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Volumn 1662, Issue 1-2, 2004, Pages 22-41

Diversity in protein-protein interactions of connexins: Emerging roles

Author keywords

Channel assembly; Channel gating; Gap junction; Intracellular trafficking

Indexed keywords

CALMODULIN; CLAUDIN; CYTOSKELETON PROTEIN; GAP JUNCTION PROTEIN; OCCLUDIN; PROTEIN KINASE C; PROTEIN SUBUNIT; PROTEIN TYROSINE KINASE;

EID: 1642312139     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2003.10.022     Document Type: Review
Times cited : (128)

References (150)
  • 1
    • 0036556336 scopus 로고    scopus 로고
    • Formation of the gap junction nexus: Binding partners for connexins
    • Duffy H.S., Delmar M., Spray D.C. Formation of the gap junction nexus: binding partners for connexins. J. Physiol. (Paris). 96:2002;243-249.
    • (2002) J. Physiol. (Paris) , vol.96 , pp. 243-249
    • Duffy, H.S.1    Delmar, M.2    Spray, D.C.3
  • 2
    • 0036872332 scopus 로고    scopus 로고
    • Interaction of connexins with protein partners in the control of channel turnover and gating
    • Thomas M.A., Huang S., Cojoka A., Riccio O., Staub O., Suter S., Chanson M. Interaction of connexins with protein partners in the control of channel turnover and gating. Biol. Cell. 94:2002;445-456.
    • (2002) Biol. Cell , vol.94 , pp. 445-456
    • Thomas, M.A.1    Huang, S.2    Cojoka, A.3    Riccio, O.4    Staub, O.5    Suter, S.6    Chanson, M.7
  • 3
    • 0032616958 scopus 로고    scopus 로고
    • Modulation of ion channels by protein phosphorylation - How the brain works
    • Levitan I.B. Modulation of ion channels by protein phosphorylation - how the brain works. Adv. Second Messenger Phosphoprot. Res. 33:1999;3-22.
    • (1999) Adv. Second Messenger Phosphoprot. Res. , vol.33 , pp. 3-22
    • Levitan, I.B.1
  • 5
    • 0035704411 scopus 로고    scopus 로고
    • Emerging issues of connexin channels: Biophysics fills the gap
    • Harris A.L. Emerging issues of connexin channels: biophysics fills the gap. Q. Rev. Biophys. 34:2001;325-472.
    • (2001) Q. Rev. Biophys. , vol.34 , pp. 325-472
    • Harris, A.L.1
  • 6
    • 0028214204 scopus 로고
    • Selective interactions among the multiple connexin proteins expressed in the vertebrate lens: The second extracellular domain is a determinant of compatibility between connexins
    • White T.W., Bruzzone R., Wolfram S., Paul D.L., Goodenough D.A. Selective interactions among the multiple connexin proteins expressed in the vertebrate lens: the second extracellular domain is a determinant of compatibility between connexins. J. Cell Biol. 125:1994;879-892.
    • (1994) J. Cell Biol. , vol.125 , pp. 879-892
    • White, T.W.1    Bruzzone, R.2    Wolfram, S.3    Paul, D.L.4    Goodenough, D.A.5
  • 7
    • 0028230758 scopus 로고
    • Selective interactions among the multiple connexin proteins expressed in the vertebrate lens: The second extracellular domain is a determinant of compatibility between connexins
    • Bruzzone R., White T.W., Paul D.L. Selective interactions among the multiple connexin proteins expressed in the vertebrate lens: the second extracellular domain is a determinant of compatibility between connexins. J. Cell. Sci. 107:1994;955-967.
    • (1994) J. Cell. Sci. , vol.107 , pp. 955-967
    • Bruzzone, R.1    White, T.W.2    Paul, D.L.3
  • 8
    • 0033135290 scopus 로고    scopus 로고
    • Selective inhibition of gap junction channel activity by synthetic peptides
    • Kwak B.R., Jongsma H.J. Selective inhibition of gap junction channel activity by synthetic peptides. J. Physiol. 516:1999;679-685.
    • (1999) J. Physiol. , vol.516 , pp. 679-685
    • Kwak, B.R.1    Jongsma, H.J.2
  • 9
    • 0034826706 scopus 로고    scopus 로고
    • Assembly of gap junction channels: Mechanism, effects of calmodulin antagonists and identification of connexin oligomerization determinants
    • Ahmad S., Martin P.E., Evans W.H. Assembly of gap junction channels: mechanism, effects of calmodulin antagonists and identification of connexin oligomerization determinants. Eur. J. Biochem. 268:2001;4544-4552.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4544-4552
    • Ahmad, S.1    Martin, P.E.2    Evans, W.H.3
  • 10
    • 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., Jalife J. A structural basis for the unequal sensitivity of the major cardiac and liver gap junctions to intracellular acidification: the carboxyl tail length. Biophys. J. 64:1993;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
  • 11
    • 0030050142 scopus 로고    scopus 로고
    • Intramolecular interactions mediate pH regulation of connexin43 channels
    • Morley G.E., Taffet S.M., Delmar M. Intramolecular interactions mediate pH regulation of connexin43 channels. Biophys. J. 70:1996;1294-1302.
    • (1996) Biophys. J. , vol.70 , pp. 1294-1302
    • Morley, G.E.1    Taffet, S.M.2    Delmar, M.3
  • 13
    • 0033535338 scopus 로고    scopus 로고
    • Dissection of the molecular basis of pp60v-src induced gating of connexin 43 gap junction channels
    • Zhou L., Kasperek E.M., Nicholson B.J. Dissection of the molecular basis of pp60v-src induced gating of connexin 43 gap junction channels. J. Cell Biol. 144:1999;1033-1045.
    • (1999) J. Cell Biol. , vol.144 , pp. 1033-1045
    • Zhou, L.1    Kasperek, E.M.2    Nicholson, B.J.3
  • 14
    • 0032838486 scopus 로고    scopus 로고
    • Molecular dissection of transjunctional voltage dependence in the connexin-32 and connexin-43 junctions
    • Revilla A., Castro C., Barrio L.C. Molecular dissection of transjunctional voltage dependence in the connexin-32 and connexin-43 junctions. Biophys. J. 77:1999;1374-1383.
    • (1999) Biophys. J. , vol.77 , pp. 1374-1383
    • Revilla, A.1    Castro, C.2    Barrio, L.C.3
  • 16
    • 0037040828 scopus 로고    scopus 로고
    • Connexin43 and connexin45 form heteromeric gap junction channels in which individual components determine permeability and regulation
    • Moreno A.P., Chanson M., Elenes S., Anumonwo J., Scerri I., Gu H., Taffet S.M., Delmar M. Connexin43 and connexin45 form heteromeric gap junction channels in which individual components determine permeability and regulation. Circ. Res. 90:2002;450-457.
    • (2002) Circ. Res. , vol.90 , pp. 450-457
    • Moreno, A.P.1    Chanson, M.2    Elenes, S.3    Anumonwo, J.4    Scerri, I.5    Gu, H.6    Taffet, S.M.7    Delmar, M.8
  • 18
    • 0025224223 scopus 로고
    • Biophysical and molecular mechanisms of Shaker potassium channel inactivation
    • Hoshi T., Zagotta W.N., Aldrich R.W. Biophysical and molecular mechanisms of Shaker potassium channel inactivation. Science. 250:1990;533-538.
    • (1990) Science , vol.250 , pp. 533-538
    • Hoshi, T.1    Zagotta, W.N.2    Aldrich, R.W.3
  • 20
    • 0035853435 scopus 로고    scopus 로고
    • The carboxyl terminal domain regulates the unitary conductance and voltage dependence of connexin40 gap junction channels
    • Anumonwo J.M., Taffet S.M., Gu H., Chanson M., Moreno A.P., Delmar M. The carboxyl terminal domain regulates the unitary conductance and voltage dependence of connexin40 gap junction channels. Circ. Res. 88:2001;666-673.
