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Volumn 71, Issue 3, 1996, Pages 1273-1284

pH regulation of connexin43: Molecular analysis of the gating particle

Author keywords

[No Author keywords available]

Indexed keywords

CONNEXIN 43;

EID: 0029781699     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79328-1     Document Type: Article
Times cited : (146)

References (38)
  • 1
    • 0027474991 scopus 로고
    • Left-handed polyproline II helices commonly occur in globular proteins
    • Adzhubei, A. A., and M. J. E. Sternberg. 1993. Left-handed polyproline II helices commonly occur in globular proteins. J. Mol. Biol. 229:472-493.
    • (1993) J. Mol. Biol. , vol.229 , pp. 472-493
    • Adzhubei, A.A.1    Sternberg, M.J.E.2
  • 5
    • 0001692697 scopus 로고
    • Gap junctional conductance: Gating
    • E. L. Herzberg and R. G. Johnson, editors. Alan R. Liss, New York
    • Bennett, M. V. L., R. L. Verselis, R. L. White, and D. C. Spray. 1988. Gap junctional conductance: gating. In Gap Junctions. E. L. Herzberg and R. G. Johnson, editors. Alan R. Liss, New York. 287-304.
    • (1988) Gap Junctions , pp. 287-304
    • Bennett, M.V.L.1    Verselis, R.L.2    White, R.L.3    Spray, D.C.4
  • 6
    • 0002780591 scopus 로고
    • The connexin family tree
    • Y. Kanno, K. Kataoka, Y. Shiba, Y. Shibata, and T. Shimazu, editors. Elsevier, Amsterdam
    • Bennett, M. V. L., X. Zheng, and M. L. Sogin. 1995. The connexin family tree. In Intercellular Communication through Gap Junctions. Y. Kanno, K. Kataoka, Y. Shiba, Y. Shibata, and T. Shimazu, editors. Elsevier, Amsterdam. 3-8.
    • (1995) Intercellular Communication Through Gap Junctions , pp. 3-8
    • Bennett, M.V.L.1    Zheng, X.2    Sogin, M.L.3
  • 7
    • 0023551497 scopus 로고
    • Connexin43: A protein from rat heart homologus to a gap junction protein from liver
    • Beyer, E. C., D. L. Paul, and D. A. Goodenough. 1987. connexin43: a protein from rat heart homologus to a gap junction protein from liver. J. Cell Biol. 105:2621-2629.
    • (1987) J. Cell Biol. , vol.105 , pp. 2621-2629
    • Beyer, E.C.1    Paul, D.L.2    Goodenough, D.A.3
  • 8
    • 0029060788 scopus 로고
    • Mutations of the connexin43 gap-junction gene in patients with heart malformations and defects of laterally
    • Britz-Cunningham, S. H., M. M. Shah, C. W. Zuppan, and W. H. Fletcher. 1995. Mutations of the connexin43 gap-junction gene in patients with heart malformations and defects of laterally. N. Engl. J. Med. 332: 1323-1329.
    • (1995) N. Engl. J. Med. , vol.332 , pp. 1323-1329
    • Britz-Cunningham, S.H.1    Shah, M.M.2    Zuppan, C.W.3    Fletcher, W.H.4
  • 9
    • 0028230758 scopus 로고
    • Expression of chimeric connexins reveals new properties of the formation and gating behavior of gap junction channels
    • Bruzzone, R., T. W. White, and D. L. Paul. 1994. Expression of chimeric connexins reveals new properties of the formation and gating behavior of gap junction channels. J. Cell Sci. 107:955-967.
    • (1994) J. Cell Sci. , vol.107 , pp. 955-967
    • Bruzzone, R.1    White, T.W.2    Paul, D.L.3
  • 10
    • 0028895654 scopus 로고
    • Modular binding domains in signal transduction proteins
    • Cohen, G. B., R. Ren, and D. Baltimore. 1995. Modular binding domains in signal transduction proteins. Cell. 80:237-248.
