connexin-43 with ZO-1 in cardiac myocytes
    • Toyofuku, T., Yabuki, M., Otsu, K., Kuzuya, T., Hori, M., and Tada, M. (1998). Direct association of the gap junction protein connexin-43 with ZO-1 in cardiac myocytes. J. Biol. Chem. 273, 12725-12731.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12725-12731
    • Toyofuku, T.1    Yabuki, M.2    Otsu, K.3    Kuzuya, T.4    Hori, M.5    Tada, M.6
  • 65
    • 7244219999 scopus 로고    scopus 로고
    • Establishment and characterization of cultured epithelial cells lacking expression of ZO-1
    • Umeda, K., Matsui, T., Nakayama, M., Furuse, K., Sasaki, H., Furuse, M., and Tsukita, S. (2004). Establishment and characterization of cultured epithelial cells lacking expression of ZO-1. J. Biol. Chem. 279, 44785-44794.
    • (2004) J. Biol. Chem. , vol.279 , pp. 44785-44794
    • Umeda, K.1    Matsui, T.2    Nakayama, M.3    Furuse, K.4    Sasaki, H.5    Furuse, M.6    Tsukita, S.7
  • 66
    • 0034106939 scopus 로고    scopus 로고
    • Analysis of connexin intracellular transport and assembly
    • VanSlyke, J. K., and Musil, L. S. (2000). Analysis of connexin intracellular transport and assembly. Methods 20, 156-164.
    • (2000) Methods , vol.20 , pp. 156-164
    • VanSlyke, J.K.1    Musil, L.S.2
  • 67
    • 21244490447 scopus 로고    scopus 로고
    • Connexin43 associated with an N-cadherin-containing multiprotein complex is required for gap junction formation in NIH3T3 cells
    • Wei, C. J., Francis, R., Xu, X., and Lo, C. W. (2005). Connexin43 associated with an N-cadherin-containing multiprotein complex is required for gap junction formation in NIH3T3 cells. J. Biol. Chem. 280, 19925-19936.
    • (2005) J. Biol. Chem. , vol.280 , pp. 19925-19936
    • Wei, C.J.1    Francis, R.2    Xu, X.3    Lo, C.W.4
  • 69
    • 21044440344 scopus 로고    scopus 로고
    • Quantitative analysis of ZO-1 colocalization with Cx43 gap junction plaques in cultures of rat neonatal cardiomyocytes
    • Zhu, C., Barker, R. J., Hunter, A. W., Zhang, Y., Jourdan, J., and Gourdie, R. G. (2005). Quantitative analysis of ZO-1 colocalization with Cx43 gap junction plaques in cultures of rat neonatal cardiomyocytes. Microsc. Microanal. 11, 244-248.
    • (2005) Microsc. Microanal. , vol.11 , pp. 244-248
    • Zhu, C.1    Barker, R.J.2    Hunter, A.W.3    Zhang, Y.4    Jourdan, J.5    Gourdie, R.G.6


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