    • (2001) Circ. Res. , vol.88 , pp. 666-673
    • Anumonwo, J.M.1    Taffet, S.M.2    Gu, H.3    Chanson, M.4    Moreno, A.P.5    Delmar, M.6
  • 23
    • 0033180348 scopus 로고    scopus 로고
    • Protein modules as organizers of membrane structure
    • Fanning A.S., Anderson J.M. Protein modules as organizers of membrane structure. Curr. Opin. Cell Biol. 11:1999;432-439.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 432-439
    • Fanning, A.S.1    Anderson, J.M.2
  • 24
    • 0036199229 scopus 로고    scopus 로고
    • Calmodulin as an ion channel subunit
    • Saimi Y., Kung C. Calmodulin as an ion channel subunit. Annu. Rev. Physiol. 64:2002;289-311.
    • (2002) Annu. Rev. Physiol. , vol.64 , pp. 289-311
    • Saimi, Y.1    Kung, C.2
  • 25
    • 0021063967 scopus 로고
    • Is calmodulin involved in the regulation of gap junction permeability?
    • Peracchia C., Bernardini G., Peracchia L.L. Is calmodulin involved in the regulation of gap junction permeability? Pflugers Arch. 399:1983;152-154.
    • (1983) Pflugers Arch. , vol.399 , pp. 152-154
    • Peracchia, C.1    Bernardini, G.2    Peracchia, L.L.3
  • 26
    • 0021952348 scopus 로고
    • Interaction of calmodulin and other calcium-modulated proteins with mammalian and arthropod junctional membrane proteins
    • Van Eldik L.J., Hertzberg E.L., Berdan R.C., Gilula N.B. Interaction of calmodulin and other calcium-modulated proteins with mammalian and arthropod junctional membrane proteins. Biochem. Biophys. Res. Commun. 126:1985;825-832.
    • (1985) Biochem. Biophys. Res. Commun. , vol.126 , pp. 825-832
    • Van Eldik, L.J.1    Hertzberg, E.L.2    Berdan, R.C.3    Gilula, N.B.4
  • 27
    • 0030773116 scopus 로고    scopus 로고
    • Connexin 32 of gap junctions contains two cytoplasmic calmodulin-binding domains
    • Török K., Stauffer K., Evans W.H. Connexin 32 of gap junctions contains two cytoplasmic calmodulin-binding domains. Biochem. J. 326:1997;479-483.
    • (1997) Biochem. J. , vol.326 , pp. 479-483
    • Török, K.1    Stauffer, K.2    Evans, W.H.3
  • 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., Hunziker W. Connexin45 directly binds to ZO-1 and localizes to the tight junction region in epithelial MDCK cells. FEBS Lett. 505:2001;92-96.
    • (2001) FEBS Lett. , vol.505 , pp. 92-96
    • Kausalya, P.J.1    Reichert, M.2    Hunziker, W.3
  • 32
    • 0029099913 scopus 로고
    • Gap junctions and cell polarity: Connexin32 and connexin43 expressed in polarized thyroid epithelial cells assemble into separate gap junctions, which are located in distinct regions of the lateral plasma membrane domain
    • Guerrier A., Fonlupt P., Morand I., Rabilloud R., Audebet C., Krutovskikh V., Gros D., Rousset B., Munari-Silem Y. Gap junctions and cell polarity: connexin32 and connexin43 expressed in polarized thyroid epithelial cells assemble into separate gap junctions, which are located in distinct regions of the lateral plasma membrane domain. J. Cell. Sci. 108:1995;2609-2617.
    • (1995) J. Cell. Sci. , vol.108 , pp. 2609-2617
    • Guerrier, A.1    Fonlupt, P.2    Morand, I.3    Rabilloud, R.4    Audebet, C.5    Krutovskikh, V.6    Gros, D.7    Rousset, B.8    Munari-Silem, Y.9
  • 33
    • 0035757722 scopus 로고    scopus 로고
    • Increased co-localization of connexin43 and ZO-1 in dissociated adult myocytes
    • Barker R.J., Price R.L., Gourdie R.G. Increased co-localization of connexin43 and ZO-1 in dissociated adult myocytes. Cell Adhes. Commun. 8:2001;205-208.
    • (2001) Cell Adhes. Commun. , vol.8 , pp. 205-208
    • Barker, R.J.1    Price, R.L.2    Gourdie, R.G.3
  • 34
    • 0037155043 scopus 로고    scopus 로고
    • Increased association of ZO-1 with connexin43 during remodeling of cardiac gap junctions
    • Barker R.J., Price R.L., Gourdie R.G. Increased association of ZO-1 with connexin43 during remodeling of cardiac gap junctions. Circ. Res. 22:2002;317-324.
    • (2002) Circ. Res. , vol.22 , pp. 317-324
    • Barker, R.J.1    Price, R.L.2    Gourdie, R.G.3
  • 35
    • 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., Tada M. Direct association of the gap junction protein connexin 43 with ZO-1 in cardiac myocytes. J. Biol. Chem. 273:1998;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
  • 36
    • 0037371343 scopus 로고    scopus 로고
    • Role of catenins in the development of gap junctions in rat cardiomyocytes
    • Wu J.C., Tsai R.Y., Chung T.H. Role of catenins in the development of gap junctions in rat cardiomyocytes. J. Cell. Biochem. 88:2003;823-835.
    • (2003) J. Cell. Biochem. , vol.88 , pp. 823-835
    • Wu, J.C.1    Tsai, R.Y.2    Chung, T.H.3
  • 37
    • 0031835796 scopus 로고    scopus 로고
    • Endometrial connexin expression in the mare and pig: Evidence for the suppression of cell-cell communication in uterine luminal epithelium
    • Day W.E., Bowen J.A., Barhoumi R., Bazer F.W., Burghardt R.C. Endometrial connexin expression in the mare and pig: evidence for the suppression of cell-cell communication in uterine luminal epithelium. Anat. Rec. 251:1998;277-285.
    • (1998) Anat. Rec. , vol.251 , pp. 277-285
    • Day, W.E.1    Bowen, J.A.2    Barhoumi, R.3    Bazer, F.W.4    Burghardt, R.C.5
  • 39
    • 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., Pointis G. Disruption of gap junctional intercellular communication by lindane is associated with aberrant localization of connexin43 and zonula occludens-1 in 42GPA9 Sertoli cells. Carcinogenesis. 22:2001;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
  • 40
    • 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., Moolenaar W.H. The gap junction protein connexin43 interacts with the second PDZ domain of the zona occludens-1 protein. Curr. Biol. 8:1998;931-934.
    • (1998) Curr. Biol. , vol.8 , pp. 931-934
    • Giepmans, B.N.1    Moolenaar, W.H.2
  • 41
    • 0028533264 scopus 로고
    • Localization and distribution of gap junctions in normal and cardiomyopathic hamster heart
    • Luque E.A., Veenstra R.D., Beyer E.C., Lemanski L.F. Localization and distribution of gap junctions in normal and cardiomyopathic hamster heart. J. Morphol. 222:1994;203-213.
    • (1994) J. Morphol. , vol.222 , pp. 203-213
    • Luque, E.A.1    Veenstra, R.D.2    Beyer, E.C.3    Lemanski, L.F.4
  • 42
    • 0033569865 scopus 로고    scopus 로고
    • C-Src regulates the interaction between connexin-43 and ZO-1 in cardiac myocytes
    • Toyofuku T., Yabuki M., Otsu K., Kuzuya T., Tada M., Hori M. c-Src regulates the interaction between connexin-43 and ZO-1 in cardiac myocytes. Circ. Res. 85:1999;672-681.