    • (1995) Cell , vol.80 , pp. 237-248
    • Cohen, G.B.1    Ren, R.2    Baltimore, D.3
  • 12
    • 0011319325 scopus 로고
    • Expression pattern of different connexins in comparison with communication compartments during early mouse development
    • Y. Kanno, K. Kataoka, Y. Shiba, Y. Shibata, and T. Shimazu, editors. Elsevier, Amsterdam
    • Dahl, E., E. Winterhager, O. Traub, A. Butterweck, B. Reuss, and K. Willecke. 1995. Expression pattern of different connexins in comparison with communication compartments during early mouse development. In Intercellular Communication through Gap Junctions. Y. Kanno, K. Kataoka, Y. Shiba, Y. Shibata, and T. Shimazu, editors. Elsevier, Amsterdam. 21-25.
    • (1995) Intercellular Communication Through Gap Junctions , pp. 21-25
    • Dahl, E.1    Winterhager, E.2    Traub, O.3    Butterweck, A.4    Reuss, B.5    Willecke, K.6
  • 14
    • 0002424856 scopus 로고
    • Toward a molecular model for the pH regulation of intercellular communication in the heart
    • D. P. Zipes and J. Jalife, editors. W. B. Saunders, Philadelphia. In press
    • Delmar, M., S. Liu, G. E. Morley, J. F. Ek, J. M. B. Anumonwo, and S. M. Taffet. 1994. Toward a molecular model for the pH regulation of intercellular communication in the heart. In Cardiac Electrophysiology. From Cell to Bedside. D. P. Zipes and J. Jalife, editors. W. B. Saunders, Philadelphia. In press.
    • (1994) Cardiac Electrophysiology. From Cell to Bedside
    • Delmar, M.1    Liu, S.2    Morley, G.E.3    Ek, J.F.4    Anumonwo, J.M.B.5    Taffet, S.M.6
  • 15
    • 0015292069 scopus 로고
    • Oogenesis in Xenopus laevis (Daudin). I. Stages of oocyte development in laboratory maintained animals
    • Dumont, J. N. 1972. Oogenesis in Xenopus laevis (Daudin). I. Stages of oocyte development in laboratory maintained animals. J. Morphol. 136: 153-180.
    • (1972) J. Morphol. , vol.136 , pp. 153-180
    • Dumont, J.N.1
  • 16
    • 0028284598 scopus 로고
    • Role of histidine 95 on the pH gating of the cardiac gap junction protein connexin43
    • Ek, J. F., M. Delmar, R. Perzova, and S. M. Taffet. 1994. Role of histidine 95 on the pH gating of the cardiac gap junction protein connexin43. Circ. Res. 74:1058-1064.
    • (1994) Circ. Res. , vol.74 , pp. 1058-1064
    • Ek, J.F.1    Delmar, M.2    Perzova, R.3    Taffet, S.M.4
  • 18
    • 0025224223 scopus 로고
    • Biophysical and molecular mechanisms of Shaker potassium channel inactivation
    • Hoshi, T., W. N. Zagotta, and R. W. Aldrich. 1990. Biophysical and molecular mechanisms of Shaker potassium channel inactivation. Science. 250:533-538.
    • (1990) Science , vol.250 , pp. 533-538
    • Hoshi, T.1    Zagotta, W.N.2    Aldrich, R.W.3
  • 20
    • 0026813055 scopus 로고
    • Molecular biology and genetics of gap junction channels
    • Kumar, N. M., and N. B. Gilula. 1992. Molecular biology and genetics of gap junction channels. Semin. Cell Biol. 3:3-16.
    • (1992) Semin. Cell Biol. , vol.3 , pp. 3-16
    • Kumar, N.M.1    Gilula, N.B.2
  • 21
    • 0028148629 scopus 로고
    • Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains
    • Lim, W. A., F. M. Richards, and R. O. Fox. 1994. Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains. Nature. 372:375-379.
