메뉴 건너뛰기




Volumn 1818, Issue 8, 2012, Pages 1844-1865

Gap junctional channels are parts of multiprotein complexes

Author keywords

Connexin; Innexin; Pannexin; Protein protein; Zonula Occludens

Indexed keywords

CALMODULIN; CARRIER PROTEIN; CAVEOLIN; CONNEXIN 26; CONNEXIN 32; CONNEXIN 43; CONNEXIN 47; CYTOSKELETON PROTEIN; GAP JUNCTION CHANNEL; GAP JUNCTION PROTEIN; INNEXIN; MEMBRANE PROTEIN; NERVE CELL ADHESION MOLECULE; PANNEXIN; PDZ PROTEIN; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN KINASE C; PROTEIN ZO1; PROTEIN ZO2; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

EID: 84861634571     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2011.12.009     Document Type: Review
Times cited : (121)

References (272)
  • 3
    • 79953182204 scopus 로고    scopus 로고
    • Pannexins or connexins?
    • A.L. Harris, D. Locke, Humana Press New York
    • G. Dahl, and A.L. Harris Pannexins or connexins? A.L. Harris, D. Locke, Connexins, A Guide 2008 Humana Press New York 287 302
    • (2008) Connexins, A Guide , pp. 287-302
    • Dahl, G.1    Harris, A.L.2
  • 4
    • 79960212462 scopus 로고    scopus 로고
    • Pannexin 3 functions as an ER Ca2 + channel, hemichannel, and gap junction to promote osteoblast differentiation
    • M. Ishikawa, T. Iwamoto, T. Nakamura, A. Doyle, S. Fukumoto, and Y. Yamada Pannexin 3 functions as an ER Ca2 + channel, hemichannel, and gap junction to promote osteoblast differentiation J. Cell Biol. 193 2011 1257 1274
    • (2011) J. Cell Biol. , vol.193 , pp. 1257-1274
    • Ishikawa, M.1    Iwamoto, T.2    Nakamura, T.3    Doyle, A.4    Fukumoto, S.5    Yamada, Y.6
  • 7
    • 38049036928 scopus 로고    scopus 로고
    • Cx23, a connexin with only four extracellular-loop cysteines, forms functional gap junction channels and hemichannels
    • M.K. Iovine, A.M. Gumpert, M.M. Falk, and T.C. Mendelson Cx23, a connexin with only four extracellular-loop cysteines, forms functional gap junction channels and hemichannels FEBS Lett. 582 2008 165 170
    • (2008) FEBS Lett. , vol.582 , pp. 165-170
    • Iovine, M.K.1    Gumpert, A.M.2    Falk, M.M.3    Mendelson, T.C.4
  • 9
    • 35748965595 scopus 로고    scopus 로고
    • Pannexin1 channels contain a glycosylation site that targets the hexamer to the plasma membrane
    • D. Boassa, C. Ambrosi, F. Qiu, G. Dahl, G. Gaietta, and G. Sosinsky Pannexin1 channels contain a glycosylation site that targets the hexamer to the plasma membrane J. Biol. Chem. 282 2007 31733 31743
    • (2007) J. Biol. Chem. , vol.282 , pp. 31733-31743
    • Boassa, D.1    Ambrosi, C.2    Qiu, F.3    Dahl, G.4    Gaietta, G.5    Sosinsky, G.6
  • 10
    • 0035704411 scopus 로고    scopus 로고
    • Emerging issues of connexin channels: Biophysics fills the gap
    • A.L. Harris 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
  • 11
    • 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
    • T.W. White, R. Bruzzone, S. Wolfram, D.L. Paul, and D.A. Goodenough 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
  • 12
    • 0028230758 scopus 로고
    • Expression of chimeric connexins reveals new properties of the formation and gating behavior of gap junction channels
    • R. Bruzzone, T.W. White, and D.L. Paul Expression of chimeric connexins reveals new properties of the formation and gating behavior of gap junction channels 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
  • 13
    • 78649831043 scopus 로고    scopus 로고
    • Peptides targeting gap junctional structures
    • J.C. Hervé, and S. Dhein Peptides targeting gap junctional structures Curr. Pharm. Des. 16 2010 3056 3070
    • (2010) Curr. Pharm. Des. , vol.16 , pp. 3056-3070
    • Hervé, J.C.1    Dhein, S.2
  • 14
    • 0001203743 scopus 로고    scopus 로고
    • Formation of heteromeric gap junction channels by connexins 40 and 43 in vascular smooth muscle cells
    • D.S. He, J.X. Jiang, S.M. Taffet, and J.M. Burt Formation of heteromeric gap junction channels by connexins 40 and 43 in vascular smooth muscle cells Proc. Natl. Acad. Sci. U. S. A. 96 1999 6495 6500
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 6495-6500
    • He, D.S.1    Jiang, J.X.2    Taffet, S.M.3    Burt, J.M.4
  • 15
    • 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
    • S. Liu, S. Taffet, L. Stoner, M. Delmar, M.L. Vallano, and J. Jalife 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
  • 16
    • 0030050142 scopus 로고    scopus 로고
    • Intramolecular interactions mediate pH regulation of connexin43 channels
    • G.E. Morley, S.M. Taffet, and M. Delmar 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
  • 19
    • 0032838486 scopus 로고    scopus 로고
    • Molecular dissection of transjunctional voltage dependence in the connexin-32 and connexin-43 junctions
    • A. Revilla, C. Castro, and L.C. Barrio 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
  • 20
    • 0000402507 scopus 로고    scopus 로고
    • Behavior of chemical- and slow voltage-sensitive gating of connexin channels: The cork gating hypothesis
    • C. Peracchia, Academic Press San Diego, CA
    • C. Peracchia, X.G. Wang, and L.L. Peracchia Behavior of chemical- and slow voltage-sensitive gating of connexin channels: the cork gating hypothesis C. Peracchia, Gap Junctions. Molecular Basis of Cell Communication in Health and Disease 2000 Academic Press San Diego, CA 271 295
    • (2000) Gap Junctions. Molecular Basis of Cell Communication in Health and Disease , pp. 271-295
    • Peracchia, C.1    Wang, X.G.2    Peracchia, L.L.3
  • 23
    • 0025224223 scopus 로고
    • Biophysical and molecular mechanisms of Shaker potassium channel inactivation
    • T. Hoshi, W.N. Zagotta, and R.W. Aldrich 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
  • 25
    • 0035853435 scopus 로고    scopus 로고
    • The carboxyl terminal domain regulates the unitary conductance and voltage dependence of connexin40 gap junction channels
    • J.M. Anumonwo, S.M. Taffet, H. Gu, M. Chanson, A.P. Moreno, and M. Delmar 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
  • 26
    • 71749094770 scopus 로고    scopus 로고
    • Characterization of the structure and intermolecular interactions between the connexin40 and connexin43 carboxyl-terminal and cytoplasmic loop domains
    • D. Bouvier, G. Spagnol, S. Chenavas, F. Kieken, H. Vitrac, S. Brownell, A. Kellezi, V. Forge, and P.L. Sorgen Characterization of the structure and intermolecular interactions between the connexin40 and connexin43 carboxyl-terminal and cytoplasmic loop domains J. Biol. Chem. 284 2009 34257 34271
    • (2009) J. Biol. Chem. , vol.284 , pp. 34257-34271
    • Bouvier, D.1    Spagnol, G.2    Chenavas, S.3    Kieken, F.4    Vitrac, H.5    Brownell, S.6    Kellezi, A.7    Forge, V.8    Sorgen, P.L.9
  • 27
    • 15744376289 scopus 로고    scopus 로고
    • Modifications in the biophysical properties of connexin43 channels by a peptide of the cytoplasmic loop region
    • A. Seki, H.S. Duffy, W. Coombs, D.C. Spray, S.M. Taffet, and M. Delmar Modifications in the biophysical properties of connexin43 channels by a peptide of the cytoplasmic loop region Circ. Res. 95 2004 e22 e28
    • (2004) Circ. Res. , vol.95
    • Seki, A.1    Duffy, H.S.2    Coombs, W.3    Spray, D.C.4    Taffet, S.M.5    Delmar, M.6
  • 31
    • 3042855148 scopus 로고    scopus 로고
    • PH-dependent dimerization of the carboxyl terminal domain of Cx43
    • P.L. Sorgen, H.S. Duffy, D.C. Spray, and M. Delmar pH-dependent dimerization of the carboxyl terminal domain of Cx43 Biophys. J. 87 2004 574 581
    • (2004) Biophys. J. , vol.87 , pp. 574-581
    • Sorgen, P.L.1    Duffy, H.S.2    Spray, D.C.3    Delmar, M.4
  • 32
    • 34247157344 scopus 로고    scopus 로고
    • Characterization of the pH-dependent interaction between the gap junction protein connexin43 carboxyl terminus and cytoplasmic loop domains
    • B.J. Hirst-Jensen, P. Sahoo, F. Kieken, M. Delmar, and P.L. Sorgen Characterization of the pH-dependent interaction between the gap junction protein connexin43 carboxyl terminus and cytoplasmic loop domains J. Biol. Chem. 282 2007 5801 5813
    • (2007) J. Biol. Chem. , vol.282 , pp. 5801-5813
    • Hirst-Jensen, B.J.1    Sahoo, P.2    Kieken, F.3    Delmar, M.4    Sorgen, P.L.5
  • 33
    • 33745427413 scopus 로고    scopus 로고
    • Heteromerization of innexin gap junction proteins regulates epithelial tissue organization in Drosophila
    • C. Lehmann, H. Lechner, B. Löer, M. Knieps, S. Herrmann, M. Famulok, R. Bauer, and M. Hoch Heteromerization of innexin gap junction proteins regulates epithelial tissue organization in Drosophila Mol. Biol. Cell 17 2006 1676 1685
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1676-1685
    • Lehmann, C.1    Lechner, H.2    Löer, B.3    Knieps, M.4    Herrmann, S.5    Famulok, M.6    Bauer, R.7    Hoch, M.8
  • 34
    • 70350112277 scopus 로고    scopus 로고
    • Glycosylation regulates pannexin intermixing and cellular localization
    • S. Penuela, R. Bhalla, K. Nag, and D.W. Laird Glycosylation regulates pannexin intermixing and cellular localization Mol. Biol. Cell 20 2009 4313 4323
    • (2009) Mol. Biol. Cell , vol.20 , pp. 4313-4323
    • Penuela, S.1    Bhalla, R.2    Nag, K.3    Laird, D.W.4
  • 35
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • T. Pawson, and J.D. Scott Signaling through scaffold, anchoring, and adaptor proteins Science 278 1997 2075 2080
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 37
    • 0032541641 scopus 로고    scopus 로고
    • From Src homology domains to other signaling modules: Proposal of the 'protein recognition code'
    • M. Sudol From Src homology domains to other signaling modules: proposal of the 'protein recognition code' Oncogene 17 1998 1469 1474
    • (1998) Oncogene , vol.17 , pp. 1469-1474
    • Sudol, M.1
  • 38
    • 0030077915 scopus 로고    scopus 로고
    • Immunolocalization of the mNav2.3 Na + channel in mouse heart: Upregulation in myometrium during pregnancy
    • T.J. Knittle, K.L. Doyle, and M.M. Tamkun Immunolocalization of the mNav2.3 Na + channel in mouse heart: upregulation in myometrium during pregnancy Am. J. Physiol. 270 1996 C688 C696
    • (1996) Am. J. Physiol. , vol.270
    • Knittle, T.J.1    Doyle, K.L.2    Tamkun, M.M.3
  • 39
    • 0033617473 scopus 로고    scopus 로고
    • Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex
    • B.J. Hillier, K.S. Christopherson, K.E. Prehoda, D.S. Bredt, and W.A. Lim Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex Science 284 1999 812 815
    • (1999) Science , vol.284 , pp. 812-815
    • Hillier, B.J.1    Christopherson, K.S.2    Prehoda, K.E.3    Bredt, D.S.4    Lim, W.A.5
  • 40
    • 0030835610 scopus 로고    scopus 로고
    • A multivalent PDZdomain protein assembles signalling complexes in a G- protein-coupled cascade
    • S. Tsunoda, J. Sierralta, Y. Sun, R. Bodner, E. Suzuki, A. Becker, M. Socolich, and C.S. Zuker A multivalent PDZdomain protein assembles signalling complexes in a G- protein-coupled cascade Nature 388 1997 243 249
    • (1997) Nature , vol.388 , pp. 243-249
    • Tsunoda, S.1    Sierralta, J.2    Sun, Y.3    Bodner, R.4    Suzuki, E.5    Becker, A.6    Socolich, M.7    Zuker, C.S.8
  • 41
    • 0028838012 scopus 로고
    • Dimerization of cell surface receptors in signal transduction
    • C.H. Heldin Dimerization of cell surface receptors in signal transduction Cell 80 1995 213 223
    • (1995) Cell , vol.80 , pp. 213-223
    • Heldin, C.H.1
  • 42
    • 0030883743 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of connexin 43 by v-Src is mediated by SH2 and SH3 domain interactions
    • M.Y. Kanemitsu, L.W. Loo, S. Simon, A.F. Lau, and W. Eckhart 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
  • 43
    • 33744484067 scopus 로고    scopus 로고
    • Role of connexin43-interacting proteins at gap junctions
    • B.N. Giepmans Role of connexin43-interacting proteins at gap junctions Adv. Cardiol. 43 2006 41 56
    • (2006) Adv. Cardiol. , vol.43 , pp. 41-56
    • Giepmans, B.N.1
  • 44
    • 0012927828 scopus 로고    scopus 로고
    • PDZ domain proteins: Plug and play!