    • (1999) Circ. Res. , vol.85 , pp. 672-681
    • Toyofuku, T.1    Yabuki, M.2    Otsu, K.3    Kuzuya, T.4    Tada, M.5    Hori, M.6
  • 43
    • 0030604722 scopus 로고    scopus 로고
    • Crystal structures of a complexed and peptide-free membrane protein-binding domain: Molecular basis of peptide recognition by PDZ
    • Doyle D.A., Lee A., Lewis J., Kim E., Sheng M., MacKinnon R. Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. Cell. 85:1996;1067-1076.
    • (1996) Cell , vol.85 , pp. 1067-1076
    • Doyle, D.A.1    Lee, A.2    Lewis, J.3    Kim, E.4    Sheng, M.5    MacKinnon, R.6
  • 44
    • 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., Hori M. c-Src regulates the interaction between connexin-43 and ZO-1 in cardiac myocytes. J. Biol. Chem. 276:2001;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
  • 46
    • 0036343899 scopus 로고    scopus 로고
    • Cx32 formation and/or Cx32-mediated intercellular communication induces expression and function of tight junctions in hepatocytic cell line
    • Kojima T., Spray D.C., Kokai Y., Chiba H., Mochizuki Y., Sawada N. Cx32 formation and/or Cx32-mediated intercellular communication induces expression and function of tight junctions in hepatocytic cell line. Exp. Cell Res. 276:2002;40-51.
    • (2002) Exp. Cell Res. , vol.276 , pp. 40-51
    • Kojima, T.1    Spray, D.C.2    Kokai, Y.3    Chiba, H.4    Mochizuki, Y.5    Sawada, N.6
  • 47
    • 0035864383 scopus 로고    scopus 로고
    • Cx32 but not Cx26 is associated with tight junctions in primary cultures of rat hepatocytes
    • Kojima T., Kokai Y., Chiba H., Yamamoto M., Mochizuki Y., Sawada N. Cx32 but not Cx26 is associated with tight junctions in primary cultures of rat hepatocytes. Exp. Cell Res. 263:2001;193-201.
    • (2001) Exp. Cell Res. , vol.263 , pp. 193-201
    • Kojima, T.1    Kokai, Y.2    Chiba, H.3    Yamamoto, M.4    Mochizuki, Y.5    Sawada, N.6
  • 48
    • 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., Kumar N.M. 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. 277:2002;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
  • 49
    • 0035750745 scopus 로고    scopus 로고
    • Characterization of the association of connexins and ZO-1 in the lens
    • Nielsen P.A., Baruch A., Giepmans B.N., Kumar N.M. Characterization of the association of connexins and ZO-1 in the lens. Cell Adhes. Commun. 8:2001;213-217.
    • (2001) Cell Adhes. Commun. , vol.8 , pp. 213-217
    • Nielsen, P.A.1    Baruch, A.2    Giepmans, B.N.3    Kumar, N.M.4
  • 51
    • 0033023747 scopus 로고    scopus 로고
    • Differential expression of gap junction proteins connexin26, 32, and 43 in normal and crush-injured rat sciatic nerves. Close relationship between connexin43 and occludin in the perineurium
    • Nagaoka T., Oyamada M., Okajima S., Takamatsu T. Differential expression of gap junction proteins connexin26, 32, and 43 in normal and crush-injured rat sciatic nerves. Close relationship between connexin43 and occludin in the perineurium. J. Histochem. Cytochem. 47:1999;937-948.
    • (1999) J. Histochem. Cytochem. , vol.47 , pp. 937-948
    • Nagaoka, T.1    Oyamada, M.2    Okajima, S.3    Takamatsu, T.4
  • 52
    • 0034703027 scopus 로고    scopus 로고
    • The coiled-coil domain of occludin can act to organize structural and functional elements of the epithelial tight junction
    • 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. J. Biol. Chem. 275:2000;29816-29822.
    • (2000) J. Biol. Chem. , vol.275 , 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
  • 55
    • 0031018236 scopus 로고    scopus 로고
    • Dynamics of connexins, E-cadherin and alpha-catenin on cell membranes during gap junction formation
    • Fujimoto K., Nagafuchi A., Tsukita S., Kuraoka A., Ohokuma A., Shibata Y.J. Dynamics of connexins, E-cadherin and alpha-catenin on cell membranes during gap junction formation. J. Cell. Sci. 110:1997;311-322.
    • (1997) J. Cell. Sci. , vol.110 , pp. 311-322
    • Fujimoto, K.1    Nagafuchi, A.2    Tsukita, S.3    Kuraoka, A.4    Ohokuma, A.5    Shibata, Y.J.6
  • 56
    • 0035479827 scopus 로고    scopus 로고
    • Molecular architecture of adherens junctions
    • Nagafuchi A. Molecular architecture of adherens junctions. Curr. Opin. Cell Biol. 13:2001;600-603.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 600-603
    • Nagafuchi, A.1
  • 58
    • 0037348756 scopus 로고    scopus 로고
    • The organization of adherens junctions and desmosomes at the cardiac intercalated disc is independent of gap junctions
    • Gutstein D.E., Liu F.Y., Meyers M.B., Choo A., Fishman G.I. The organization of adherens junctions and desmosomes at the cardiac intercalated disc is independent of gap junctions. J. Cell. Sci. 116:2003;875-885.
    • (2003) J. Cell. Sci. , vol.116 , pp. 875-885
    • Gutstein, D.E.1    Liu, F.Y.2    Meyers, M.B.3    Choo, A.4    Fishman, G.I.5
  • 59
    • 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., Johnson R.G. Inhibition of gap junction and adherens junction assembly by connexin and A-CAM antibodies. J. Cell Biol. 119:1992;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
  • 60
    • 0033597942 scopus 로고    scopus 로고
    • Spatiotemporal development and distribution of intercellular junctions in adult rat cardiomyocytes in culture
    • Kostin S., Hein S., Bauer E.P., Schaper J. Spatiotemporal development and distribution of intercellular junctions in adult rat cardiomyocytes in culture. Circ. Res. 85:1999;154-167.
    • (1999) Circ. Res. , vol.85 , pp. 154-167
    • Kostin, S.1    Hein, S.2    Bauer, E.P.3    Schaper, J.4
  • 62
    • 0035498831 scopus 로고    scopus 로고
    • Control of intracellular movement of connexins by E-cadherin in murine skin papilloma cells
    • Hernandez-Blazquez F.J., Joazeiro P.P., Omori Y., Yamasaki H. Control of intracellular movement of connexins by E-cadherin in murine skin papilloma cells. Exp. Cell Res. 270:2001;235-247.
    • (2001) Exp. Cell Res. , vol.270 , pp. 235-247
    • Hernandez-Blazquez, F.J.1    Joazeiro, P.P.2    Omori, Y.3    Yamasaki, H.4
  • 63
    • 27244462402 scopus 로고
    • Tyrosine phosphorylation of the gap junction protein connexin43 is required for the pp60v-src-induced inhibition of communication
    • Swenson K.I., Piwnica-Worms H., McNamee H., Paul D.L. Tyrosine phosphorylation of the gap junction protein connexin43 is required for the pp60v-src-induced inhibition of communication. Cell Regul. 1:1990;989-1002.
    • (1990) Cell Regul. , vol.1 , pp. 989-1002
    • Swenson, K.I.1    Piwnica-Worms, H.2    McNamee, H.3    Paul, D.L.4
  • 64
    • 0032588111 scopus 로고    scopus 로고
    • In vivo association of pp60v-src and the gap-junction protein connexin 43 in v-src-transformed fibroblasts
    • Loo L.W., Kanemitsu M.Y., Lau A.F. In vivo association of pp60v-src and the gap-junction protein connexin 43 in v-src-transformed fibroblasts. Mol. Carcinog. 25:1999;187-195.
