메뉴 건너뛰기




Volumn 116, Issue 15, 2003, Pages 3189-3201

Specific amino-acid residues in the N-terminus and TM3 implicated in channel function and oligomerization compatibility of connexin43

Author keywords

Connexin subunit assembly; Gap junction; Gap junction diseases; Green flourescent protein; Membrane channels; Oligomeric proteins

Indexed keywords

CONNEXIN 26; CONNEXIN 32; CONNEXIN 43; LUCIFER YELLOW;

EID: 0042386448     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.00604     Document Type: Review
Times cited : (65)

References (64)
  • 3
    • 0032579554 scopus 로고    scopus 로고
    • Isoform composition of connexin channels determines selectivity among second messengers and uncharged molecules
    • Bevans, C. G., Kordel, M., Rhee, S. K. and Harris, A. L. (1998). Isoform composition of connexin channels determines selectivity among second messengers and uncharged molecules. J. Biol. Chem. 273, 2808-2816.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2808-2816
    • Bevans, C.G.1    Kordel, M.2    Rhee, S.K.3    Harris, A.L.4
  • 6
    • 0030250207 scopus 로고    scopus 로고
    • The cellular Internet: On-line with connexins
    • Bruzzone, R., White, T. W. and Goodenough, D. A. (1996). The cellular Internet: on-line with connexins. Bioessays 18, 709-718.
    • (1996) Bioessays , vol.18 , pp. 709-718
    • Bruzzone, R.1    White, T.W.2    Goodenough, D.A.3
  • 8
    • 0035195813 scopus 로고    scopus 로고
    • Heterotypic gap junction channel formation between heteromeric and homomeric Cx40 and Cx43 connexons
    • Cottrell, G. T. and Burt, J. M. (2001). Heterotypic gap junction channel formation between heteromeric and homomeric Cx40 and Cx43 connexons. Am. J. Physiol. Cell Physiol. 281, C1559-C1567.
    • (2001) Am. J. Physiol. Cell Physiol. , vol.281
    • Cottrell, G.T.1    Burt, J.M.2
  • 9
  • 10
    • 0035203507 scopus 로고    scopus 로고
    • Multimeric connexin interactions prior to the trans-Golgi network
    • Das Sarma, J., Meyer, R. A., Wang, F., Abraham, V., Lo, C. W. and Koval, M. (2001). Multimeric connexin interactions prior to the trans-Golgi network. J. Cell Sci. 114, 4013-4024.
    • (2001) J. Cell Sci. , vol.114 , pp. 4013-4024
    • Das Sarma, J.1    Meyer, R.A.2    Wang, F.3    Abraham, V.4    Lo, C.W.5    Koval, M.6
  • 11
    • 0037036426 scopus 로고    scopus 로고
    • Targeted gap junction protein constructs reveal connexin-specific differences in oligomerization
    • Das Sarma, J. D., Wang, F. and Koval, M. (2002). Targeted gap junction protein constructs reveal connexin-specific differences in oligomerization. J. Biol. Chem. 277, 20911-20918.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20911-20918
    • Das Sarma, J.D.1    Wang, F.2    Koval, M.3
  • 13
    • 0036382811 scopus 로고    scopus 로고
    • Expression of a connexin31 mutation causing erythrokeratodermia variabilis is lethal for HeLa cells
    • Diestel, S., Richard, G., Doring, B. and Traub, O. (2002). Expression of a connexin31 mutation causing erythrokeratodermia variabilis is lethal for HeLa cells. Biochem. Biophys. Res. Commun. 296, 721-728.
    • (2002) Biochem. Biophys. Res. Commun. , vol.296 , pp. 721-728
    • Diestel, S.1    Richard, G.2    Doring, B.3    Traub, O.4
  • 14
    • 0033848257 scopus 로고    scopus 로고
    • Biosynthesis and structural composition of gap junction intercellular membrane channels