    • RE7
    • C. Nourry, S.G. Grant, and J.P. Borg PDZ domain proteins: plug and play! Sci. STKE 179 2003 RE7
    • (2003) Sci. STKE , vol.179
    • Nourry, C.1    Grant, S.G.2    Borg, J.P.3
  • 45
  • 47
    • 77950567390 scopus 로고    scopus 로고
    • Pannexin1 and pannexin3 delivery, cell surface dynamics, and cytoskeletal interactions
    • R. Bhalla-Gehi, S. Penuela, J.M. Churko, Q. Shao, and D.W. Laird Pannexin1 and pannexin3 delivery, cell surface dynamics, and cytoskeletal interactions J. Biol. Chem. 285 2010 9147 9160
    • (2010) J. Biol. Chem. , vol.285 , pp. 9147-9160
    • Bhalla-Gehi, R.1    Penuela, S.2    Churko, J.M.3    Shao, Q.4    Laird, D.W.5
  • 48
    • 67349209224 scopus 로고    scopus 로고
    • The role of the cytoskeleton in the formation of gap junctions by Connexin 30
    • C. Qu, P. Gardner, and I. Schrijver The role of the cytoskeleton in the formation of gap junctions by Connexin 30 Exp. Cell Res. 315 2009 1683 1692
    • (2009) Exp. Cell Res. , vol.315 , pp. 1683-1692
    • Qu, C.1    Gardner, P.2    Schrijver, I.3
  • 49
    • 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
    • Y. Yamane, H. Shiga, H. Asou, H. Haga, K. Kawabata, K. Abe, and E. Ito 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
  • 50
    • 1942445036 scopus 로고    scopus 로고
    • Drebrin is a novel connexin-43 binding partner that links gap junctions to the submembrane cytoskeleton
    • E. Butkevich, S. Hulsmann, D. Wenzel, T. Shirao, R. Duden, and I. Majoul Drebrin is a novel connexin-43 binding partner that links gap junctions to the submembrane cytoskeleton Curr. Biol. 14 2004 650 658
    • (2004) Curr. Biol. , vol.14 , pp. 650-658
    • Butkevich, E.1    Hulsmann, S.2    Wenzel, D.3    Shirao, T.4    Duden, R.5    Majoul, I.6
  • 53
    • 0035754494 scopus 로고    scopus 로고
    • Connexin-43 interactions with ZO-1 and alpha- and beta-tubulin
    • B.N. Giepmans, I. Verlaan, and W.H. Moolenaar 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
  • 55
    • 39849084350 scopus 로고    scopus 로고
    • Structural and functional associations of apical junctions with cytoskeleton
    • J. Miyoshi, and Y. Takai Structural and functional associations of apical junctions with cytoskeleton Biochim. Biophys. Acta 1778 2008 670 691
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 670-691
    • Miyoshi, J.1    Takai, Y.2
  • 56
    • 39849100440 scopus 로고    scopus 로고
    • Adherens and tight junctions: Structure, function and connections to the actin cytoskeleton
    • A. Hartsock, and W.J. Nelson Adherens and tight junctions: structure, function and connections to the actin cytoskeleton Biochim. Biophys. Acta 1778 2008 660 669
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 660-669
    • Hartsock, A.1    Nelson, W.J.2
  • 57
    • 39849103311 scopus 로고    scopus 로고
    • The cytoplasmic plaque of tight junctions: A scaffolding and signalling center
    • L. Guillemot, S. Paschoud, P. Pulimeno, A. Foglia, and S. Citi The cytoplasmic plaque of tight junctions: a scaffolding and signalling center Biochim. Biophys. Acta 1778 2008 601 613
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 601-613
    • Guillemot, L.1    Paschoud, S.2    Pulimeno, P.3    Foglia, A.4    Citi, S.5
  • 59
    • 0032557460 scopus 로고    scopus 로고
    • Direct association of the gap junction protein connexin-43 with ZO-1 in cardiac myocytes
    • T. Toyofuku, M. Yabuki, K. Otsu, T. Kuzuya, M. Hori, and M. Tada 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
  • 60
    • 13144252170 scopus 로고    scopus 로고
    • The gap junction protein connexin43 interacts with the second PDZ domain of the zona occludens-1 protein
    • B.N. Giepmans, and W.H. Moolenaar 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
  • 61
    • 21044440344 scopus 로고    scopus 로고
    • Quantitative analysis of ZO-1 colocalization with Cx43 gap junction plaques in cultures of rat neonatal cardiomyocytes
    • C. Zhu, R.J. Barker, A.W. Hunter, Y. Zhang, J. Jourdan, and R.G. Gourdie Quantitative analysis of ZO-1 colocalization with Cx43 gap junction plaques in cultures of rat neonatal cardiomyocytes Microsc. Microanal. 11 2005 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
  • 62
    • 28644434657 scopus 로고    scopus 로고
    • Zonula occludens-1 alters connexin43 gap junction size and organization by influencing channel accretion
    • A.W. Hunter, R.J. Barker, C. Zhu, and R.G. Gourdie Zonula occludens-1 alters connexin43 gap junction size and organization by influencing channel accretion Mol. Biol. Cell 16 2005 5686 5698
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5686-5698
    • Hunter, A.W.1    Barker, R.J.2    Zhu, C.3    Gourdie, R.G.4
  • 64
    • 24044554201 scopus 로고    scopus 로고
    • Connexin 43 interacts with zona occludens-1 and -2 proteins in a cell cycle stage-specific manner
    • D. Singh, J.L. Solan, S.M. Taffet, R. Javier, and P.D. Lampe Connexin 43 interacts with zona occludens-1 and -2 proteins in a cell cycle stage-specific manner J. Biol. Chem. 280 2005 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
  • 65
    • 0035910415 scopus 로고    scopus 로고
    • C-Src regulates the interaction between connexin-43 and ZO-1 in cardiac myocytes
    • T. Toyofuku, Y. Akamatsu, H. Zhang, T. Kuzuya, M. Tada, and M. Hori 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
  • 66
    • 63249111743 scopus 로고    scopus 로고
    • Epithelial cell-cell junctions and plasma membrane domains
    • B.N. Giepmans, and S.C. van Ijzendoorn Epithelial cell-cell junctions and plasma membrane domains Biochim. Biophys. Acta 1788 2009 820 831
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 820-831
    • Giepmans, B.N.1    Van Ijzendoorn, S.C.2
  • 68
    • 0035864383 scopus 로고    scopus 로고
    • Cx32 but not Cx26 is associated with tight junctions in primary cultures of rat hepatocytes
    • T. Kojima, Y. Kokai, H. Chiba, M. Yamamoto, Y. Mochizuki, and N. Sawada 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
  • 69
    • 0034703027 scopus 로고    scopus 로고
    • The coiled-coil domain of occludin can act to organize structural and functional elements of the epithelial tight junction
    • A. Nusrat, J.A. Chen, C.S. Foley, T.W. Liang, J. Tom, M. Cromwell, C. Quan, and R.J. Mrsny 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
  • 71
    • 33744908040 scopus 로고    scopus 로고
    • Possible involvement of gap junctions in the barrier function of tight junctions of brain and lung endothelial cells
    • K. Nagasawa, H. Chiba, H. Fujita, T. Kojima, T. Saito, T. Endo, and N. Sawada Possible involvement of gap junctions in the barrier function of tight junctions of brain and lung endothelial cells J. Cell. Physiol. 208 2006 123 132
    • (2006) J. Cell. Physiol. , vol.208 , pp. 123-132
    • Nagasawa, K.1    Chiba, H.2    Fujita, H.3    Kojima, T.4    Saito, T.5    Endo, T.6    Sawada, N.7
  • 72
    • 53949111787 scopus 로고    scopus 로고
    • Ablation of Cx47 in transgenic mice leads to the loss of MUPP1, ZONAB and multiple connexins at oligodendrocyte-astrocyte gap junctions
    • X. Li, M. Penes, B. Odermatt, K. Willecke, and J.I. Nagy Ablation of Cx47 in transgenic mice leads to the loss of MUPP1, ZONAB and multiple connexins at oligodendrocyte-astrocyte gap junctions Eur. J. Neurosci. 28 2008 1503 1517
    • (2008) Eur. J. Neurosci. , vol.28 , pp. 1503-1517
    • Li, X.1    Penes, M.2    Odermatt, B.3    Willecke, K.4    Nagy, J.I.5
  • 73
    • 77953878405 scopus 로고    scopus 로고
    • Adherens junctions: From molecules to morphogenesis
    • T.J. Harris, and U. Tepass Adherens junctions: from molecules to morphogenesis Nat. Rev. Mol. Cell Biol. 11 2010 502 514
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 502-514
    • Harris, T.J.1    Tepass, U.2
  • 74
    • 39849088124 scopus 로고    scopus 로고
    • Molecular components of the adherens junction
    • C.M. Niessen, and C.J. Gottardi Molecular components of the adherens junction Biochim. Biophys. Acta 1778 2008 562 571
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 562-571
    • Niessen, C.M.1    Gottardi, C.J.2
  • 75
    • 21244490447 scopus 로고    scopus 로고
    • Connexin43 associated with an N-cadherin-containing multiprotein complex is required for gap junction formation in NIH3T3 cells
    • C.J. Wei, R. Francis, X. Xu, and C.W. Lo Connexin43 associated with an N-cadherin-containing multiprotein complex is required for gap junction formation in NIH3T3 cells J. Biol. Chem. 280 2005 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
  • 76
    • 33846695393 scopus 로고    scopus 로고
    • Microtubule plus-end-tracking proteins target gap junctions directly from the cell interior to adherens junctions
    • R.M. Shaw, A.J. Fay, M.A. Puthenveedu, M. von Zastrow, Y.N. Jan, and L.Y. Jan Microtubule plus-end-tracking proteins target gap junctions directly from the cell interior to adherens junctions Cell 128 2007 547 560
    • (2007) Cell , vol.128 , pp. 547-560
    • Shaw, R.M.1    Fay, A.J.2    Puthenveedu, M.A.3    Von Zastrow, M.4    Jan, Y.N.5    Jan, L.Y.6
  • 78
    • 0037371343 scopus 로고    scopus 로고
    • Role of catenins in the development of gap junctions in rat cardiomyocytes
    • J.C. Wu, R.Y. Tsai, and T.H. Chung 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
  • 79
    • 33750379847 scopus 로고    scopus 로고
    • Connexin 43-mediated modulation of polarized cell movement and the directional migration of cardiac neural crest cells
    • X. Xu, R. Francis, C.J. Wei, K.L. Linask, and C.W. Lo Connexin 43-mediated modulation of polarized cell movement and the directional migration of cardiac neural crest cells Development 133 2006 3629 3639
    • (2006) Development , vol.133 , pp. 3629-3639
    • Xu, X.1    Francis, R.2    Wei, C.J.3    Linask, K.L.4    Lo, C.W.5
  • 80
    • 2542471450 scopus 로고    scopus 로고
    • Gap junction channel protein innexin 2 is essential for epithelial morphogenesis in the Drosophila embryo
    • R. Bauer, C. Lehmann, J. Martini, F. Eckardt, and M. Hoch Gap junction channel protein innexin 2 is essential for epithelial morphogenesis in the Drosophila embryo Mol. Biol. Cell 15 2004 2992 3004
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2992-3004
    • Bauer, R.1    Lehmann, C.2    Martini, J.3    Eckardt, F.4    Hoch, M.5
  • 81
    • 4644348991 scopus 로고    scopus 로고