    • (1999) Mol. Carcinog. , vol.25 , pp. 187-195
    • Loo, L.W.1    Kanemitsu, M.Y.2    Lau, A.F.3
  • 65
    • 1642321958 scopus 로고    scopus 로고
    • Regulation of gap junctions by tyrosine protein kinases
    • (this issue)
    • Warn-Cramer B.J., Lau A.F. Regulation of gap junctions by tyrosine protein kinases. Biochim. Biophys. Acta. 2004;. (this issue).
    • (2004) Biochim. Biophys. Acta
    • Warn-Cramer, B.J.1    Lau, A.F.2
  • 66
    • 0030883743 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of connexin 43 by v-Src is mediated by SH2 and SH3 domain interactions
    • Kanemitsu M.Y., Loo L.W., Simon S., Lau A.F., Eckhart W. Tyrosine phosphorylation of connexin 43 by v-Src is mediated by SH2 and SH3 domain interactions. J. Biol. Chem. 272:1997;22824-22831.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22824-22831
    • Kanemitsu, M.Y.1    Loo, L.W.2    Simon, S.3    Lau, A.F.4    Eckhart, W.5
  • 67
    • 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., Moolenaar W.H. Interaction of c-Src with gap junction protein connexin-43. Role in the regulation of cell-cell communication. J. Biol. Chem. 276:2001;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
  • 68
    • 0033621884 scopus 로고    scopus 로고
    • The epsilon subtype of protein kinase C is required for cardiomyocyte connexin-43 phosphorylation
    • Doble B.W., Ping P., Kardami E. The epsilon subtype of protein kinase C is required for cardiomyocyte connexin-43 phosphorylation. Circ. Res. 86:2000;293-301.
    • (2000) Circ. Res. , vol.86 , pp. 293-301
    • Doble, B.W.1    Ping, P.2    Kardami, E.3
  • 70
    • 0037590100 scopus 로고    scopus 로고
    • Ischemic preconditioning preserves connexin 43 phosphorylation during sustained ischemia in pig hearts in vivo
    • Schulz R., Gres P., Skyschally A., Duschin A., Belosjorow S., Konietzka I., Heusch G. Ischemic preconditioning preserves connexin 43 phosphorylation during sustained ischemia in pig hearts in vivo. FASEB J. 17:2003;1355-1357.
    • (2003) FASEB J. , vol.17 , pp. 1355-1357
    • Schulz, R.1    Gres, P.2    Skyschally, A.3    Duschin, A.4    Belosjorow, S.5    Konietzka, I.6    Heusch, G.7
  • 71
    • 0037160066 scopus 로고    scopus 로고
    • Casein kinase 1 regulates connexin-43 gap junction assembly
    • Cooper C.D., Lampe P.D. Casein kinase 1 regulates connexin-43 gap junction assembly. J. Biol. Chem. 277:2002;44962-44968.
    • (2002) J. Biol. Chem. , vol.277 , pp. 44962-44968
    • Cooper, C.D.1    Lampe, P.D.2
  • 72
    • 0032992140 scopus 로고    scopus 로고
    • Myotonic dystrophy protein kinase expressed in rat cardiac muscle is associated with sarcoplasmic reticulum and gap junctions
    • Mussini I., Biral D., Marin O., Furlan S., Salvatori S. Myotonic dystrophy protein kinase expressed in rat cardiac muscle is associated with sarcoplasmic reticulum and gap junctions. J. Histochem. Cytochem. 47:1999;383-392.
    • (1999) J. Histochem. Cytochem. , vol.47 , pp. 383-392
    • Mussini, I.1    Biral, D.2    Marin, O.3    Furlan, S.4    Salvatori, S.5
  • 73
    • 0036727092 scopus 로고    scopus 로고
    • Myotonic dystrophy protein kinase of the cardiac muscle: Evaluation using an immunochemical approach
    • Schiavon G., Furlan S., Marin O., Salvatori S. Myotonic dystrophy protein kinase of the cardiac muscle: evaluation using an immunochemical approach. Microsc. Res. Tech. 58:2002;404-411.
    • (2002) Microsc. Res. Tech. , vol.58 , pp. 404-411
    • Schiavon, G.1    Furlan, S.2    Marin, O.3    Salvatori, S.4
  • 76
    • 0035754494 scopus 로고    scopus 로고
    • Connexin-43 interactions with ZO-1 and alpha- and beta-tubulin
    • Giepmans B.N., Verlaan I., Moolenaar W.H. Connexin-43 interactions with ZO-1 and alpha- and beta-tubulin. Cell Commun. Adhes. 8:2001;219-223.
    • (2001) Cell Commun. Adhes. , vol.8 , pp. 219-223
    • Giepmans, B.N.1    Verlaan, I.2    Moolenaar, W.H.3
  • 77
    • 0031214677 scopus 로고    scopus 로고
    • Relationship of cytoskeletal filaments to annular gap junction expression in human adrenal cortical tumor cells in culture
    • Murray S.A., Williams S.Y., Dillard C.Y., Narayanan S.K., McCauley J. Relationship of cytoskeletal filaments to annular gap junction expression in human adrenal cortical tumor cells in culture. Exp. Cell. Res. 234:1997;398-404.
    • (1997) Exp. Cell. Res. , vol.234 , pp. 398-404
    • Murray, S.A.1    Williams, S.Y.2    Dillard, C.Y.3    Narayanan, S.K.4    McCauley, J.5
  • 78
    • 0035754245 scopus 로고    scopus 로고
    • Role of cytoskeletal elements in the recruitment of Cx43-GFP and Cx26-YFP into gap junctions
    • Thomas T., Jordan K., Laird D.W. Role of cytoskeletal elements in the recruitment of Cx43-GFP and Cx26-YFP into gap junctions. Cell Adhes. Commun. 8:2001;231-236.
    • (2001) Cell Adhes. Commun. , vol.8 , pp. 231-236
    • Thomas, T.1    Jordan, K.2    Laird, D.W.3
  • 79
    • 0028204934 scopus 로고
    • Actin filament bundles are associated with fiber gap junctions in the primate lens
    • Lo W.K., Mills A., Kuck J.F. Actin filament bundles are associated with fiber gap junctions in the primate lens. Exp. Eye Res. 58:1994;189-196.
    • (1994) Exp. Eye Res. , vol.58 , pp. 189-196
    • Lo, W.K.1    Mills, A.2    Kuck, J.F.3
  • 80
    • 0032763905 scopus 로고    scopus 로고
    • Dynamics of astrocyte adhesion as analyzed by a combination of atomic force microscopy and immuno-cytochemistry: The involvement of actin filaments and connexin 43 in the early stage of adhesion
    • Yamane Y., Shiga H., Asou H., Haga H., Kawabata K., Abe K., Ito E. Dynamics of astrocyte adhesion as analyzed by a combination of atomic force microscopy and immuno-cytochemistry: the involvement of actin filaments and connexin 43 in the early stage of adhesion. Arch. Histol. Cytol. 62:1999;355-361.
    • (1999) Arch. Histol. Cytol. , vol.62 , pp. 355-361
    • Yamane, Y.1    Shiga, H.2    Asou, H.3    Haga, H.4    Kawabata, K.5    Abe, K.6    Ito, E.7
  • 82
    • 0037035519 scopus 로고    scopus 로고
    • Connexin family members target to lipid raft domains and interact with caveolin-1
    • Schubert A.L., Schubert W., Spray D.C., Lisanti M.P. Connexin family members target to lipid raft domains and interact with caveolin-1. Biochemistry. 41:2002;5754-5764.