    • Falk, M. M. (2000). Biosynthesis and structural composition of gap junction intercellular membrane channels. Eur. J. Cell Biol. 79, 564-574.
    • (2000) Eur. J. Cell Biol. , vol.79 , pp. 564-574
    • Falk, M.M.1
  • 15
    • 0032478623 scopus 로고    scopus 로고
    • Connexin membrane protein biosynthesis is influenced by polypeptide positioning within the translocon and signal peptidase access
    • Falk, M. M. and Gilula, N. B. (1998). Connexin membrane protein biosynthesis is influenced by polypeptide positioning within the translocon and signal peptidase access. J. Biol. Chem. 273, 7856-7864.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7856-7864
    • Falk, M.M.1    Gilula, N.B.2
  • 16
    • 0028077475 scopus 로고
    • Membrane insertion of gap junction connexins: Polytopic channel forming membrane proteins
    • Falk, M. M., Kumar, N. M. and Gilula, N. B. (1994). Membrane insertion of gap junction connexins: polytopic channel forming membrane proteins. J. Cell Biol. 127, 343-355.
    • (1994) J. Cell Biol. , vol.127 , pp. 343-355
    • Falk, M.M.1    Kumar, N.M.2    Gilula, N.B.3
  • 17
    • 0031001091 scopus 로고    scopus 로고
    • Cellfree synthesis and assembly of connexins into functional gap junction membrane channels
    • Falk, M. M., Buehler, L. K., Kumar, N. M. and Gilula, N. B. (1997). Cellfree synthesis and assembly of connexins into functional gap junction membrane channels. EMBO J. 16, 2703-2716.
    • (1997) EMBO J. , vol.16 , pp. 2703-2716
    • Falk, M.M.1    Buehler, L.K.2    Kumar, N.M.3    Gilula, N.B.4
  • 18
    • 0031777369 scopus 로고    scopus 로고
    • Prediction of functional residues in water channels and related proteins
    • Froger, A., Tallur, B., Thomas, D. and Delamarche, C. (1998). Prediction of functional residues in water channels and related proteins. Protein Sci. 7, 1458-1468.
    • (1998) Protein Sci. , vol.7 , pp. 1458-1468
    • Froger, A.1    Tallur, B.2    Thomas, D.3    Delamarche, C.4
  • 19
    • 0033224243 scopus 로고    scopus 로고
    • Selective transfer of endogenous metabolites through gap junctions composed of different connexins
    • Goldberg, G. S., Lampe, P. D. and Nicholson, B. J. (1999). Selective transfer of endogenous metabolites through gap junctions composed of different connexins. Nat. Cell Biol. 1, 457-459.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 457-459
    • Goldberg, G.S.1    Lampe, P.D.2    Nicholson, B.J.3
  • 20
    • 0030013202 scopus 로고    scopus 로고
    • Connexins, connexons, and intercellular communication
    • Goodenough, D. A., Goliger, J. A. and Paul, D. L. (1996). Connexins, connexons, and intercellular communication. Annu. Rev. Biochem. 65, 475-502.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 475-502
    • Goodenough, D.A.1    Goliger, J.A.2    Paul, D.L.3
  • 22
    • 0344172759 scopus 로고    scopus 로고
    • Molecular determinants of glycine receptor subunit assembly
    • Griffon, N., Buttner, C., Nicke, A., Kuhse, J., Schmalzing, G. and Betz, H. (1999). Molecular determinants of glycine receptor subunit assembly. EMBO J. 18, 4711-4721.
    • (1999) EMBO J. , vol.18 , pp. 4711-4721
    • Griffon, N.1    Buttner, C.2    Nicke, A.3    Kuhse, J.4    Schmalzing, G.5    Betz, H.6
  • 23
    • 0001203743 scopus 로고    scopus 로고
    • Formation of heteromeric gap junction channels by connexins 40 and 43 in vascular smooth muscle cells