    • Tyrosine-phosphorylated and nonphosphorylated sodium channel beta1 subunits are differentially localized in cardiac myocytes
    • J.D. Malhotra, V. Thyagarajan, C. Chen, and L.L. Isom Tyrosine-phosphorylated and nonphosphorylated sodium channel beta1 subunits are differentially localized in cardiac myocytes J. Biol. Chem. 279 2004 40748 40754
    • (2004) J. Biol. Chem. , vol.279 , pp. 40748-40754
    • Malhotra, J.D.1    Thyagarajan, V.2    Chen, C.3    Isom, L.L.4
  • 82
    • 20444505236 scopus 로고    scopus 로고
    • Developmental regulation of the direct interaction between the intracellular loop of connexin 45.6 and the C terminus of major intrinsic protein (aquaporin-0)
    • X.S. Yu, X. Yin, E.M. Lafer, and J.X. Jiang Developmental regulation of the direct interaction between the intracellular loop of connexin 45.6 and the C terminus of major intrinsic protein (aquaporin-0) J. Biol. Chem. 280 2005 22081 22090
    • (2005) J. Biol. Chem. , vol.280 , pp. 22081-22090
    • Yu, X.S.1    Yin, X.2    Lafer, E.M.3    Jiang, J.X.4
  • 83
    • 79251560605 scopus 로고    scopus 로고
    • Aquaporin 0 enhances gap junction coupling via its cell adhesion function and interaction with connexin 50
    • J. Liu, J. Xu, S. Gu, B.J. Nicholson, and J.X. Jiang Aquaporin 0 enhances gap junction coupling via its cell adhesion function and interaction with connexin 50 J. Cell Sci. 124 2011 198 206
    • (2011) J. Cell Sci. , vol.124 , pp. 198-206
    • Liu, J.1    Xu, J.2    Gu, S.3    Nicholson, B.J.4    Jiang, J.X.5
  • 84
    • 33644993662 scopus 로고    scopus 로고
    • Ischemia impairs the association between connexin 43 and M3 subtype of acetylcholine muscarinic receptor (M3-mAChR) in ventricular myocytes
    • P. Yue, Y. Zhang, Z. Du, J. Xiao, Z. Pan, N. Wang, H. Yu, W. Ma, H. Qin, W.H. Wang, D.H. Lin, and B. Yang Ischemia impairs the association between connexin 43 and M3 subtype of acetylcholine muscarinic receptor (M3-mAChR) in ventricular myocytes Cell. Physiol. Biochem. 17 2006 129 136
    • (2006) Cell. Physiol. Biochem. , vol.17 , pp. 129-136
    • Yue, P.1    Zhang, Y.2    Du, Z.3    Xiao, J.4    Pan, Z.5    Wang, N.6    Yu, H.7    Ma, W.8    Qin, H.9    Wang, W.H.10    Lin, D.H.11    Yang, B.12
  • 85
    • 2942591296 scopus 로고    scopus 로고
    • High-resolution proteomic mapping in the vertebrate central nervous system: Close proximity of connexin35 to NMDA glutamate receptor clusters and co-localization of connexin36 with immunoreactivity for zonula occludens protein-1 (ZO-1)
    • J.E. Rash, A. Pereda, N. Kamasawa, C.S. Furman, T. Yasumura, K.G. Davidson, F.E. Dudek, C. Olson, X. Li, and J.I. Nagy High-resolution proteomic mapping in the vertebrate central nervous system: close proximity of connexin35 to NMDA glutamate receptor clusters and co-localization of connexin36 with immunoreactivity for zonula occludens protein-1 (ZO-1) J. Neurocytol. 33 2004 131 151
    • (2004) J. Neurocytol. , vol.33 , pp. 131-151
    • Rash, J.E.1    Pereda, A.2    Kamasawa, N.3    Furman, C.S.4    Yasumura, T.5    Davidson, K.G.6    Dudek, F.E.7    Olson, C.8    Li, X.9    Nagy, J.I.10
  • 88
    • 33750473352 scopus 로고    scopus 로고
    • Pannexin-1 mediates large pore formation and interleukin-1beta release by the ATP-gated P2X7 receptor
    • P. Pelegrin, and A. Surprenant Pannexin-1 mediates large pore formation and interleukin-1beta release by the ATP-gated P2X7 receptor EMBO J. 25 2006 5071 5082
    • (2006) EMBO J. , vol.25 , pp. 5071-5082
    • Pelegrin, P.1    Surprenant, A.2
  • 90
    • 0036199229 scopus 로고    scopus 로고
    • Calmodulin as an ion channel subunit
    • S. Saimi, and C. Kung Calmodulin as an ion channel subunit Annu. Rev. Physiol. 64 2002 289 311
    • (2002) Annu. Rev. Physiol. , vol.64 , pp. 289-311
    • Saimi, S.1    Kung, C.2
  • 91
    • 0021063967 scopus 로고
    • Is calmodulin involved in the regulation of gap junction permeability ?
    • C. Peracchia, G. Bernardini, and L.L. Peracchia 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
  • 92
    • 0021952348 scopus 로고
    • Interaction of calmodulin and other calcium-modulated proteins with mammalian and arthropod junctional membrane proteins
    • L.J. Van Eldik, E.L. Hertzberg, R.C. Berdan, and N.B. Gilula 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
  • 93
    • 0030773116 scopus 로고    scopus 로고
    • Connexin 32 of gap junctions contains two cytoplasmic calmodulin-binding domains
    • K. Török, K. Stauffer, and W.H. Evans 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
  • 94
    • 23744486999 scopus 로고    scopus 로고
    • Role of intramolecular interaction in connexin50: Mediating the Ca2 +-dependent binding of calmodulin to gap junction
    • X. Zhang, and Y. Qi Role of intramolecular interaction in connexin50: mediating the Ca2 +-dependent binding of calmodulin to gap junction Arch. Biochem. Biophys. 440 2005 111 117
    • (2005) Arch. Biochem. Biophys. , vol.440 , pp. 111-117
    • Zhang, X.1    Qi, Y.2
  • 95
    • 1942503184 scopus 로고    scopus 로고
    • Gap junctions and connexin-interacting proteins
    • B.N. Giepmans Gap junctions and connexin-interacting proteins Cardiovasc. Res. 62 2004 233 245
    • (2004) Cardiovasc. Res. , vol.62 , pp. 233-245
    • Giepmans, B.N.1
  • 96
    • 4344687590 scopus 로고    scopus 로고
    • Is the junctional uncoupling elicited in rat ventricular myocytes by some dephosphorylation treatments due to changes in the phosphorylation status of Cx43?
    • J.C. Hervé, I. Plaisance, J. Loncarek, D. Duthe, and D. Sarrouilhe Is the junctional uncoupling elicited in rat ventricular myocytes by some dephosphorylation treatments due to changes in the phosphorylation status of Cx43? Eur. Biophys. J. 33 2004 201 210
    • (2004) Eur. Biophys. J. , vol.33 , pp. 201-210
    • Hervé, J.C.1    Plaisance, I.2    Loncarek, J.3    Duthe, D.4    Sarrouilhe, D.5
  • 97
    • 20444411484 scopus 로고    scopus 로고
    • Connexin phosphorylation as a regulatory event linked to gap junction channel assembly
    • J.L. Solan, and P.D. Lampe Connexin phosphorylation as a regulatory event linked to gap junction channel assembly Biochim. Biophys. Acta 1711 2005 154 163
    • (2005) Biochim. Biophys. Acta , vol.1711 , pp. 154-163
    • Solan, J.L.1    Lampe, P.D.2
  • 98
    • 34249014302 scopus 로고    scopus 로고
    • Gap junction channel gating modulated through protein phosphorylation
    • A.P. Moreno, and A.F. Lau Gap junction channel gating modulated through protein phosphorylation Prog. Biophys. Mol. Biol. 94 2007 107 119
    • (2007) Prog. Biophys. Mol. Biol. , vol.94 , pp. 107-119
    • Moreno, A.P.1    Lau, A.F.2
  • 99
    • 0032588111 scopus 로고    scopus 로고
    • v-src and the gap-junction protein connexin 43 in v-src-transformed fibroblasts
    • v-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
  • 100
    • 0035896527 scopus 로고    scopus 로고
    • Interaction of c-Src with gap junction protein connexin-43. Role in the regulation of cell-cell communication
    • B.N. Giepmans, T. Hengeveld, F.R. Postma, and W.H. Moolenaar 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
  • 102
    • 0033621884 scopus 로고    scopus 로고
    • The epsilon subtype of protein kinase C is required for cardiomyocyte connexin-43 phosphorylation
    • B.W. Doble, P. Ping, and E. Kardami 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
  • 104
    • 27244457253 scopus 로고    scopus 로고
    • Regulation of lens cell-to-cell communication by activation of PKCgamma and disassembly of Cx50 channels
    • G.A. Zampighi, A.M. Planells, D. Lin, and D. Takemoto Regulation of lens cell-to-cell communication by activation of PKCgamma and disassembly of Cx50 channels Invest. Ophthalmol. Vis. Sci. 46 2005 3247 3255
    • (2005) Invest. Ophthalmol. Vis. Sci. , vol.46 , pp. 3247-3255
    • Zampighi, G.A.1    Planells, A.M.2    Lin, D.3    Takemoto, D.4
  • 105
    • 36348932857 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha-induced anterior pituitary folliculostellate TtT/GF cell uncoupling is mediated by connexin 43 dephosphorylation
    • M.A. Meilleur, C.D. Akpovi, R.M. Pelletier, and M.L. Vitale Tumor necrosis factor-alpha-induced anterior pituitary folliculostellate TtT/GF cell uncoupling is mediated by connexin 43 dephosphorylation Endocrinology 148 2007 5913 5924
    • (2007) Endocrinology , vol.148 , pp. 5913-5924
    • Meilleur, M.A.1    Akpovi, C.D.2    Pelletier, R.M.3    Vitale, M.L.4
  • 106
    • 0036727092 scopus 로고    scopus 로고
    • Myotonic dystrophy protein kinase of the cardiac muscle: Evaluation using an immunochemical approach
    • G. Schiavon, S. Furlan, O. Marin, and S. Salvatori 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
  • 107
    • 14844330674 scopus 로고    scopus 로고
    • Regulation of connexin43-protein binding in astrocytes in response to chemical ischemia/hypoxia
    • W. Li, E.L. Hertzberg, and D.C. Spray Regulation of connexin43-protein binding in astrocytes in response to chemical ischemia/hypoxia J. Biol. Chem. 280 2005 7941 7948
    • (2005) J. Biol. Chem. , vol.280 , pp. 7941-7948
    • Li, W.1    Hertzberg, E.L.2    Spray, D.C.3
  • 109
    • 77954724789 scopus 로고    scopus 로고
    • Variability of distribution of Ca(2 +)/calmodulin-dependent kinase II at mixed synapses on the mauthner cell: Colocalization and association with connexin 35
    • C.E. Flores, R. Cachope, S. Nannapaneni, S. Ene, A.C. Nairn, and A.E. Pereda Variability of distribution of Ca(2 +)/calmodulin-dependent kinase II at mixed synapses on the mauthner cell: colocalization and association with connexin 35 J. Neurosci. 30 2010 9488 9499
    • (2010) J. Neurosci. , vol.30 , pp. 9488-9499
    • Flores, C.E.1    Cachope, R.2    Nannapaneni, S.3    Ene, S.4    Nairn, A.C.5    Pereda, A.E.6
  • 110
    • 28344452986 scopus 로고    scopus 로고
    • Protein phosphatase modulation of the intercellular junctional communication: Importance in cardiac myocytes
    • J.C. Hervé, and D. Sarrouilhe Protein phosphatase modulation of the intercellular junctional communication: importance in cardiac myocytes Prog. Biophys. Mol. Biol. 90 2006 225 248
    • (2006) Prog. Biophys. Mol. Biol. , vol.90 , pp. 225-248
    • Hervé, J.C.1    Sarrouilhe, D.2
  • 111
    • 11844254718 scopus 로고    scopus 로고
    • Connexin 43 downregulation and dephosphorylation in nonischemic heart failure is associated with enhanced colocalized protein phosphatase type 2A