    • (2002) Biochemistry , vol.41 , pp. 5754-5764
    • Schubert, A.L.1    Schubert, W.2    Spray, D.C.3    Lisanti, M.P.4
  • 83
    • 0027252759 scopus 로고
    • Ultrastructural analysis of gap junctions in C6 glioma cells transfected with connexin43 cDNA
    • Naus C.C., Hearn S., Zhu D., Nicholson B.J., Shivers R.R. Ultrastructural analysis of gap junctions in C6 glioma cells transfected with connexin43 cDNA. Exp. Cell Res. 206:1993;72-84.
    • (1993) Exp. Cell Res. , vol.206 , pp. 72-84
    • Naus, C.C.1    Hearn, S.2    Zhu, D.3    Nicholson, B.J.4    Shivers, R.R.5
  • 84
    • 0030297087 scopus 로고    scopus 로고
    • Changes in the expression and distribution of connexin 43 in isolated cultured adult guinea pig cardiomyocytes
    • Huang X.D., Horackova M., Pressler M.L. Changes in the expression and distribution of connexin 43 in isolated cultured adult guinea pig cardiomyocytes. Exp. Cell Res. 228:1996;254-261.
    • (1996) Exp. Cell Res. , vol.228 , pp. 254-261
    • Huang, X.D.1    Horackova, M.2    Pressler, M.L.3
  • 85
    • 0028276554 scopus 로고
    • Degradation of the tumor suppressor protein p53 by the ubiquitin-mediated proteolytic system requires a novel species of ubiquitin-carrier protein, E2
    • Ciechanover A., Shkedy D., Oren M., Bercovich B. Degradation of the tumor suppressor protein p53 by the ubiquitin-mediated proteolytic system requires a novel species of ubiquitin-carrier protein, E2. J. Biol. Chem. 269:1994;9289-9582.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9289-9582
    • Ciechanover, A.1    Shkedy, D.2    Oren, M.3    Bercovich, B.4
  • 87
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • Hicke L. Protein regulation by monoubiquitin. Nat. Rev. Mol. Cell Biol. 2:2001;195-201.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 195-201
    • Hicke, L.1
  • 88
    • 0028817813 scopus 로고
    • The gap junction protein connexin43 is degraded via the ubiquitin proteasome pathway
    • Laing J.G., Beyer E.C. The gap junction protein connexin43 is degraded via the ubiquitin proteasome pathway. J. Biol. Chem. 270:1995;26399-26403.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26399-26403
    • Laing, J.G.1    Beyer, E.C.2
  • 89
    • 4244040008 scopus 로고    scopus 로고
    • Immunogold labeling of dispersed and ubiquitinated gap junction channels
    • R. Werner. Amsterdam, Netherlands: IOS Press
    • Hülser D.F., Rehkopf B., Traub O. Immunogold labeling of dispersed and ubiquitinated gap junction channels. Werner R. Gap Junctions. 1998;18-22 IOS Press, Amsterdam, Netherlands.
    • (1998) Gap Junctions , pp. 18-22
    • Hülser, D.F.1    Rehkopf, B.2    Traub, O.3
  • 90
    • 0035138999 scopus 로고    scopus 로고
    • Supramolecular dynamics of gap junctions
    • Rutz M.L., Hulser D.F. Supramolecular dynamics of gap junctions. Eur. J. Cell Biol. 80:2001;20-30.
    • (2001) Eur. J. Cell Biol. , vol.80 , pp. 20-30
    • Rutz, M.L.1    Hulser, D.F.2
  • 91
    • 1642380071 scopus 로고    scopus 로고
    • Characterization of a novel SH3-containing protein that may interact with connexin43
    • R. Werner. Amsterdam, Netherlands: IOS Press
    • Jin C., Lau A.F. Characterization of a novel SH3-containing protein that may interact with connexin43. Werner R. Gap Junctions. 1998;230-234 IOS Press, Amsterdam, Netherlands.
    • (1998) Gap Junctions , pp. 230-234
    • Jin, C.1    Lau, A.F.2
  • 92
    • 0034097698 scopus 로고    scopus 로고
    • Identification of connexin-interacting proteins: Application of the yeast two-hybrid screen
    • Jin C., Lau A.F., Martyn K.D. Identification of connexin-interacting proteins: application of the yeast two-hybrid screen. Methods. 20:2000;219-231.
    • (2000) Methods , vol.20 , pp. 219-231
    • Jin, C.1    Lau, A.F.2    Martyn, K.D.3
  • 93
    • 12244261647 scopus 로고    scopus 로고
    • Toward an understanding of cochlear homeostasis: The impact of location and the role of OCP1 and OCP2
    • Thalmann R., Henzl M.T., Killick R., Ignatova E.G., Thalmann I. Toward an understanding of cochlear homeostasis: the impact of location and the role of OCP1 and OCP2. Acta Oto-Laryngol. 123:2003;203-208.
    • (2003) Acta Oto-Laryngol. , vol.123 , pp. 203-208
    • Thalmann, R.1    Henzl, M.T.2    Killick, R.3    Ignatova, E.G.4    Thalmann, I.5
  • 94
    • 1642288872 scopus 로고    scopus 로고
    • Characterization of AP26, a protein which specifically binds to a tumor suppressor gene, connexin26
    • Wang X., Omori Y., Saito T., Ise K., Miura D., Yamasaki H. Characterization of AP26, a protein which specifically binds to a tumor suppressor gene, connexin26. Proc. Am. Assoc. Cancer Res. 44:2003;316.
    • (2003) Proc. Am. Assoc. Cancer Res. , vol.44 , pp. 316
    • Wang, X.1    Omori, Y.2    Saito, T.3    Ise, K.4    Miura, D.5    Yamasaki, H.6
  • 96
    • 0035754423 scopus 로고    scopus 로고
    • Determination of a potential role of the CCN family of growth regulators in connexin43 transfected C6 glioma cells
    • McLeod T.L., Bechberger J.F., Naus C.C. Determination of a potential role of the CCN family of growth regulators in connexin43 transfected C6 glioma cells. Cell Adhes. Commun. 8:2001;441-445.
    • (2001) Cell Adhes. Commun. , vol.8 , pp. 441-445
    • McLeod, T.L.1    Bechberger, J.F.2    Naus, C.C.3
  • 98
    • 0033950079 scopus 로고    scopus 로고
    • The importance of being proline: The interaction of proline-rich motifs in signaling proteins with their cognate domains
    • Kay B.K., Williamson M.P., Sudol M. The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J. 14:2000;231-241.
    • (2000) FASEB J. , vol.14 , pp. 231-241
    • Kay, B.K.1    Williamson, M.P.2    Sudol, M.3
  • 99
    • 0032543289 scopus 로고    scopus 로고
    • A 17 mer peptide interferes with acidification-induced uncoupling of connexin43
    • Calero G., Kanemitsu M., Taffet S.M., Lau A.F., Delmar M. A 17 mer peptide interferes with acidification-induced uncoupling of connexin43. Circ. Res. 82:1998;929-935.
    • (1998) Circ. Res. , vol.82 , pp. 929-935
    • Calero, G.1    Kanemitsu, M.2    Taffet, S.M.3    Lau, A.F.4    Delmar, M.5
  • 101
    • 0034234655 scopus 로고    scopus 로고
    • Targeting motifs and functional parameters governing the assembly of connexins into gap junctions
    • Martin P.E., Steggles J., Wilson C., Ahmad S., Evans W.H. Targeting motifs and functional parameters governing the assembly of connexins into gap junctions. Biochem. J. 349:2000;281-287.
    • (2000) Biochem. J. , vol.349 , pp. 281-287
    • Martin, P.E.1    Steggles, J.2    Wilson, C.3    Ahmad, S.4    Evans, W.H.5
  • 102
    • 0033538828 scopus 로고    scopus 로고
    • Connexin-occludin chimeras containing the ZO-binding domain of occludin localize at MDCK tight junctions and NRK cell contacts
    • Mitic L.L., Schneeberger E.F., Fanning A.S., Anderson J.M. Connexin-occludin chimeras containing the ZO-binding domain of occludin localize at MDCK tight junctions and NRK cell contacts. J. Cell Biol. 146:1999;683-693.