    • He, D. S., Jiang, J. X., Taffet, S. M. and Burt, J. M. (1999). Formation of heteromeric gap junction channels by connexins 40 and 43 in vascular smooth muscle cells. Proc. Natl. Acad. Sci. USA 96, 6495-6500.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6495-6500
    • He, D.S.1    Jiang, J.X.2    Taffet, S.M.3    Burt, J.M.4
  • 24
    • 0024165145 scopus 로고
    • Topology of the Mr 27,000 liver gap junction protein. Cytoplasmic localization of amino- and carboxyl termini and a hydrophilic domain which is protease-hypersensitive
    • Hertzberg, E. L., Disher, R. M., Tiller, A. A., Zhou, Y. and Cook, R. G. (1988). Topology of the Mr 27,000 liver gap junction protein. Cytoplasmic localization of amino- and carboxyl termini and a hydrophilic domain which is protease-hypersensitive. J. Biol. Chem. 263, 19105-19111.
    • (1988) J. Biol. Chem. , vol.263 , pp. 19105-19111
    • Hertzberg, E.L.1    Disher, R.M.2    Tiller, A.A.3    Zhou, Y.4    Cook, R.G.5
  • 25
    • 0030052934 scopus 로고    scopus 로고
    • Heteromeric connexons in lens gap junction channels
    • Jiang, J. X. and Goodenough, D. A. (1996). Heteromeric connexons in lens gap junction channels. Proc. Natl. Acad. Sci. USA 93, 1287-1291.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1287-1291
    • Jiang, J.X.1    Goodenough, D.A.2
  • 26
    • 0033012698 scopus 로고    scopus 로고
    • Trafficking, assembly, and function of a connexin43-green fluorescent protein chimera in live mammalian cells
    • Jordan, K., Solan, J. L., Dominguez, M., Sia, M., Hand, A., Lampe, P. D. and Laird, D. W. (1999). Trafficking, assembly, and function of a connexin43-green fluorescent protein chimera in live mammalian cells. Mol. Biol. Cell 10, 2033-2050.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2033-2050
    • Jordan, K.1    Solan, J.L.2    Dominguez, M.3    Sia, M.4    Hand, A.5    Lampe, P.D.6    Laird, D.W.7
  • 27
    • 0035186795 scopus 로고    scopus 로고
    • Human diseases: Clues to cracking the connexin code?
    • Kelsell, D. P., Dunlop, J. and Hodgins, M. B. (2001). Human diseases: clues to cracking the connexin code? Trends Cell Biol. 11, 2-6.
    • (2001) Trends Cell Biol. , vol.11 , pp. 2-6
    • Kelsell, D.P.1    Dunlop, J.2    Hodgins, M.B.3
  • 28
    • 0029127695 scopus 로고
    • Purification of bovine lens cell-to-cell channels composed of connexin44 and connexin50
    • Konig, N. and Zampighi, G. A. (1995). Purification of bovine lens cell-to-cell channels composed of connexin44 and connexin50. J. Cell Sci. 108, 3091-3098.
    • (1995) J. Cell Sci. , vol.108 , pp. 3091-3098
    • Konig, N.1    Zampighi, G.A.2
  • 29
    • 0029618669 scopus 로고
    • Synthesis and assembly of human beta 1 gap junctions in BHK cells by DNA transfection with the human beta 1 cDNA
    • Kumar, N. M., Friend, D. S. and Gilula, N. B. (1995). Synthesis and assembly of human beta 1 gap junctions in BHK cells by DNA transfection with the human beta 1 cDNA. J. Cell Sci. 108, 3725-3734.
    • (1995) J. Cell Sci. , vol.108 , pp. 3725-3734
    • Kumar, N.M.1    Friend, D.S.2    Gilula, N.B.3
  • 30
    • 0026813055 scopus 로고
    • Molecular biology and genetics of gap junction channels
    • Kumar, N. M. and Gilula, N. B. (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
  • 31
    • 0030028301 scopus 로고    scopus 로고
    • The gap junction communication channel