    • X. Ai, and S.M. Pogwizd Connexin 43 downregulation and dephosphorylation in nonischemic heart failure is associated with enhanced colocalized protein phosphatase type 2A Circ. Res. 96 2005 54 63
    • (2005) Circ. Res. , vol.96 , pp. 54-63
    • Ai, X.1    Pogwizd, S.M.2
  • 112
    • 33749386740 scopus 로고    scopus 로고
    • Ubiquitin protein ligase Nedd4 binds to connexin43 by a phosphorylation-modulated process
    • K. Leykauf, M. Salek, J. Bomke, M. Frech, W.D. Lehmann, M. Durst, and A. Alonso Ubiquitin protein ligase Nedd4 binds to connexin43 by a phosphorylation-modulated process J. Cell Sci. 119 2006 3634 3642
    • (2006) J. Cell Sci. , vol.119 , pp. 3634-3642
    • Leykauf, K.1    Salek, M.2    Bomke, J.3    Frech, M.4    Lehmann, W.D.5    Durst, M.6    Alonso, A.7
  • 115
    • 0037035519 scopus 로고    scopus 로고
    • Connexin family members target to lipid raft domains and interact with caveolin-1
    • A.L. Schubert, W. Schubert, D.C. Spray, and M.P. Lisanti 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
  • 116
    • 0344420042 scopus 로고    scopus 로고
    • Protein kinase C gamma regulation of gap junction activity through caveolin-1-containing lipid rafts
    • D. Lin, J. Zhou, P.S. Zelenka, and D.J. Takemoto Protein kinase C gamma regulation of gap junction activity through caveolin-1-containing lipid rafts Invest. Ophthalmol. Vis. Sci. 44 2003 5259 5268
    • (2003) Invest. Ophthalmol. Vis. Sci. , vol.44 , pp. 5259-5268
    • Lin, D.1    Zhou, J.2    Zelenka, P.S.3    Takemoto, D.J.4
  • 117
    • 41649104490 scopus 로고    scopus 로고
    • Caveolin-1 and -2 interact with connexin43 and regulate gap junctional intercellular communication in keratinocytes
    • S. Langlois, K.N. Cowan, Q. Shao, B.J. Cowan, and D.W. Laird Caveolin-1 and -2 interact with connexin43 and regulate gap junctional intercellular communication in keratinocytes Mol. Biol. Cell 19 2008 912 928
    • (2008) Mol. Biol. Cell , vol.19 , pp. 912-928
    • Langlois, S.1    Cowan, K.N.2    Shao, Q.3    Cowan, B.J.4    Laird, D.W.5
  • 118
    • 24044527872 scopus 로고    scopus 로고
    • Molecular cloning and functional analysis of a novel Cx43 partner protein CIP150
    • M. Akiyama, N. Ishida, T. Ogawa, K. Yogo, and T. Takeya Molecular cloning and functional analysis of a novel Cx43 partner protein CIP150 Biochem. Biophys. Res. Commun. 335 2005 1264 1271
    • (2005) Biochem. Biophys. Res. Commun. , vol.335 , pp. 1264-1271
    • Akiyama, M.1    Ishida, N.2    Ogawa, T.3    Yogo, K.4    Takeya, T.5
  • 119
    • 14044272826 scopus 로고    scopus 로고
    • Novel rab GAP-like protein, CIP85, interacts with connexin43 and induces its degradation
    • Z. Lan, W.E. Kurata, K.D. Martyn, C. Jin, and A.F. Lau Novel rab GAP-like protein, CIP85, interacts with connexin43 and induces its degradation Biochemistry 44 2005 2385 2396
    • (2005) Biochemistry , vol.44 , pp. 2385-2396
    • Lan, Z.1    Kurata, W.E.2    Martyn, K.D.3    Jin, C.4    Lau, A.F.5
  • 120
    • 78650388517 scopus 로고    scopus 로고
    • Ubiquitin-independent proteasomal degradation of endoplasmic reticulum-localized connexin43 mediated by CIP75
    • V. Su, R. Nakagawa, M. Koval, and A.F. Lau Ubiquitin-independent proteasomal degradation of endoplasmic reticulum-localized connexin43 mediated by CIP75 J. Biol. Chem. 285 2010 40979 40990
    • (2010) J. Biol. Chem. , vol.285 , pp. 40979-40990
    • Su, V.1    Nakagawa, R.2    Koval, M.3    Lau, A.F.4
  • 121
  • 124
    • 4344644035 scopus 로고    scopus 로고
    • CCN3 (NOV) interacts with connexin43 in C6 glioma cells: Possible mechanism of connexin-mediated growth suppression
    • C.T. Fu, J.F. Bechberger, M.A. Ozog, B. Perbal, and C.C. Naus CCN3 (NOV) interacts with connexin43 in C6 glioma cells: possible mechanism of connexin-mediated growth suppression J. Biol. Chem. 279 2004 36943 36950
    • (2004) J. Biol. Chem. , vol.279 , pp. 36943-36950
    • Fu, C.T.1    Bechberger, J.F.2    Ozog, M.A.3    Perbal, B.4    Naus, C.C.5
  • 127
    • 34249050091 scopus 로고    scopus 로고
    • Molecular basis of voltage dependence of connexin channels: An integrative appraisal
    • D. González, J.M. Gómez-Hernández, and L.C. Barrio Molecular basis of voltage dependence of connexin channels: an integrative appraisal Prog. Biophys. Mol. Biol. 94 2007 66 106
    • (2007) Prog. Biophys. Mol. Biol. , vol.94 , pp. 66-106
    • González, D.1    Gómez-Hernández, J.M.2    Barrio, L.C.3
  • 128
    • 22144496843 scopus 로고    scopus 로고
    • Connexin43 PDZ2 binding domain mutants create functional gap junctions and exhibit altered phosphorylation
    • C. Jin, K.D. Martyn, W.E. Kurata, B.J. Warn-Cramer, and A.F. Lau Connexin43 PDZ2 binding domain mutants create functional gap junctions and exhibit altered phosphorylation Cell Commun. Adhes. 11 2004 67 87
    • (2004) Cell Commun. Adhes. , vol.11 , pp. 67-87
    • Jin, C.1    Martyn, K.D.2    Kurata, W.E.3    Warn-Cramer, B.J.4    Lau, A.F.5
  • 129
    • 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
    • P.L. Sorgen, H.S. Duffy, P. Sahoo, W. Coombs, M. Delmar, and D.C. Spray 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 2004 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
  • 130
    • 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
    • P.A. Nielsen, D.L. Beahm, B.N. Giepmans, A. Baruch, J.E. Hall, and N.M. Kumar 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
  • 131
    • 0035823043 scopus 로고    scopus 로고
    • Connexin45 directly binds to ZO-1 and localizes to the tight junction region in epithelial MDCK cells
    • P.J. Kausalya, M. Reichert, and W. Hunziker 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
  • 132
    • 0035750745 scopus 로고    scopus 로고
    • Characterization of the association of connexins and ZO-1 in the lens
    • P.A. Nielsen, A. Baruch, B.N. Giepmans, and N.M. Kumar Characterization of the association of connexins and ZO-1 in the lens Cell Commun. Adhes. 8 2001 213 217
    • (2001) Cell Commun. Adhes. , vol.8 , pp. 213-217
    • Nielsen, P.A.1    Baruch, A.2    Giepmans, B.N.3    Kumar, N.M.4
  • 133
    • 34249034245 scopus 로고    scopus 로고
    • Connexin47, connexin29 and connexin32 co-expression in oligodendrocytes and Cx47 association with zonula occludens-1 (ZO-1) in mouse brain
    • X. Li, A.V. Ionescu, B.D. Lynn, S. Lu, N. Kamasawa, M. Morita, K.G. Davidson, T. Yasumura, J.E. Rash, and J.I. Nagy Connexin47, connexin29 and connexin32 co-expression in oligodendrocytes and Cx47 association with zonula occludens-1 (ZO-1) in mouse brain Neuroscience 26 2004 11 30
    • (2004) Neuroscience , vol.26 , pp. 11-30
    • Li, X.1    Ionescu, A.V.2    Lynn, B.D.3    Lu, S.4    Kamasawa, N.5    Morita, M.6    Davidson, K.G.7    Yasumura, T.8    Rash, J.E.9    Nagy, J.I.10
  • 135
    • 12944263962 scopus 로고    scopus 로고
    • Association of connexin36 with zonula occludens-1 in HeLa cells, betaTC-3 cells, pancreas, and adrenal gland
    • X. Li, C. Olson, S. Lu, and J.I. Nagy Association of connexin36 with zonula occludens-1 in HeLa cells, betaTC-3 cells, pancreas, and adrenal gland Histochem. Cell Biol. 122 2004 485 498
    • (2004) Histochem. Cell Biol. , vol.122 , pp. 485-498
    • Li, X.1    Olson, C.2    Lu, S.3    Nagy, J.I.4
  • 136
    • 2342567031 scopus 로고    scopus 로고
    • Neuronal connexin36 association with zonula occludens-1 protein (ZO-1) in mouse brain and interaction with the first PDZ domain of ZO-1
    • X. Li, C. Olson, S. Lu, N. Kamasawa, T. Yasumura, J.E. Rash, and J.I. Nagy Neuronal connexin36 association with zonula occludens-1 protein (ZO-1) in mouse brain and interaction with the first PDZ domain of ZO-1 Eur. J. Neurosci. 19 2004 2132 2146
    • (2004) Eur. J. Neurosci. , vol.19 , 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
  • 137
    • 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
    • M. Itoh, M. Furuse, K. Morita, K. Kubota, M. Saitou, and S. Tsukita 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
  • 138
    • 33646495062 scopus 로고    scopus 로고
    • Association of connexin36 and zonula occludens-1 with zonula occludens-2 and the transcription factor zonula occludens-1-associated nucleic acid-binding protein at neuronal gap junctions in rodent retina
    • C. Ciolofan, X.B. Li, C. Olson, N. Kamasawa, B.R. Gebhardt, T. Yasumura, M. Morita, J.E. Rash, and J.I. Nagy Association of connexin36 and zonula occludens-1 with zonula occludens-2 and the transcription factor zonula occludens-1-associated nucleic acid-binding protein at neuronal gap junctions in rodent retina Neuroscience 140 2006 433 451
    • (2006) Neuroscience , vol.140 , pp. 433-451
    • Ciolofan, C.1    Li, X.B.2    Olson, C.3    Kamasawa, N.4    Gebhardt, B.R.5    Yasumura, T.6    Morita, M.7    Rash, J.E.8    Nagy, J.I.9
  • 139
    • 37249013014 scopus 로고    scopus 로고
    • The C-terminus of connexin43 adopts different conformations in the Golgi and gap junction as detected with structure-specific antibodies
    • G.E. Sosinsky, S.L. Solan, G.M. Gaietta, L. Ngan, G.J. Lee, M.R. Mackey, and P.D. Lampe The C-terminus of connexin43 adopts different conformations in the Golgi and gap junction as detected with structure-specific antibodies Biochem. J. 408 2007 375 385
    • (2007) Biochem. J. , vol.408 , pp. 375-385
    • Sosinsky, G.E.1    Solan, S.L.2    Gaietta, G.M.3    Ngan, L.4    Lee, G.J.5    MacKey, M.R.6    Lampe, P.D.7
  • 140
    • 32144443312 scopus 로고    scopus 로고
    • Association with ZO-1 correlates with plasma membrane partitioning in truncated Connexin45 mutants
    • J.G. Laing, M. Koval, and T.H. Steinberg Association with ZO-1 correlates with plasma membrane partitioning in truncated Connexin45 mutants J. Membr. Biol. 207 2005 45 53
    • (2005) J. Membr. Biol. , vol.207 , pp. 45-53
    • Laing, J.G.1    Koval, M.2    Steinberg, T.H.3
  • 144
  • 145
    • 1642321958 scopus 로고    scopus 로고
    • Regulation of gap junctions by tyrosine protein kinases
    • B.J. Warn-Cramer, and A.F. Lau Regulation of gap junctions by tyrosine protein kinases Biochim. Biophys. Acta 1662 2004 81 95
    • (2004) Biochim. Biophys. Acta , vol.1662 , pp. 81-95
    • Warn-Cramer, B.J.1    Lau, A.F.2
  • 146
    • 0033950079 scopus 로고    scopus 로고
    • The importance of being proline: The interaction of proline-rich motifs in signaling proteins with their cognate domains
    • B.K. Kay, M.P. Williamson, and M. Sudol 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