    • (1999) J. Cell Biol. , vol.146 , pp. 683-693
    • Mitic, L.L.1    Schneeberger, E.F.2    Fanning, A.S.3    Anderson, J.M.4
  • 104
    • 0026535991 scopus 로고
    • Immunolocalization and expression of functional and nonfunctional cell-to-cell channels from wild-type and mutant rat heart connexin43 cDNA
    • Dunham B., Liu S., Taffet S., Trabka Janik E., Delmar M., Petryshyn R., Zheng S., Perzova R., Vallano M.L. Immunolocalization and expression of functional and nonfunctional cell-to-cell channels from wild-type and mutant rat heart connexin43 cDNA. Circ. Res. 70:1992;1233-1243.
    • (1992) Circ. Res. , vol.70 , pp. 1233-1243
    • Dunham, B.1    Liu, S.2    Taffet, S.3    Trabka Janik, E.4    Delmar, M.5    Petryshyn, R.6    Zheng, S.7    Perzova, R.8    Vallano, M.L.9
  • 105
    • 0035188530 scopus 로고    scopus 로고
    • Multiple pathways in the trafficking and assembly of connexin 26, 32 and 43 into gap junction intercellular communication channels
    • Martin P.E., Blundell G., Ahmad S., Errington R.J., Evans W.H. Multiple pathways in the trafficking and assembly of connexin 26, 32 and 43 into gap junction intercellular communication channels. J. Cell. Sci. 114:2001;3845-3855.
    • (2001) J. Cell. Sci. , vol.114 , pp. 3845-3855
    • Martin, P.E.1    Blundell, G.2    Ahmad, S.3    Errington, R.J.4    Evans, W.H.5
  • 106
    • 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., Falk M.M. Dynamic trafficking and delivery of connexons to the plasma membrane and accretion to gap junctions in living cells. Proc. Natl. Acad. Sci. U. S. A. 99:2002;10446-10451.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , 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
  • 108
    • 0037147288 scopus 로고    scopus 로고
    • Impaired trafficking of connexins in androgen-independent human prostate cancer cell lines and its mitigation by alpha-catenin
    • Govindarajan R., Zhao S., Song X.H., Guo R.J., Wheelock M., Johnson K.R., Mehta P.P. Impaired trafficking of connexins in androgen-independent human prostate cancer cell lines and its mitigation by alpha-catenin. J. Biol. Chem. 277:2002;50087-50097.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50087-50097
    • Govindarajan, R.1    Zhao, S.2    Song, X.H.3    Guo, R.J.4    Wheelock, M.5    Johnson, K.R.6    Mehta, P.P.7
  • 110
    • 0030579159 scopus 로고    scopus 로고
    • Gap junction formation between cultured embryonic lens cells is inhibited by antibody to N-cadherin
    • Frenzel E.M., Johnson R.G. Gap junction formation between cultured embryonic lens cells is inhibited by antibody to N-cadherin. Dev. Biol. 179:1996;1-16.
    • (1996) Dev. Biol. , vol.179 , pp. 1-16
    • Frenzel, E.M.1    Johnson, R.G.2
  • 111
    • 0030053566 scopus 로고    scopus 로고
    • N-cadherin in adult rat cardiomyocytes in culture: II. Spatio-temporal appearance of proteins involved in cell-cell contact and communication. Formation of two distinct N-cadherin/catenin complexes
    • Hertig C.M., Eppenberger-Eberhardt M., Koch S., Eppenberger H.M. N-cadherin in adult rat cardiomyocytes in culture: II. Spatio-temporal appearance of proteins involved in cell-cell contact and communication. Formation of two distinct N-cadherin/catenin complexes. J. Cell. Sci. 109:1996;1-10.
    • (1996) J. Cell. Sci. , vol.109 , pp. 1-10
    • Hertig, C.M.1    Eppenberger-Eberhardt, M.2    Koch, S.3    Eppenberger, H.M.4
  • 112
    • 0036204837 scopus 로고    scopus 로고
    • Rho and Rho-kinase (ROCK) signaling in adherens and gap junction assembly in corneal epithelium
    • Anderson S.C., Stone C., Tkach L., SundarRaj N. Rho and Rho-kinase (ROCK) signaling in adherens and gap junction assembly in corneal epithelium. Invest. Ophthalmol. Visual Sci. 43:2002;978-986.
    • (2002) Invest. Ophthalmol. Visual Sci. , vol.43 , pp. 978-986
    • Anderson, S.C.1    Stone, C.2    Tkach, L.3    Sundarraj, N.4
  • 113
    • 0031281674 scopus 로고    scopus 로고
    • Degradation of connexin43 gap junctions involves both the proteasome and the lysosome
    • Laing J.G., Tadros P.N., Westphale E.M., Beyer E.C. Degradation of connexin43 gap junctions involves both the proteasome and the lysosome. Exp. Cell Res. 236:1997;482-492.
    • (1997) Exp. Cell Res. , vol.236 , pp. 482-492
    • Laing, J.G.1    Tadros, P.N.2    Westphale, E.M.3    Beyer, E.C.4
  • 114
    • 0037672616 scopus 로고    scopus 로고
    • A tyrosine-based sorting signal is involved in connexin43 stability and gap junction turnover
    • Thomas M.A., Zosso N., Scerri I., Demaurex N., Chanson M., Staub O. A tyrosine-based sorting signal is involved in connexin43 stability and gap junction turnover. J. Cell. Sci. 116:2003;2213-2222.
    • (2003) J. Cell. Sci. , vol.116 , pp. 2213-2222
    • Thomas, M.A.1    Zosso, N.2    Scerri, I.3    Demaurex, N.4    Chanson, M.5    Staub, O.6
  • 115
    • 0030042852 scopus 로고    scopus 로고
    • Evidence that disruption of connexon particle arrangements in gap junction plaques is associated with inhibition of gap junctional communication by a glycyrrhetinic acid derivative
    • Goldberg G.S., Moreno A.P., Bechberger J.F., Hearn S.S., Shivers R.R., MacPhee D.J., Zhang Y., Naus C.C.G. Evidence that disruption of connexon particle arrangements in gap junction plaques is associated with inhibition of gap junctional communication by a glycyrrhetinic acid derivative. Exp. Cell Res. 222:1996;48-53.
    • (1996) Exp. Cell Res. , vol.222 , pp. 48-53
    • Goldberg, G.S.1    Moreno, A.P.2    Bechberger, J.F.3    Hearn, S.S.4    Shivers, R.R.5    MacPhee, D.J.6    Zhang, Y.7    Naus, C.C.G.8
  • 116
    • 0029757386 scopus 로고    scopus 로고
    • Gap-junction disassembly and connexin 43 dephosphorylation induced by 18 beta-glycyrrhetinic acid
    • Guan X., Wilson S., Schlender K.K., Ruch R. Gap-junction disassembly and connexin 43 dephosphorylation induced by 18 beta-glycyrrhetinic acid. Mol. Carcinog. 16:1996;157-164.
    • (1996) Mol. Carcinog. , vol.16 , pp. 157-164
    • Guan, X.1    Wilson, S.2    Schlender, K.K.3    Ruch, R.4
  • 117
    • 0033060335 scopus 로고    scopus 로고
    • Inhibition of gap junction communication in alveolar epithelial cells by 18alpha-glycyrrhetinic acid
    • Guo Y., Martinez-Williams C., Gilbert K.A., Rannels D.E. Inhibition of gap junction communication in alveolar epithelial cells by 18alpha- glycyrrhetinic acid. Am. J. Physiol. 276:1999;L1018-L1026.