    • (1994) Nature , vol.372 , pp. 375-379
    • Lim, W.A.1    Richards, F.M.2    Fox, R.O.3
  • 22
    • 0029002720 scopus 로고
    • The hydrophobic effect in protein folding
    • Lins, L., and R. Brasseur. 1995. The hydrophobic effect in protein folding. FASEB J. 9:535-540.
    • (1995) FASEB J. , vol.9 , pp. 535-540
    • Lins, L.1    Brasseur, R.2
  • 23
    • 0027172696 scopus 로고
    • A structural basis for the unequal sensitivity of the major cardiac and liver gap junctions to intracellular acidification: The carboxyl tail length
    • Liu, S., S. Taffet, L. Stoner, M. Delmar, M. L. Vallano, and J. Jalife. 1993. A structural basis for the unequal sensitivity of the major cardiac and liver gap junctions to intracellular acidification: the carboxyl tail length. Biophys. J. 64:1422-1433.
    • (1993) Biophys. J. , vol.64 , pp. 1422-1433
    • Liu, S.1    Taffet, S.2    Stoner, L.3    Delmar, M.4    Vallano, M.L.5    Jalife, J.6
  • 24
    • 0030050142 scopus 로고    scopus 로고
    • Intramolecular interactions mediate pH regulation of connexin43 channels
    • Morley, G. E., S. M. Taffet, and M. Delmar. 1996. Intramolecular interactions mediate pH regulation of connexin43 channels. Biophys. J. 70:1294-1302.
    • (1996) Biophys. J. , vol.70 , pp. 1294-1302
    • Morley, G.E.1    Taffet, S.M.2    Delmar, M.3
  • 25
    • 0024545772 scopus 로고
    • Intracellular pH and cell-to-cell transmission in sheep Purkinje fibers
    • Pressler, M. 1989. Intracellular pH and cell-to-cell transmission in sheep Purkinje fibers. Biophys. J. 55:53-65.
    • (1989) Biophys. J. , vol.55 , pp. 53-65
    • Pressler, M.1
  • 26
    • 85030275250 scopus 로고
    • Determination of disulfide bond patterns in the extracellular docking domains of gap junctions
    • Rosinski, C., and B. J. Nicholson. 1994. Determination of disulfide bond patterns in the extracellular docking domains of gap junctions. Mol. Biol. Cell. 5:198a.
    • (1994) Mol. Biol. Cell. , vol.5
    • Rosinski, C.1    Nicholson, B.J.2
  • 27
    • 0019365945 scopus 로고
    • Equilibrium properties of a voltage-dependent junctional conductance
    • Spray, D. C., A. L. Harris, and M. V. L. Bennett. 1981. Equilibrium properties of a voltage-dependent junctional conductance. J. Gen. Physiol. 77:77-93.
    • (1981) J. Gen. Physiol. , vol.77 , pp. 77-93
    • Spray, D.C.1    Harris, A.L.2    Bennett, M.V.L.3
  • 28
    • 0026814616 scopus 로고
    • Structure of gap junction channels
    • Stauffer, K. A., and N. Unwin. 1992. Structure of gap junction channels. Semin. Cell Biol. 3:17-20.
    • (1992) Semin. Cell Biol. , vol.3 , pp. 17-20
    • Stauffer, K.A.1    Unwin, N.2
  • 29
    • 0027442575 scopus 로고
    • Identification of a proline residue as a transduction element involved in voltage gating of gap junctions
    • Suchyna, T. M., L. Xian-Xu, F. Gao, C. R. Fourtner, and B. J. Nicholson. 1993. Identification of a proline residue as a transduction element involved in voltage gating of gap junctions. Nature. 365:847-849.
    • (1993) Nature , vol.365 , pp. 847-849
    • Suchyna, T.M.1    Xian-Xu, L.2    Gao, F.3    Fourtner, C.R.4    Nicholson, B.J.5
  • 30
    • 0024560509 scopus 로고
    • Formation of gap junctions by expression of connexins in Xenopus oocyte pairs