  • 147
    • 0032543289 scopus 로고    scopus 로고
    • A 17mer peptide interferes with acidification-induced uncoupling of connexin43
    • G. Calero, M. Kanemitsu, S.M. Taffet, A.F. Lau, and M. Delmar A 17mer 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
  • 148
    • 48449099842 scopus 로고    scopus 로고
    • Structural changes in the carboxyl terminus of the gap junction protein connexin 40 caused by the interaction with c-Src and zonula occludens-1
    • D. Bouvier, F. Kieken, A. Kellezi, and P.L. Sorgen Structural changes in the carboxyl terminus of the gap junction protein connexin 40 caused by the interaction with c-Src and zonula occludens-1 Cell Commun. Adhes. 15 2008 107 118
    • (2008) Cell Commun. Adhes. , vol.15 , pp. 107-118
    • Bouvier, D.1    Kieken, F.2    Kellezi, A.3    Sorgen, P.L.4
  • 149
    • 79957606971 scopus 로고    scopus 로고
    • The identification of novel protein, brain-derived integrating factor-1 (BDIF1), which interacts with astrocytic gap junctional protein
    • T. Ito, T. Ueki, H. Furukawa, and K. Sato The identification of novel protein, brain-derived integrating factor-1 (BDIF1), which interacts with astrocytic gap junctional protein Neurosci. Res. 70 2011 330 333
    • (2011) Neurosci. Res. , vol.70 , pp. 330-333
    • Ito, T.1    Ueki, T.2    Furukawa, H.3    Sato, K.4
  • 150
    • 41949131052 scopus 로고    scopus 로고
    • A novel connexin43-interacting protein, CIP75, which belongs to the UbL-UBA protein family, regulates the turnover of connexin43
    • X. Li, V. Su, W.E. Kurata, C. Jin, and A.F. Lau A novel connexin43-interacting protein, CIP75, which belongs to the UbL-UBA protein family, regulates the turnover of connexin43 J. Biol. Chem. 283 2008 5748 5759
    • (2008) J. Biol. Chem. , vol.283 , pp. 5748-5759
    • Li, X.1    Su, V.2    Kurata, W.E.3    Jin, C.4    Lau, A.F.5
  • 151
    • 0034234655 scopus 로고    scopus 로고
    • Targeting motifs and functional parameters governing the assembly of connexins into gap junctions
    • P.E. Martin, J. Steggles, C. Wilson, S. Ahmad, and W.H. Evans 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
  • 152
    • 0034826706 scopus 로고    scopus 로고
    • Assembly of gap junction channels: Mechanism, effects of calmodulin antagonists and identification of connexin oligomerization determinants
    • S. Ahmad, P.E. Martin, and W.H. Evans 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
  • 153
    • 79957603294 scopus 로고    scopus 로고
    • Asparagine 175 of connexin32 is a critical residue for docking and forming functional heterotypic gap junction channels with connexin26
    • S. Nakagawa, X.Q. Gong, S. Maeda, Y. Dong, Y. Misumi, T. Tsukihara, and D. Bai Asparagine 175 of connexin32 is a critical residue for docking and forming functional heterotypic gap junction channels with connexin26 J. Biol. Chem. 286 2011 19672 19681
    • (2011) J. Biol. Chem. , vol.286 , pp. 19672-19681
    • Nakagawa, S.1    Gong, X.Q.2    Maeda, S.3    Dong, Y.4    Misumi, Y.5    Tsukihara, T.6    Bai, D.7
  • 154
    • 34249995953 scopus 로고    scopus 로고
    • Anti-innexin 2 aptamers specifically inhibit the heterologous interaction of the innexin 2 and innexin 3 carboxyl-termini in vitro
    • M. Knieps, S. Herrmann, C. Lehmann, B. Löer, M. Hoch, and M. Famulok Anti-innexin 2 aptamers specifically inhibit the heterologous interaction of the innexin 2 and innexin 3 carboxyl-termini in vitro Biol. Chem. 388 2007 561 568
    • (2007) Biol. Chem. , vol.388 , pp. 561-568
    • Knieps, M.1    Herrmann, S.2    Lehmann, C.3    Löer, B.4    Hoch, M.5    Famulok, M.6
  • 155
    • 36348994843 scopus 로고    scopus 로고
    • The connexin turnover, an important modulating factor of the level of cell-to-cell junctional communication: Comparison with other integral membrane proteins
    • J.C. Hervé, M. Derangeon, B. Bahbouhi, M. Mesnil, and D. Sarrouilhe The connexin turnover, an important modulating factor of the level of cell-to-cell junctional communication: comparison with other integral membrane proteins J. Membr. Biol. 217 2007 21 33
    • (2007) J. Membr. Biol. , vol.217 , pp. 21-33
    • Hervé, J.C.1    Derangeon, M.2    Bahbouhi, B.3    Mesnil, M.4    Sarrouilhe, D.5
  • 156
    • 0035991948 scopus 로고    scopus 로고
    • Gap junctions: Structure and function
    • W.H. Evans, and P.E.M. Martin Gap junctions: structure and function Mol. Membr. Biol. 19 2002 121 136
    • (2002) Mol. Membr. Biol. , vol.19 , pp. 121-136
    • Evans, W.H.1    Martin, P.E.M.2
  • 159
    • 0036677449 scopus 로고    scopus 로고
    • Dynamic trafficking and delivery of connexons to the plasma membrane and accretion to gap junctions in living cells
    • U. Lauf, B.N. Giepmans, P. Lopez, S. Braconnot, S.C. Chen, and M.M. Falk 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
  • 162
    • 79955501784 scopus 로고    scopus 로고
    • Connexin 43 connexon to gap junction transition is regulated by zonula occludens-1
    • J.M. Rhett, J. Jourdan, and R.G. Gourdie Connexin 43 connexon to gap junction transition is regulated by zonula occludens-1 Mol. Biol. Cell 22 2011 1516 1528
    • (2011) Mol. Biol. Cell , vol.22 , pp. 1516-1528
    • Rhett, J.M.1    Jourdan, J.2    Gourdie, R.G.3
  • 163
    • 55749108015 scopus 로고    scopus 로고
    • Connexin45-containing neuronal gap junctions in rodent retina also contain connexin36 in both apposing hemiplaques, forming bihomotypic gap junctions, with scaffolding contributed by zonula occludens-1
    • X. Li, N. Kamasawa, C. Ciolofan, C.O. Olson, S. Lu, K.G. Davidson, T. Yasumura, R. Shigemoto, J.E. Rash, and J.I. Nagy Connexin45-containing neuronal gap junctions in rodent retina also contain connexin36 in both apposing hemiplaques, forming bihomotypic gap junctions, with scaffolding contributed by zonula occludens-1 J. Neurosci. 28 2008 9769 9789
    • (2008) J. Neurosci. , vol.28 , pp. 9769-9789
    • Li, X.1    Kamasawa, N.2    Ciolofan, C.3    Olson, C.O.4    Lu, S.5    Davidson, K.G.6    Yasumura, T.7    Shigemoto, R.8    Rash, J.E.9    Nagy, J.I.10
  • 164
    • 48449089725 scopus 로고    scopus 로고
    • The second PDZ domain of zonula occludens-1 is dispensable for targeting to connexin 43 gap junctions
    • A.W. Hunter, and R.G. Gourdie The second PDZ domain of zonula occludens-1 is dispensable for targeting to connexin 43 gap junctions Cell Commun. Adhes. 15 2008 55 63
    • (2008) Cell Commun. Adhes. , vol.15 , pp. 55-63
    • Hunter, A.W.1    Gourdie, R.G.2
  • 166
    • 34548186903 scopus 로고    scopus 로고
    • Gap junction adhesion is necessary for radial migration in the neocortex
    • L.A. Elias, D.D. Wang, and A.R. Kriegstein Gap junction adhesion is necessary for radial migration in the neocortex Nature 448 2007 901 907
    • (2007) Nature , vol.448 , pp. 901-907
    • Elias, L.A.1    Wang, D.D.2    Kriegstein, A.R.3
  • 167
    • 60149097598 scopus 로고    scopus 로고
    • Adhesive properties of connexin hemichannels
    • M.L. Cotrina, J.H. Lin, and M. Nedergaard Adhesive properties of connexin hemichannels Glia 56 2008 1791 1798
    • (2008) Glia , vol.56 , pp. 1791-1798
    • Cotrina, M.L.1    Lin, J.H.2    Nedergaard, M.3
  • 168
    • 79251572022 scopus 로고    scopus 로고
    • Connexon-mediated cell adhesion drives microtissue self-assembly
    • B. Bao, J. Jiang, T. Yanase, Y. Nishi, and J.R. Morgan Connexon-mediated cell adhesion drives microtissue self-assembly FASEB J. 25 2011 255 264
    • (2011) FASEB J. , vol.25 , pp. 255-264
    • Bao, B.1    Jiang, J.2    Yanase, T.3    Nishi, Y.4    Morgan, J.R.5
  • 169
    • 63249111750 scopus 로고    scopus 로고
    • Reciprocal influence of connexins and apical junction proteins on their expressions and functions
    • M. Derangeon, D.C. Spray, N. Bourmeyster, D. Sarrouilhe, and J.C. Hervé Reciprocal influence of connexins and apical junction proteins on their expressions and functions Biochim. Biophys. Acta 1788 2009 768 778
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 768-778
    • Derangeon, M.1    Spray, D.C.2    Bourmeyster, N.3    Sarrouilhe, D.4    Hervé, J.C.5
  • 170
    • 77951222414 scopus 로고    scopus 로고
    • E-cadherin differentially regulates the assembly of Connexin43 and Connexin32 into gap junctions in human squamous carcinoma cells
    • S. Chakraborty, S. Mitra, M.M. Falk, S.H. Caplan, M.J. Wheelock, K.R. Johnson, and P.P. Mehta E-cadherin differentially regulates the assembly of Connexin43 and Connexin32 into gap junctions in human squamous carcinoma cells J. Biol. Chem. 285 2010 10761 10776
    • (2010) J. Biol. Chem. , vol.285 , pp. 10761-10776
    • Chakraborty, S.1    Mitra, S.2    Falk, M.M.3    Caplan, S.H.4    Wheelock, M.J.5    Johnson, K.R.6    Mehta, P.P.7
  • 171
    • 78650151102 scopus 로고    scopus 로고
    • Assembly of connexin43 into gap junctions is regulated differentially by E-cadherin and N-cadherin in rat liver epithelial cells
    • R. Govindarajan, S. Chakraborty, K.E. Johnson, M.M. Falk, M.J. Wheelock, K.R. Johnson, and P.P. Mehta Assembly of connexin43 into gap junctions is regulated differentially by E-cadherin and N-cadherin in rat liver epithelial cells Mol. Biol. Cell 21 2010 4089 4107
    • (2010) Mol. Biol. Cell , vol.21 , pp. 4089-4107
    • Govindarajan, R.1    Chakraborty, S.2    Johnson, K.E.3    Falk, M.M.4    Wheelock, M.J.5    Johnson, K.R.6    Mehta, P.P.7
  • 173
    • 20444397355 scopus 로고    scopus 로고
    • Structural organization of gap junction channels
    • G.E. Sosinsky, and B.J. Nicholson Structural organization of gap junction channels Biochim. Biophys. Acta 1711 2005 99 125
    • (2005) Biochim. Biophys. Acta , vol.1711 , pp. 99-125
    • Sosinsky, G.E.1    Nicholson, B.J.2
  • 175
    • 0029020099 scopus 로고
    • Functional analysis of selective interactions among rodent connexins
    • T.W. White, D.L. Paul, D.A. Goodenough, and R. Bruzzone Functional analysis of selective interactions among rodent connexins Mol. Biol. Cell 6 1995 459 470
    • (1995) Mol. Biol. Cell , vol.6 , pp. 459-470
    • White, T.W.1    Paul, D.L.2    Goodenough, D.A.3    Bruzzone, R.4
  • 178
    • 34547784117 scopus 로고    scopus 로고
    • A cytoskeletal-based perimeter fence selectively corrals a sub-population of cell surface Kv2.1 channels
    • M.M. Tamkun, K.M. O'Connell, and A.S. Rolig A cytoskeletal-based perimeter fence selectively corrals a sub-population of cell surface Kv2.1 channels J. Cell Sci. 120 2007 2413 2423