    • (1999) Am. J. Physiol. , vol.276 , pp. 1018-L1026
    • Guo, Y.1    Martinez-Williams, C.2    Gilbert, K.A.3    Rannels, D.E.4
  • 119
    • 0032431737 scopus 로고    scopus 로고
    • Deficient epithelial-fibroblast heterocellular gap junction communication can be overcome by co-culture with an intermediate cell type but not by E-cadherin transgene expression
    • Woodward T.L., Sia M.A., Blaschuk O.W., Turner J.D., Laird D.W. Deficient epithelial-fibroblast heterocellular gap junction communication can be overcome by co-culture with an intermediate cell type but not by E-cadherin transgene expression. J. Cell. Sci. 111:1998;3529-3539.
    • (1998) J. Cell. Sci. , vol.111 , pp. 3529-3539
    • Woodward, T.L.1    Sia, M.A.2    Blaschuk, O.W.3    Turner, J.D.4    Laird, D.W.5
  • 120
    • 0031390117 scopus 로고    scopus 로고
    • E-cadherin expression can alter the specificity of gap junction formation
    • Prowse D.M., Cadwallader G.P., Pitts J.D. E-cadherin expression can alter the specificity of gap junction formation. Cell Biol. Int. 21:1997;833-843.
    • (1997) Cell Biol. Int. , vol.21 , pp. 833-843
    • Prowse, D.M.1    Cadwallader, G.P.2    Pitts, J.D.3
  • 121
    • 0031044910 scopus 로고    scopus 로고
    • An inhibition of gap-junctional communication by cadherins
    • Wang Y., Rose B. An inhibition of gap-junctional communication by cadherins. J. Cell. Sci. 110:1997;301-309.
    • (1997) J. Cell. Sci. , vol.110 , pp. 301-309
    • Wang, Y.1    Rose, B.2
  • 122
    • 0034025433 scopus 로고    scopus 로고
    • Cadherin repertoire determines partner-specific gap junctional communication during melanoma progression
    • Hsu M., Andl T., Li G., Meinkoth J.L., Herlyn M. Cadherin repertoire determines partner-specific gap junctional communication during melanoma progression. J. Cell. Sci. 113:2000;1535-1542.
    • (2000) J. Cell. Sci. , vol.113 , pp. 1535-1542
    • Hsu, M.1    Andl, T.2    Li, G.3    Meinkoth, J.L.4    Herlyn, M.5
  • 123
    • 0033561399 scopus 로고    scopus 로고
    • ATP counteracts the rundown of gap junctional channels of rat ventricular myocytes by promoting protein phosphorylation
    • Verrecchia F., Duthé F., Duval S., Duchatelle I., Sarrouilhe D., Hervé J.C. ATP counteracts the rundown of gap junctional channels of rat ventricular myocytes by promoting protein phosphorylation. J. Physiol. 516:1999;447-459.
    • (1999) J. Physiol. , vol.516 , pp. 447-459
    • Verrecchia, F.1    Duthé, F.2    Duval, S.3    Duchatelle, I.4    Sarrouilhe, D.5    Hervé, J.C.6
  • 124
    • 0023161934 scopus 로고
    • Dependence of junctional conductance on proton, calcium and magnesium ions in cardiac paired cells of guinea-pig
    • Noma A., Tsuboi N. Dependence of junctional conductance on proton, calcium and magnesium ions in cardiac paired cells of guinea-pig. J. Physiol. 382:1987;193-211.
    • (1987) J. Physiol. , vol.382 , pp. 193-211
    • Noma, A.1    Tsuboi, N.2
  • 125
    • 0030881006 scopus 로고    scopus 로고
    • Effects of peroxisome proliferators and 12-O-tetradecanoyl phorbol-13-acetate on intercellular communication and connexin43 in two hamster fibroblast systems
    • Cruciani V., Mikalsen S.O., Vasseur P., Sanner T. Effects of peroxisome proliferators and 12-O-tetradecanoyl phorbol-13-acetate on intercellular communication and connexin43 in two hamster fibroblast systems. Int. J. Cancer. 73:1997;240-248.
    • (1997) Int. J. Cancer , vol.73 , pp. 240-248
    • Cruciani, V.1    Mikalsen, S.O.2    Vasseur, P.3    Sanner, T.4
  • 126
    • 0001779624 scopus 로고    scopus 로고
    • Enhanced gap junction assembly following the elevation of cAMP requires full-length Cx43
    • R. Werner. Amsterdam, Netherlands: IOS Press
    • TenBroek E., Taffet P.S., Reynhout J., Martyn K., Kurata W., Lau A., Johnson R. Enhanced gap junction assembly following the elevation of cAMP requires full-length Cx43. Werner R. Gap Junctions. 1998;215-219 IOS Press, Amsterdam, Netherlands.
    • (1998) Gap Junctions , pp. 215-219
    • Tenbroek, E.1    Taffet, P.S.2    Reynhout, J.3    Martyn, K.4    Kurata, W.5    Lau, A.6    Johnson, R.7
  • 127
    • 0032978738 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase and phosphorylation of connexin43 are not sufficient for the disruption of gap junctional communication by platelet-derived growth factor and tetradecanoylphorbol acetate
    • Hossain M.Z., Jagdale A.B., Ao P., Boynton A.L. Mitogen-activated protein kinase and phosphorylation of connexin43 are not sufficient for the disruption of gap junctional communication by platelet-derived growth factor and tetradecanoylphorbol acetate. J. Cell. Physiol. 179:1999;87-96.
    • (1999) J. Cell. Physiol. , vol.179 , pp. 87-96
    • Hossain, M.Z.1    Jagdale, A.B.2    Ao, P.3    Boynton, A.L.4
  • 128
    • 0033537929 scopus 로고    scopus 로고
    • Disruption of gap junctional communication by the platelet-derived growth factor is mediated via multiple signaling pathways
    • Hossain M.Z., Jagdale A.B., Ao P., Kazlauskas A., Boynton A.L. Disruption of gap junctional communication by the platelet-derived growth factor is mediated via multiple signaling pathways. J. Biol. Chem. 274:1999;10489-10496.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10489-10496
    • Hossain, M.Z.1    Jagdale, A.B.2    Ao, P.3    Kazlauskas, A.4    Boynton, A.L.5
  • 129
    • 0034570579 scopus 로고    scopus 로고
    • Dephosphorylation agents depress gap junctional communication between rat cardiac cells without modifying the Connexin43 phosphorylation degree
    • Duthe F., Dupont E., Verrecchia F., Plaisance I., Severs N.J., Sarrouilhe D., Hervé J.C. Dephosphorylation agents depress gap junctional communication between rat cardiac cells without modifying the Connexin43 phosphorylation degree. Gen. Physiol. Biophys. 19:2000;441-449.
    • (2000) Gen. Physiol. Biophys. , vol.19 , pp. 441-449
    • Duthe, F.1    Dupont, E.2    Verrecchia, F.3    Plaisance, I.4    Severs, N.J.5    Sarrouilhe, D.6    Hervé, J.C.7
  • 130
    • 0034031992 scopus 로고    scopus 로고
    • Electrical conductance of mouse connexin45 gap junction channels is modulated by phosphorylation
    • van Veen T.A.B., van Rijen H.V., Jongsma H.J. Electrical conductance of mouse connexin45 gap junction channels is modulated by phosphorylation. Cardiovasc. Res. 46:2000;496-510.
    • (2000) Cardiovasc. Res. , vol.46 , pp. 496-510
    • Van Veen, T.A.B.1    Van Rijen, H.V.2    Jongsma, H.J.3
  • 131
    • 0024566344 scopus 로고
    • Comparative characterization of the 21-kD and 26-kD gap junction proteins in murine liver and cultured hepatocytes
    • Traub O., Look J., Dermietzel R., Hulser D., Willecke K. Comparative characterization of the 21-kD and 26-kD gap junction proteins in murine liver and cultured hepatocytes. J. Cell Biol. 108:1989;1039-1051.