    • Swenson, K. I., J. R. Jordan, E. C. Beyer, and D. L. Paul. 1989. Formation of gap junctions by expression of connexins in Xenopus oocyte pairs. Cell. 57:145-155.
    • (1989) Cell , vol.57 , pp. 145-155
    • Swenson, K.I.1    Jordan, J.R.2    Beyer, E.C.3    Paul, D.L.4
  • 32
    • 0023929638 scopus 로고
    • A simple and rapid method for the selection of oligodeoxynucleotidedictated mutants
    • Vandeyar, M. A., M. P. Weiner, C. J. Hutton, and C. A. Batt. 1988. A simple and rapid method for the selection of oligodeoxynucleotidedictated mutants. Gene. 65:129-133.
    • (1988) Gene , vol.65 , pp. 129-133
    • Vandeyar, M.A.1    Weiner, M.P.2    Hutton, C.J.3    Batt, C.A.4
  • 33
    • 0030022421 scopus 로고    scopus 로고
    • Characterization of the mitogen-aclivated protein kinase phosphorylation sites on the Connexin-43 gap junction protein
    • Warn-Cramer, B. J., P. D. Lampe, W. E. Kurata, M. Y. Kanemitsu, L. W. M. Loo, W. Eckhart, and A. F. Lau. 1996. Characterization of the mitogen-aclivated protein kinase phosphorylation sites on the Connexin-43 gap junction protein. J. Biol. Chem. 271:3779-3786.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3779-3786
    • Warn-Cramer, B.J.1    Lampe, P.D.2    Kurata, W.E.3    Kanemitsu, M.Y.4    Loo, L.W.M.5    Eckhart, W.6    Lau, A.F.7
  • 34
    • 0026071778 scopus 로고
    • Gating properties of connexin32 cell-cell channels and their mutants expressed in Xenopus oocytes
    • Werner, R., E. Levine, C. Rabadan-Diehl, and G. Dahl. 1991. Gating properties of connexin32 cell-cell channels and their mutants expressed in Xenopus oocytes. Proc. R. Soc. Lond. 243:5-11.
    • (1991) Proc. R. Soc. Lond. , vol.243 , pp. 5-11
    • Werner, R.1    Levine, E.2    Rabadan-Diehl, C.3    Dahl, G.4
  • 35
    • 0028214204 scopus 로고
    • Selective interactions among the multiple connexin proteins expressed in the vertebrate lens: The second extracellular domain is a determinant of compatibility between connexins
    • White, T. W., R. Bruzzone, S. Wolfram, D. L. Paul, and D. A. Goodenough. 1994. 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: 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
  • 36
    • 0029020099 scopus 로고
    • Functional analysis of selective interactions among rodent connexins
    • White, T. W., D. L. Paul, D. A. Goodenough, and R. Bruzzone. 1995. Functional analysis of selective interactions among rodent connexins. Mol. Biol. Cell. 6:459-470.
    • (1995) Mol. Biol. Cell. , vol.6 , pp. 459-470
    • White, T.W.1    Paul, D.L.2    Goodenough, D.A.3    Bruzzone, R.4
  • 37
    • 0028097921 scopus 로고
    • The structure and function of proline-rich regions in proteins
    • Williamson, M. P. 1994. The structure and function of proline-rich regions in proteins. Biochem. J. 297:249-260.
    • (1994) Biochem. J. , vol.297 , pp. 249-260
    • Williamson, M.P.1
  • 38
    • 0013484134 scopus 로고
    • Structural basis for the binding of proline-rich peptides to SH3 domains
    • Yu, H., J. K. Chen, S. Feng, D. C. Dalgarno, A. W. Brauer, and S. L. Schreiber. 1994. Structural basis for the binding of proline-rich peptides to SH3 domains. Cell. 76:933-945.
    • (1994) Cell , vol.76 , pp. 933-945
    • Yu, H.1    Chen, J.K.2    Feng, S.3    Dalgarno, D.C.4    Brauer, A.W.5    Schreiber, S.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.