    • (2007) J. Cell Sci. , vol.120 , pp. 2413-2423
    • Tamkun, M.M.1    O'Connell, K.M.2    Rolig, A.S.3
  • 179
    • 66049117301 scopus 로고    scopus 로고
    • ZO-1 and the spatial organization of gap junctions and glutamate receptors in the outer plexiform layer of the mammalian retina
    • P. Puller, L.P. de Sevilla Müller, U. Janssen-Bienhold, and S. Haverkamp ZO-1 and the spatial organization of gap junctions and glutamate receptors in the outer plexiform layer of the mammalian retina J. Neurosci. 29 2009 6266 6275
    • (2009) J. Neurosci. , vol.29 , pp. 6266-6275
    • Puller, P.1    De Sevilla Müller, L.P.2    Janssen-Bienhold, U.3    Haverkamp, S.4
  • 180
    • 33847687362 scopus 로고    scopus 로고
    • Role of an alternatively spliced form of alphaII-spectrin in localization of connexin 43 in cardiomyocytes and regulation by stress-activated protein kinase
    • J.A. Ursitti, B.G. Petrich, P.C. Lee, W.G. Resneck, X. Ye, J. Yang, W.R. Randall, R.J. Bloch, and Y. Wang Role of an alternatively spliced form of alphaII-spectrin in localization of connexin 43 in cardiomyocytes and regulation by stress-activated protein kinase J. Mol. Cell. Cardiol. 42 2007 572 581
    • (2007) J. Mol. Cell. Cardiol. , vol.42 , pp. 572-581
    • Ursitti, J.A.1    Petrich, B.G.2    Lee, P.C.3    Resneck, W.G.4    Ye, X.5    Yang, J.6    Randall, W.R.7    Bloch, R.J.8    Wang, Y.9
  • 182
    • 66149087287 scopus 로고    scopus 로고
    • Structural and molecular mechanisms of gap junction remodeling in epicardial border zone myocytes following myocardial infarction
    • F. Kieken, N. Mutsaers, E. Dolmatova, K. Virgil, A.L. Wit, A. Kellezi, B.J. Hirst-Jensen, H.S. Duffy, and P.L. Sorgen Structural and molecular mechanisms of gap junction remodeling in epicardial border zone myocytes following myocardial infarction Circ. Res. 104 2009 1103 1112
    • (2009) Circ. Res. , vol.104 , pp. 1103-1112
    • Kieken, F.1    Mutsaers, N.2    Dolmatova, E.3    Virgil, K.4    Wit, A.L.5    Kellezi, A.6    Hirst-Jensen, B.J.7    Duffy, H.S.8    Sorgen, P.L.9
  • 183
    • 20444381286 scopus 로고    scopus 로고
    • Functional consequences of heterogeneous gap junction channel formation and its influence in health and disease
    • G.T. Cottrell, and J.M. Burt Functional consequences of heterogeneous gap junction channel formation and its influence in health and disease Biochim. Biophys. Acta 1711 2005 126 141
    • (2005) Biochim. Biophys. Acta , vol.1711 , pp. 126-141
    • Cottrell, G.T.1    Burt, J.M.2
  • 185
    • 0014811573 scopus 로고
    • The recovery of resting potential and input resistance in sheep heart injured by knife or laser
    • J. Délèze The recovery of resting potential and input resistance in sheep heart injured by knife or laser J. Physiol. 208 1970 547 562
    • (1970) J. Physiol. , vol.208 , pp. 547-562
    • Délèze, J.1
  • 186
    • 55249113183 scopus 로고    scopus 로고
    • Calmodulin association with connexin32-derived peptides suggests trans-domain interaction in chemical gating of gap junction channels
    • R. Dodd, C. Peracchia, D. Stolady, and K. Török Calmodulin association with connexin32-derived peptides suggests trans-domain interaction in chemical gating of gap junction channels J. Biol. Chem. 283 2008 26911 26920
    • (2008) J. Biol. Chem. , vol.283 , pp. 26911-26920
    • Dodd, R.1    Peracchia, C.2    Stolady, D.3    Török, K.4
  • 187
    • 0033561399 scopus 로고    scopus 로고
    • ATP counteracts the rundown of gap junctional channels of rat ventricular myocytes by promoting protein phosphorylation
    • F. Verrecchia, F. Duthe, S. Duval, I. Duchatelle, D. Sarrouilhe, and J.C. Hervé 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    Duthe, F.2    Duval, S.3    Duchatelle, I.4    Sarrouilhe, D.5    Hervé, J.C.6
  • 188
    • 0023161934 scopus 로고
    • Dependence of junctional conductance on proton, calcium and magnesium ions in cardiac paired cells of guinea-pig
    • A. Noma, and N. Tsuboi 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
  • 193
    • 0018570734 scopus 로고
    • Evidence for the participation of actin microfilaments and bristle coats in the internalization of gap junction membrane
    • W.J. Larsen, H.N. Tung, S.A. Murray, and C.A. Swenson Evidence for the participation of actin microfilaments and bristle coats in the internalization of gap junction membrane J. Cell Biol. 83 1979 576 587
    • (1979) J. Cell Biol. , vol.83 , pp. 576-587
    • Larsen, W.J.1    Tung, H.N.2    Murray, S.A.3    Swenson, C.A.4
  • 194
    • 0037155043 scopus 로고    scopus 로고
    • Increased association of ZO-1 with connexin43 during remodeling of cardiac gap junctions
    • R.J. Barker, R.L. Price, and R.G. Gourdie Increased association of ZO-1 with connexin43 during remodeling of cardiac gap junctions Circ. Res. 90 2002 317 324
    • (2002) Circ. Res. , vol.90 , pp. 317-324
    • Barker, R.J.1    Price, R.L.2    Gourdie, R.G.3
  • 195
    • 59349109991 scopus 로고    scopus 로고
    • Molecular reorganization of Cx43, Zo-1 and Src complexes during the endocytosis of gap junction plaques in response to a non-genomic carcinogen
    • J. Gilleron, C. Fiorini, D. Carette, C. Avondet, M.M. Falk, D. Segretain, and G. Pointis Molecular reorganization of Cx43, Zo-1 and Src complexes during the endocytosis of gap junction plaques in response to a non-genomic carcinogen J. Cell Sci. 121 2008 4069 4078
    • (2008) J. Cell Sci. , vol.121 , pp. 4069-4078
    • Gilleron, J.1    Fiorini, C.2    Carette, D.3    Avondet, C.4    Falk, M.M.5    Segretain, D.6    Pointis, G.7
  • 196
    • 56649099046 scopus 로고    scopus 로고
    • Acute internalization of gap junctions in vascular endothelial cells in response to inflammatory mediator-induced G-protein coupled receptor activation
    • S.M. Baker, N. Kim, A.M. Gumpert, D. Segretain, and M.M. Falk Acute internalization of gap junctions in vascular endothelial cells in response to inflammatory mediator-induced G-protein coupled receptor activation FEBS Lett. 582 2008 4039 4046
    • (2008) FEBS Lett. , vol.582 , pp. 4039-4046
    • Baker, S.M.1    Kim, N.2    Gumpert, A.M.3    Segretain, D.4    Falk, M.M.5
  • 197
    • 67650599486 scopus 로고    scopus 로고
    • Connexin 43 gap junction plaque endocytosis implies molecular remodelling of ZO-1 and c-Src partners
    • J. Gilleron, D. Carette, C. Fiorini, M. Benkdane, D. Segretain, and G. Pointis Connexin 43 gap junction plaque endocytosis implies molecular remodelling of ZO-1 and c-Src partners Commun. Integr. Biol. 2 2009 104 106
    • (2009) Commun. Integr. Biol. , vol.2 , pp. 104-106
    • Gilleron, J.1    Carette, D.2    Fiorini, C.3    Benkdane, M.4    Segretain, D.5    Pointis, G.6
  • 198
    • 33947276680 scopus 로고    scopus 로고
    • ZO-1 is required for protein kinase C gamma-driven disassembly of connexin 43
    • V. Akoyev, and D.J. Takemoto ZO-1 is required for protein kinase C gamma-driven disassembly of connexin 43 Cell. Signal. 19 2007 958 967
    • (2007) Cell. Signal. , vol.19 , pp. 958-967
    • Akoyev, V.1    Takemoto, D.J.2
  • 201
    • 0028817813 scopus 로고
    • The gap junction protein connexin43 is degraded via the ubiquitin proteasome pathway
    • J.G. Laing, and E.C. Beyer 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
  • 202
    • 9244265420 scopus 로고    scopus 로고
    • Ubiquitination and down-regulation of gap junction protein connexin-43 in response to 12-O-tetradecanoylphorbol 13-acetate treatment
    • E. Leithe, and E. Rivedal Ubiquitination and down-regulation of gap junction protein connexin-43 in response to 12-O-tetradecanoylphorbol 13-acetate treatment J. Biol. Chem. 279 2004 50089 50096
    • (2004) J. Biol. Chem. , vol.279 , pp. 50089-50096
    • Leithe, E.1    Rivedal, E.2
  • 203
    • 1842426943 scopus 로고    scopus 로고
    • Epidermal growth factor regulates ubiquitination, internalization and proteasome-dependent degradation of connexin43
    • E. Leithe, and E. Rivedal Epidermal growth factor regulates ubiquitination, internalization and proteasome-dependent degradation of connexin43 J. Cell Sci. 117 2004 1211 1220
    • (2004) J. Cell Sci. , vol.117 , pp. 1211-1220
    • Leithe, E.1    Rivedal, E.2
  • 204
    • 70450277811 scopus 로고    scopus 로고
    • Ubiquitylation of the gap junction protein connexin-43 signals its trafficking from early endosomes to lysosomes in a process mediated by Hrs and Tsg101
    • E. Leithe, A. Kjenseth, S. Sirnes, H. Stenmark, A. Brech, and E. Rivedal Ubiquitylation of the gap junction protein connexin-43 signals its trafficking from early endosomes to lysosomes in a process mediated by Hrs and Tsg101 J. Cell Sci. 122 2009 3883 3893
    • (2009) J. Cell Sci. , vol.122 , pp. 3883-3893
    • Leithe, E.1    Kjenseth, A.2    Sirnes, S.3    Stenmark, H.4    Brech, A.5    Rivedal, E.6
  • 205
    • 67649834031 scopus 로고    scopus 로고
    • Connexin 43 and plakophilin-2 as a protein complex that regulates blood-testis barrier dynamics
    • M.W. Li, D.D. Mruk, W.M. Lee, and C.Y. Cheng Connexin 43 and plakophilin-2 as a protein complex that regulates blood-testis barrier dynamics Proc. Natl. Acad. Sci. U. S. A. 106 2009 10213 10218
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 10213-10218
    • Li, M.W.1    Mruk, D.D.2    Lee, W.M.3    Cheng, C.Y.4
  • 206
    • 78149242584 scopus 로고    scopus 로고
    • Connexin 43 is critical to maintain the homeostasis of the blood-testis barrier via its effects on tight junction reassembly
    • M.W. Li, D.D. Mruk, W.M. Lee, and C.Y. Cheng Connexin 43 is critical to maintain the homeostasis of the blood-testis barrier via its effects on tight junction reassembly Proc. Natl. Acad. Sci. U. S. A. 107 2010 17998 18003
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 17998-18003
    • Li, M.W.1    Mruk, D.D.2    Lee, W.M.3    Cheng, C.Y.4
  • 207
    • 80053047894 scopus 로고    scopus 로고
    • Connexin43 interacts with βarrestin: A pre-requisite for osteoblast survival induced by parathyroid hormone
    • N. Bivi, V. Lezcano, M. Romanello, T. Bellido, and L.L. Plotkin Connexin43 interacts with βarrestin: a pre-requisite for osteoblast survival induced by parathyroid hormone J. Cell. Biochem. 112 2011 2920 2930
    • (2011) J. Cell. Biochem. , vol.112 , pp. 2920-2930
    • Bivi, N.1    Lezcano, V.2    Romanello, M.3    Bellido, T.4    Plotkin, L.L.5
  • 208
    • 29344452180 scopus 로고    scopus 로고