    • (1989) J. Cell Biol. , vol.108 , pp. 1039-1051
    • Traub, O.1    Look, J.2    Dermietzel, R.3    Hulser, D.4    Willecke, K.5
  • 132
    • 0028882497 scopus 로고
    • Differential regulation of distinct types of gap junction channels by similar phosphorylating conditions
    • Kwak B.R., Hermans M.M.P., De Jonge H.R., Lohmann S.M., Jongsma H.J., Chanson M. Differential regulation of distinct types of gap junction channels by similar phosphorylating conditions. Mol. Biol. Cell. 6:1995;1707-1719.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1707-1719
    • Kwak, B.R.1    Hermans, M.M.P.2    De Jonge, H.R.3    Lohmann, S.M.4    Jongsma, H.J.5    Chanson, M.6
  • 133
    • 0033932651 scopus 로고    scopus 로고
    • Connexin43 phosphorylation state and intercellular communication in cultured astrocytes following hypoxia and protein phosphatase inhibition
    • Li W.E., Nagy J.I. Connexin43 phosphorylation state and intercellular communication in cultured astrocytes following hypoxia and protein phosphatase inhibition. Eur. J. Neurosci. 12:2000;2644-2650.
    • (2000) Eur. J. Neurosci. , vol.12 , pp. 2644-2650
    • Li, W.E.1    Nagy, J.I.2
  • 134
    • 0013388927 scopus 로고    scopus 로고
    • Down-regulation of gap junctional intercellular communication between osteoblastic MC3T3-E1 cells by basic fibroblast growth factor and a phorbol ester (12-O-tetradecanoylphorbol-13-acetate)
    • Shiokawa-Sawada M., Mano H., Hanada K., Kakudo S., Kameda T., Miyazawa K., Nakamaru Y., Yuasa T., Mori Y., Kumegawa M., Hakeda Y. Down-regulation of gap junctional intercellular communication between osteoblastic MC3T3-E1 cells by basic fibroblast growth factor and a phorbol ester (12-O- tetradecanoylphorbol-13-acetate). J. Bone Miner. Res. 12:1997;1165-1173.
    • (1997) J. Bone Miner. Res. , vol.12 , pp. 1165-1173
    • Shiokawa-Sawada, M.1    Mano, H.2    Hanada, K.3    Kakudo, S.4    Kameda, T.5    Miyazawa, K.6    Nakamaru, Y.7    Yuasa, T.8    Mori, Y.9    Kumegawa, M.10    Hakeda, Y.11
  • 135
    • 0032502785 scopus 로고    scopus 로고
    • Regulation of connexin-43 gap junctional intercellular communication by mitogen-activated protein kinase
    • Warn-Cramer B.J., Cottrell G.T., Burt J.M., Lau A.F. Regulation of connexin-43 gap junctional intercellular communication by mitogen-activated protein kinase. J. Biol. Chem. 273:1998;9188-9196.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9188-9196
    • Warn-Cramer, B.J.1    Cottrell, G.T.2    Burt, J.M.3    Lau, A.F.4
  • 137
    • 0033966213 scopus 로고    scopus 로고
    • Internalization of the Kv1.4 potassium channel is suppressed by clustering interactions with PSD-95
    • Jugloff D.G., Khanna R., Schlichter L.C., Jones O.T. Internalization of the Kv1.4 potassium channel is suppressed by clustering interactions with PSD-95. J. Biol. Chem. 275:2000;1357-1364.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1357-1364
    • Jugloff, D.G.1    Khanna, R.2    Schlichter, L.C.3    Jones, O.T.4
  • 140
    • 0037004026 scopus 로고    scopus 로고
    • Microinjected anti-actin antibodies decrease gap junctional intercellular commmunication in cultured astrytes
    • Theiss C., Meller K. Microinjected anti-actin antibodies decrease gap junctional intercellular commmunication in cultured astrytes. Exp. Cell Res. 281:2002;197-204.
    • (2002) Exp. Cell Res. , vol.281 , pp. 197-204
    • Theiss, C.1    Meller, K.2
  • 141
    • 0037025055 scopus 로고    scopus 로고
    • Gap junctional channel inhibition alters actin organization and calcium propagation in rat cultured astrocytes
    • Yamane Y., Shiga H., Asou H., Ito E. Gap junctional channel inhibition alters actin organization and calcium propagation in rat cultured astrocytes. Neuroscience. 112:2002;593-603.
    • (2002) Neuroscience , vol.112 , pp. 593-603
    • Yamane, Y.1    Shiga, H.2    Asou, H.3    Ito, E.4
  • 142
    • 0032213261 scopus 로고    scopus 로고
    • Cytoskeletal assembly and ATP release regulate astrocytic calcium signaling
    • Cotrina M.L., Lin J.H., Nedergaard M.J. Cytoskeletal assembly and ATP release regulate astrocytic calcium signaling. J. Neurosci. 18:1998;8794-8804.
    • (1998) J. Neurosci. , vol.18 , pp. 8794-8804
    • Cotrina, M.L.1    Lin, J.H.2    Nedergaard, M.J.3
  • 144
    • 0037040922 scopus 로고    scopus 로고
    • Transduction of cell survival signals by connexin-43 hemichannels
    • Plotkin L.I., Manolagas S.C., Bellido T. Transduction of cell survival signals by connexin-43 hemichannels. J. Biol. Chem. 277:2002;8648-8657.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8648-8657
    • Plotkin, L.I.1    Manolagas, S.C.2    Bellido, T.3
  • 145
    • 80755173667 scopus 로고    scopus 로고
    • Reciprocal regulation of the junctional proteins claudin-1 and connexin43 by interleukin-1beta in primary human fetal astrocytes
    • Duffy H.S., John G.R., Lee S.C., Brosnan C.F., Spray D.C. Reciprocal regulation of the junctional proteins claudin-1 and connexin43 by interleukin-1beta in primary human fetal astrocytes. J. Neurosci. 20:2000;1-6.
    • (2000) J. Neurosci. , vol.20 , pp. 1-6
    • Duffy, H.S.1    John, G.R.2    Lee, S.C.3    Brosnan, C.F.4    Spray, D.C.5
  • 146
    • 0033552629 scopus 로고    scopus 로고
    • Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins
    • Itoh M., Furuse M., Morita K., Kubota K., Saitou M., Tsukita S. Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins. J. Cell Biol. 147:1999;1351-1363.
    • (1999) J. Cell Biol. , vol.147 , pp. 1351-1363
    • Itoh, M.1    Furuse, M.2    Morita, K.3    Kubota, K.4    Saitou, M.5    Tsukita, S.6
  • 147
    • 0033851771 scopus 로고    scopus 로고
    • Molecular physiology and pathophysiology of tight junctions I. Tight junction structure and function lessons from mutant animals and proteins
    • Mitic L.L., Van Itallie C.M., Anderson J.M. Molecular physiology and pathophysiology of tight junctions I. Tight junction structure and function lessons from mutant animals and proteins. Am. J. Physiol. 279:2000;G250-G254.
    • (2000) Am. J. Physiol. , vol.279 , pp. 250-G254
    • Mitic, L.L.1    Van Itallie, C.M.2    Anderson, J.M.3
  • 148
    • 0033860051 scopus 로고    scopus 로고
    • Ligand-gated ion channel interactions with cytoskeletal and signaling proteins
    • Sheng M., Pak D.T. Ligand-gated ion channel interactions with cytoskeletal and signaling proteins. Annu. Rev. Physiol. 62:2000;755-778.
    • (2000) Annu. Rev. Physiol. , vol.62 , pp. 755-778
    • Sheng, M.1    Pak, D.T.2


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