    • Activation of pannexin 1 channels by ATP through P2Y receptors and by cytoplasmic calcium
    • S. Locovei, L. Bao, and G. Dahl Activation of pannexin 1 channels by ATP through P2Y receptors and by cytoplasmic calcium FEBS Lett. 580 2006 239 244
    • (2006) FEBS Lett. , vol.580 , pp. 239-244
    • Locovei, S.1    Bao, L.2    Dahl, G.3
  • 209
    • 33846438625 scopus 로고    scopus 로고
    • Pannexin1 is part of the pore forming unit of the P2X(7) receptor death complex
    • S. Locovei, E. Scemes, F. Qiu, D.C. Spray, and G. Dahl Pannexin1 is part of the pore forming unit of the P2X(7) receptor death complex FEBS Lett. 581 2007 483 488
    • (2007) FEBS Lett. , vol.581 , pp. 483-488
    • Locovei, S.1    Scemes, E.2    Qiu, F.3    Spray, D.C.4    Dahl, G.5
  • 211
    • 66149173401 scopus 로고    scopus 로고
    • Pannexin 1: The molecular substrate of astrocyte hemichannels
    • R. Iglesias, G. Dahl, F. Qiu, D.C. Spray, and E. Scemes Pannexin 1: the molecular substrate of astrocyte hemichannels J. Neurosci. 29 2009 7092 7097
    • (2009) J. Neurosci. , vol.29 , pp. 7092-7097
    • Iglesias, R.1    Dahl, G.2    Qiu, F.3    Spray, D.C.4    Scemes, E.5
  • 212
    • 77951928146 scopus 로고    scopus 로고
    • Pannexin-I/P2X 7 purinergic receptor channels mediate the release of cardioprotectants induced by ischemic pre- and postconditioning
    • D.A. Vessey, L. Li, and M. Kelley Pannexin-I/P2X 7 purinergic receptor channels mediate the release of cardioprotectants induced by ischemic pre- and postconditioning J. Cardiovasc. Pharmacol. Ther. 15 2010 190 195
    • (2010) J. Cardiovasc. Pharmacol. Ther. , vol.15 , pp. 190-195
    • Vessey, D.A.1    Li, L.2    Kelley, M.3
  • 213
    • 0034595219 scopus 로고    scopus 로고
    • The tight junction protein ZO-1 and an interacting transcription factor regulate ErbB-2 expression
    • M.S. Balda, and K. Matter The tight junction protein ZO-1 and an interacting transcription factor regulate ErbB-2 expression EMBO J. 19 2000 2024 2033
    • (2000) EMBO J. , vol.19 , pp. 2024-2033
    • Balda, M.S.1    Matter, K.2
  • 214
    • 0347986547 scopus 로고    scopus 로고
    • The tight junction protein ZO-2 associates with Jun, Fos and C/EBP transcription factors in epithelial cells
    • A. Betanzos, M. Huerta, E. Lopez-Bayghen, E. Azuara, J. Amerena, and L. González-Mariscal The tight junction protein ZO-2 associates with Jun, Fos and C/EBP transcription factors in epithelial cells Exp. Cell Res. 292 2004 51 66
    • (2004) Exp. Cell Res. , vol.292 , pp. 51-66
    • Betanzos, A.1    Huerta, M.2    Lopez-Bayghen, E.3    Azuara, E.4    Amerena, J.5    González-Mariscal, L.6
  • 215
    • 37349087184 scopus 로고    scopus 로고
    • C-terminal truncation of connexin43 changes number, size, and localization of cardiac gap junction plaques
    • K. Maass, J. Shibayama, S.E. Chase, K. Willecke, and M. Delmar C-terminal truncation of connexin43 changes number, size, and localization of cardiac gap junction plaques Circ. Res. 101 2007 1283 1291
    • (2007) Circ. Res. , vol.101 , pp. 1283-1291
    • Maass, K.1    Shibayama, J.2    Chase, S.E.3    Willecke, K.4    Delmar, M.5
  • 217
    • 34250373313 scopus 로고    scopus 로고
    • Cx43 mediates TGF-beta signaling through competitive Smads binding to microtubules
    • P. Dai, T. Nakagami, H. Tanaka, T. Hitomi, and T. Takamatsu Cx43 mediates TGF-beta signaling through competitive Smads binding to microtubules Mol. Biol. Cell 18 2007 2264 2273
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2264-2273
    • Dai, P.1    Nakagami, T.2    Tanaka, H.3    Hitomi, T.4    Takamatsu, T.5
  • 219
    • 64249170988 scopus 로고    scopus 로고
    • Connexin43 phosphorylation: Structural changes and biological effects
    • J.L. Solan, and P.D. Lampe Connexin43 phosphorylation: structural changes and biological effects Biochem. J. 419 2009 261 272
    • (2009) Biochem. J. , vol.419 , pp. 261-272
    • Solan, J.L.1    Lampe, P.D.2
  • 220
    • 0014021760 scopus 로고
    • Intercellular communication and the control of tissue growth: Lack of communication between cancer cells
    • W.R. Loewenstein, and Y. Kanno Intercellular communication and the control of tissue growth: lack of communication between cancer cells Nature 209 1966 1248 1249
    • (1966) Nature , vol.209 , pp. 1248-1249
    • Loewenstein, W.R.1    Kanno, Y.2
  • 222
    • 16344366009 scopus 로고    scopus 로고
    • The catenin p120ctn inhibits Kaiso-mediated transcriptional repression of the beta-catenin/TCF target gene matrilysin
    • C.M. Spring, K.F. Kelly, I. O'Kelly, M. Graham, H.C. Crawford, and J.M. Daniel The catenin p120ctn inhibits Kaiso-mediated transcriptional repression of the beta-catenin/TCF target gene matrilysin Exp. Cell Res. 305 2005 253 265
    • (2005) Exp. Cell Res. , vol.305 , pp. 253-265
    • Spring, C.M.1    Kelly, K.F.2    O'Kelly, I.3    Graham, M.4    Crawford, H.C.5    Daniel, J.M.6
  • 223
    • 61449254263 scopus 로고    scopus 로고
    • Direct association of connexin36 with zonula occludens-2 and zonula occludens-3
    • X. Li, S. Lu, and J.I. Nagy Direct association of connexin36 with zonula occludens-2 and zonula occludens-3 Neurochem. Int. 54 2009 393 402
    • (2009) Neurochem. Int. , vol.54 , pp. 393-402
    • Li, X.1    Lu, S.2    Nagy, J.I.3
  • 224
    • 70350243052 scopus 로고    scopus 로고
    • Connexins, cell motility, and the cytoskeleton
    • S. Olk, G. Zoidl, and R. Dermietzel Connexins, cell motility, and the cytoskeleton Cell Motil. Cytoskeleton 66 2009 1000 1016
    • (2009) Cell Motil. Cytoskeleton , vol.66 , pp. 1000-1016
    • Olk, S.1    Zoidl, G.2    Dermietzel, R.3
  • 225
    • 75749152627 scopus 로고    scopus 로고
    • Non-junction functions of pannexin-1 channels
    • B.A. MacVicar, and R.J. Thompson Non-junction functions of pannexin-1 channels Trends Neurosci. 33 2010 93 102
    • (2010) Trends Neurosci. , vol.33 , pp. 93-102
    • MacVicar, B.A.1    Thompson, R.J.2
  • 227
    • 78149326486 scopus 로고    scopus 로고
    • Pannexin-1 hemichannel-mediated ATP release together with P2X1 and P2X4 receptors regulate T-cell activation at the immune synapse
    • T. Woehrle, L. Yip, A. Elkhal, Y. Sumi, Y. Chen, Y. Yao, P.A. Insel, and W.G. Junger Pannexin-1 hemichannel-mediated ATP release together with P2X1 and P2X4 receptors regulate T-cell activation at the immune synapse Blood 116 2010 3475 3484
    • (2010) Blood , vol.116 , pp. 3475-3484
    • Woehrle, T.1    Yip, L.2    Elkhal, A.3    Sumi, Y.4    Chen, Y.5    Yao, Y.6    Insel, P.A.7    Junger, W.G.8
  • 228
    • 12344301871 scopus 로고    scopus 로고
    • Expression and function of connexins in the epidermis, analyzed with transgenic mouse mutants
    • M. Kretz, K. Maass, and K. Willecke Expression and function of connexins in the epidermis, analyzed with transgenic mouse mutants Eur. J. Cell Biol. 83 2004 647 654
    • (2004) Eur. J. Cell Biol. , vol.83 , pp. 647-654
    • Kretz, M.1    Maass, K.2    Willecke, K.3
  • 229
    • 0034961003 scopus 로고    scopus 로고
    • Trans-dominant inhibition of connexin-43 by mutant connexin-26: Implications for dominant connexin disorders affecting epidermal differentiation
    • F. Rouan, T.W. White, N. Brown, A.M. Taylor, T.W. Lucke, D.L. Paul, C.S. Munro, J. Uitto, M.B. Hodgins, and G. Richard Trans-dominant inhibition of connexin-43 by mutant connexin-26: implications for dominant connexin disorders affecting epidermal differentiation J. Cell Sci. 114 2001 2105 2113
    • (2001) J. Cell Sci. , vol.114 , pp. 2105-2113
    • Rouan, F.1    White, T.W.2    Brown, N.3    Taylor, A.M.4    Lucke, T.W.5    Paul, D.L.6    Munro, C.S.7    Uitto, J.8    Hodgins, M.B.9    Richard, G.10
  • 230
    • 2442502595 scopus 로고    scopus 로고
    • Functional domain mapping and selective trans-dominant effects exhibited by Cx26 disease-causing mutations
    • T. Thomas, D. Telford, and D.W. Laird Functional domain mapping and selective trans-dominant effects exhibited by Cx26 disease-causing mutations J. Biol. Chem. 279 2004 19157 19168
    • (2004) J. Biol. Chem. , vol.279 , pp. 19157-19168
    • Thomas, T.1    Telford, D.2    Laird, D.W.3
  • 234
    • 22144479749 scopus 로고    scopus 로고
    • Heterocellular contact at the myoendothelial junction influences gap junction organization
    • B.E. Isakson, and B.R. Duling Heterocellular contact at the myoendothelial junction influences gap junction organization Circ. Res. 97 2005 44 51
    • (2005) Circ. Res. , vol.97 , pp. 44-51
    • Isakson, B.E.1    Duling, B.R.2
  • 236
    • 23744463471 scopus 로고    scopus 로고
    • Dependence of electrical coupling on mechanical coupling in cardiac myocytes: Insights gained from cardiomyopathies caused by defects in cell-cell connections
    • J.E. Saffitz Dependence of electrical coupling on mechanical coupling in cardiac myocytes: insights gained from cardiomyopathies caused by defects in cell-cell connections Ann. N. Y. Acad. Sci. 1047 2005 336 344
    • (2005) Ann. N. Y. Acad. Sci. , vol.1047 , pp. 336-344
    • Saffitz, J.E.1
  • 238
    • 39749165131 scopus 로고    scopus 로고
    • Gap junction remodelling in human heart failure is associated with increased interaction of connexin43 with ZO-1
    • A.F. Bruce, S. Rothery, E. Dupont, and N.J. Severs Gap junction remodelling in human heart failure is associated with increased interaction of connexin43 with ZO-1 Cardiovasc. Res. 77 2008 757 765
    • (2008) Cardiovasc. Res. , vol.77 , pp. 757-765
    • Bruce, A.F.1    Rothery, S.2    Dupont, E.3    Severs, N.J.4
  • 241
    • 14044256554 scopus 로고    scopus 로고
    • Induced deletion of the N-cadherin gene in the heart leads to dissolution of the intercalated disc structure
    • I. Kostetskii, J. Li, Y. Xiong, R. Zhou, V.A. Ferrari, V.V. Patel, J.D. Molkentin, and G.L. Radice Induced deletion of the N-cadherin gene in the heart leads to dissolution of the intercalated disc structure Circ. Res. 96 2005 346 354
    • (2005) Circ. Res. , vol.96 , pp. 346-354
    • Kostetskii, I.1    Li, J.2    Xiong, Y.3    Zhou, R.4    Ferrari, V.A.5    Patel, V.V.6    Molkentin, J.D.7    Radice, G.L.8
  • 242
    • 0037089088 scopus 로고    scopus 로고
    • Remodeling the intercalated disc leads to cardiomyopathy in mice misexpressing cadherins in the heart
    • M.C. Ferreira-Cornwell, Y. Luo, N. Narula, J.M. Lenox, M. Lieberman, and G.L. Radice Remodeling the intercalated disc leads to cardiomyopathy in mice misexpressing cadherins in the heart J. Cell Sci. 115 2002 1623 1634
    • (2002) J. Cell Sci. , vol.115 , pp. 1623-1634
    • Ferreira-Cornwell, M.C.1    Luo, Y.2    Narula, N.3    Lenox, J.M.4    Lieberman, M.5    Radice, G.L.6
  • 243
    • 34548253988 scopus 로고    scopus 로고
    • Molecular composition of the intercalated disc in a spontaneous canine animal model of arrhythmogenic right ventricular dysplasia/cardiomyopathy
    • E.M. Oxford, M. Everitt, W. Coombs, P.R. Fox, M. Kraus, A.R. Gelzer, J. Saffitz, S.M. Taffet, N.S. Moïse, and M. Delmar Molecular composition of the intercalated disc in a spontaneous canine animal model of arrhythmogenic right ventricular dysplasia/cardiomyopathy Hear. Rhythm. 4 2007 1196 1205
    • (2007) Hear. Rhythm. , vol.4 , pp. 1196-1205
    • Oxford, E.M.1    Everitt, M.2    Coombs, W.3    Fox, P.R.4    Kraus, M.5    Gelzer, A.R.6    Saffitz, J.7    Taffet, S.M.8    Moïse, N.S.9    Delmar, M.10
  • 244
    • 50449098772 scopus 로고    scopus 로고
    • Interaction between connexin35 and zonula occludens-1 and its potential role in the regulation of electrical synapses
    • C.E. Flores, X. Li, M.V. Bennett, J.I. Nagy, and A.E. Pereda Interaction between connexin35 and zonula occludens-1 and its potential role in the regulation of electrical synapses Proc. Natl. Acad. Sci. U. S. A. 105 2008 12545 12550
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 12545-12550
    • Flores, C.E.1    Li, X.2    Bennett, M.V.3    Nagy, J.I.4    Pereda, A.E.5
  • 245
    • 1642377170 scopus 로고    scopus 로고
    • Gap junctions and neurological disorders of the central nervous system
    • T. Nakase, and C.C. Naus Gap junctions and neurological disorders of the central nervous system Biochim. Biophys. Acta 1662 2004 149 158
    • (2004) Biochim. Biophys. Acta , vol.1662 , pp. 149-158
    • Nakase, T.1    Naus, C.C.2
  • 246
    • 2342548650 scopus 로고    scopus 로고
    • Four classes of intercellular channels between glial cells in the CNS
    • B.M. Altevogt, and D.L. Paul Four classes of intercellular channels between glial cells in the CNS J. Neurosci. 24 2004 4313 4323
    • (2004) J. Neurosci. , vol.24 , pp. 4313-4323
    • Altevogt, B.M.1    Paul, D.L.2
  • 247
    • 0038351949 scopus 로고    scopus 로고
    • Connexins 26 and 30 are co-assembled to form gap junctions in the cochlea of mice
    • S. Ahmad, S. Chen, J. Sun, and X. Lin Connexins 26 and 30 are co-assembled to form gap junctions in the cochlea of mice Biochem. Biophys. Res. Commun. 307 2003 362 368
    • (2003) Biochem. Biophys. Res. Commun. , vol.307 , pp. 362-368
    • Ahmad, S.1    Chen, S.2    Sun, J.3    Lin, X.4
  • 249
    • 0033563283 scopus 로고    scopus 로고
    • Assembly of heteromeric connexons in guinea-pig liver en route to the Golgi apparatus, plasma membrane and gap junctions
    • J.A. Diez, S. Ahmad, and W.H. Evans Assembly of heteromeric connexons in guinea-pig liver en route to the Golgi apparatus, plasma membrane and gap junctions Eur. J. Biochem. 262 1999 142 148
    • (1999) Eur. J. Biochem. , vol.262 , pp. 142-148
    • Diez, J.A.1    Ahmad, S.2    Evans, W.H.3
  • 250
    • 0342944791 scopus 로고    scopus 로고
    • Electrophysiological properties of gap junction channels in hepatocytes isolated from connexin32-deficient and wild-type mice
    • V. Valiunas, H. Niessen, K. Willecke, and R. Weingart Electrophysiological properties of gap junction channels in hepatocytes isolated from connexin32-deficient and wild-type mice Pflügers Arch. 437 1999 846 856
    • (1999) Pflügers Arch. , vol.437 , pp. 846-856
    • Valiunas, V.1    Niessen, H.2    Willecke, K.3    Weingart, R.4
  • 251
    • 0034115524 scopus 로고    scopus 로고
    • Developmental expression and assembly of connexins into homomeric and heteromeric gap junction hemichannels in the mouse mammary gland
    • D. Locke, N. Perusinghe, T. Newman, H. Jayatilake, W.H. Evans, and P. Monaghan Developmental expression and assembly of connexins into homomeric and heteromeric gap junction hemichannels in the mouse mammary gland J. Cell. Physiol. 183 2000 228 237
    • (2000) J. Cell. Physiol. , vol.183 , pp. 228-237
    • Locke, D.1    Perusinghe, N.2    Newman, T.3    Jayatilake, H.4    Evans, W.H.5    Monaghan, P.6
  • 253
    • 33745190968 scopus 로고    scopus 로고
    • Heteromeric, but not homomeric, connexin channels are selectively permeable to inositol phosphates
    • W.A. Ayad, D., Locke, I.V., Koreen, A.L., Harris, Heteromeric, but not homomeric, connexin channels are selectively permeable to inositol phosphates. J. Biol. Chem. 281 (2006) 16727-16739.
    • (2006) J. Biol. Chem. , vol.281 , pp. 16727-16739
    • Ayad, W.A.D.1    Locke, I.V.2    Koreen, A.L.3    Harris4
  • 255
    • 0033546257 scopus 로고    scopus 로고
    • Multiple connexins form gap junction channels in rat basilar artery smooth muscle cells
    • X. Li, and J.M. Simard Multiple connexins form gap junction channels in rat basilar artery smooth muscle cells Circ. Res. 84 1999 1277 1284
    • (1999) Circ. Res. , vol.84 , pp. 1277-1284
    • Li, X.1    Simard, J.M.2
  • 256
    • 0036128134 scopus 로고    scopus 로고
    • Expression and regulation of connexins in cultured ventricular myocytes isolated from adult rat hearts
    • L.O. Polontchouk, V. Valiunas, J.A. Haefliger, H.M. Eppenberger, and R. Weingart Expression and regulation of connexins in cultured ventricular myocytes isolated from adult rat hearts Pflügers Arch. 443 2002 676 689
    • (2002) Pflügers Arch. , vol.443 , pp. 676-689
    • Polontchouk, L.O.1    Valiunas, V.2    Haefliger, J.A.3    Eppenberger, H.M.4    Weingart, R.5
  • 259
    • 23244464404 scopus 로고    scopus 로고
    • Expression of zonula occludens-1 (ZO-1) and the transcription factor ZO-1-associated nucleic acid-binding protein (ZONAB)-MsY3 in glial cells and colocalization at oligodendrocyte and astrocyte gap junctions in mouse brain
    • M.C. Penes, X. Li, and J.I. Nagy Expression of zonula occludens-1 (ZO-1) and the transcription factor ZO-1-associated nucleic acid-binding protein (ZONAB)-MsY3 in glial cells and colocalization at oligodendrocyte and astrocyte gap junctions in mouse brain Eur. J. Neurosci. 22 2005 404 418
    • (2005) Eur. J. Neurosci. , vol.22 , pp. 404-418
    • Penes, M.C.1    Li, X.2    Nagy, J.I.3
  • 260
    • 34250829013 scopus 로고    scopus 로고
    • Connexin 36 is expressed and associated with zonula occludens-1 protein in PC-12 cells
    • S.H. Lu, H. Li, F.H. Zhou, J.J. Zhang, and L.X. Wang Connexin 36 is expressed and associated with zonula occludens-1 protein in PC-12 cells Gen. Physiol. Biophys. 26 2007 33 39
    • (2007) Gen. Physiol. Biophys. , vol.26 , pp. 33-39
    • Lu, S.H.1    Li, H.2    Zhou, F.H.3    Zhang, J.J.4    Wang, L.X.5
  • 261
    • 2942683207 scopus 로고    scopus 로고
    • A proposed role for ZO-1 in targeting connexin 43 gap junctions to the endocytic pathway
    • D. Segretain, C. Fiorini, X. Decrouy, N. Defamie, J.R. Prat, and G. Pointis A proposed role for ZO-1 in targeting connexin 43 gap junctions to the endocytic pathway Biochimie 86 2004 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
  • 262
    • 35048876325 scopus 로고    scopus 로고
    • The proteasome regulates the interaction between Cx43 and ZO-1
    • H. Girao, and P. Pereira The proteasome regulates the interaction between Cx43 and ZO-1 J. Cell. Biochem. 102 2007 719 728
    • (2007) J. Cell. Biochem. , vol.102 , pp. 719-728
    • Girao, H.1    Pereira, P.2
  • 264
    • 0345865198 scopus 로고    scopus 로고
    • Identification of connexin-43 interacting proteins
    • D. Singh, and P.D. Lampe Identification of connexin-43 interacting proteins Cell Commun. Adhes. 10 2003 215 220
    • (2003) Cell Commun. Adhes. , vol.10 , pp. 215-220
    • Singh, D.1    Lampe, P.D.2
  • 266
    • 1642365478 scopus 로고    scopus 로고
    • Interaction of major intrinsic protein (aquaporin-0) with fiber connexins in lens development
    • X.S. Yu, and J.X. Jiang Interaction of major intrinsic protein (aquaporin-0) with fiber connexins in lens development J. Cell Sci. 117 2004 871 880
    • (2004) J. Cell Sci. , vol.117 , pp. 871-880
    • Yu, X.S.1    Jiang, J.X.2
  • 267
    • 0037160066 scopus 로고    scopus 로고
    • Casein kinase 1 regulates connexin-43 gap junction assembly
    • C.D. Cooper, and P.D. Lampe 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
  • 268
    • 69249144738 scopus 로고    scopus 로고
    • Identification of binding partners for the cytoplasmic loop of connexin43: A novel interaction with beta-tubulin
    • E.Y. Kang, M. Ponzio, P.P. Gupta, F. Liu, A. Butensky, and D.E. Gutstein Identification of binding partners for the cytoplasmic loop of connexin43: a novel interaction with beta-tubulin Cell Commun. Adhes. 9 2009 1 10
    • (2009) Cell Commun. Adhes. , vol.9 , pp. 1-10
    • Kang, E.Y.1    Ponzio, M.2    Gupta, P.P.3    Liu, F.4    Butensky, A.5    Gutstein, D.E.6
  • 269
    • 70350560632 scopus 로고    scopus 로고
    • Cortactin/tyrosine-phosphorylated cortactin interaction with connexin 43 in mouse seminiferous tubules
    • M.L. Vitale, C.P. Akpovi, and R.M. Pelletier Cortactin/tyrosine- phosphorylated cortactin interaction with connexin 43 in mouse seminiferous tubules Microsc. Res. Tech. 72 2009 856 867
    • (2009) Microsc. Res. Tech. , vol.72 , pp. 856-867
    • Vitale, M.L.1    Akpovi, C.P.2    Pelletier, R.M.3
  • 270
    • 84867854600 scopus 로고    scopus 로고
    • Down-regulation of connexin43 expression reveals the involvement of caveolin-1 containing lipid rafts in human U251 glioblastoma cell invasion
    • 10.1002/mc.20853
    • P.O. Strale, J. Clarhaut, C. Lamiche, L. Cronier, M. Mesnil, and N. Defamie Down-regulation of connexin43 expression reveals the involvement of caveolin-1 containing lipid rafts in human U251 glioblastoma cell invasion Mol. Carcinog. 2011 10.1002/mc.20853
    • (2011) Mol. Carcinog.
    • Strale, P.O.1    Clarhaut, J.2    Lamiche, C.3    Cronier, L.4    Mesnil, M.5    Defamie, N.6
  • 272
    • 33645013130 scopus 로고    scopus 로고
    • Identification of a potential regulator of the gap junction protein pannexin1
    • S. Bunse, A. Haghika, G. Zoidl, and R. Dermietzel Identification of a potential regulator of the gap junction protein pannexin1 Cell Commun. Adhes. 12 2005 231 236
    • (2005) Cell Commun. Adhes. , vol.12 , pp. 231-236
    • Bunse, S.1    Haghika, A.2    Zoidl, G.3    Dermietzel, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.