    • Kumar, N. M. and Gilula, N. B. (1996). The gap junction communication channel. Cell 84, 381-388.
    • (1996) Cell , vol.84 , pp. 381-388
    • Kumar, N.M.1    Gilula, N.B.2
  • 34
    • 0035370120 scopus 로고    scopus 로고
    • Expression of fluorescently tagged connexins: A novel approach to rescue function of oligomeric DsRed-tagged proteins
    • Lauf, U., Lopez, P. and Falk, M. M. (2001). Expression of fluorescently tagged connexins: a novel approach to rescue function of oligomeric DsRed-tagged proteins. FEBS Lett. 498, 11-15.
    • (2001) FEBS Lett. , vol.498 , pp. 11-15
    • Lauf, U.1    Lopez, P.2    Falk, M.M.3
  • 35
    • 0026794064 scopus 로고
    • Specification of subunit assembly by the hydrophilic amino-terminal domain of the Shaker potassium channel
    • Li, M., Jan, Y. N. and Jan, L. Y. (1992). Specification of subunit assembly by the hydrophilic amino-terminal domain of the Shaker potassium channel. Science 257, 1225-1230.
    • (1992) Science , vol.257 , pp. 1225-1230
    • Li, M.1    Jan, Y.N.2    Jan, L.Y.3
  • 37
    • 0034115524 scopus 로고    scopus 로고
    • Developmental expression and assembly of connexins into homomeric and heteromeric gap junction hemichannels in the mouse mammary gland
    • Locke, D., Perusinghe, N., Newman, T., Jayatilake, H., Evans, W. H. and Monaghan, P. (2000). Developmental expression and assembly of connexins into homomeric and heteromeric gap junction hemichannels in the mouse mammary gland. J. Cell. Physiol. 183, 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
  • 38
    • 0024095587 scopus 로고
    • Topology of the 32-kd liver gap junction protein determined by site-directed antibody localizations
    • Milks, L. C., Kumar, N. M., Houghten, R., Unwin, N. and Gilula, N. B. (1988). Topology of the 32-kd liver gap junction protein determined by site-directed antibody localizations. EMBO J. 7, 2967-2975.
    • (1988) EMBO J. , vol.7 , pp. 2967-2975
    • Milks, L.C.1    Kumar, N.M.2    Houghten, R.3    Unwin, N.4    Gilula, N.B.5
  • 39
    • 0027364529 scopus 로고
    • Multisubunit assembly of an integral plasma membrane channel protein, gap junction connexin43, occurs after exit from the ER
    • Musil, L. S. and Goodenough, D. A. (1993). Multisubunit assembly of an integral plasma membrane channel protein, gap junction connexin43, occurs after exit from the ER. Cell 74, 1065-1077.
    • (1993) Cell , vol.74 , pp. 1065-1077
    • Musil, L.S.1    Goodenough, D.A.2
  • 40
    • 0025817567 scopus 로고
    • Developmental regulation of gap junction gene expression during mouse embryonic development
    • Nishi, M., Kumar, N. M. and Gilula, N. B. (1991). Developmental regulation of gap junction gene expression during mouse embryonic development. Dev. Biol. 146, 117-130.
    • (1991) Dev. Biol. , vol.146 , pp. 117-130
    • Nishi, M.1    Kumar, N.M.2    Gilula, N.B.3
  • 41
    • 0037449718 scopus 로고    scopus 로고
    • Roles of M34, C64, and R75 in the assembly of human connexin 26: Implication for key amino acid residues for channel formation and function
    • Oshima, A., Doi, T., Mitsuoka, K., Maeda, S. and Fujiyoshi, Y. (2003). Roles of M34, C64, and R75 in the assembly of human connexin 26: Implication for key amino acid residues for channel formation and function. J. Biol. Chem. 278, 1807-1816.
    • (2003) J. Biol. Chem. , vol.278 , pp. 1807-1816
    • Oshima, A.1    Doi, T.2    Mitsuoka, K.3    Maeda, S.4    Fujiyoshi, Y.5
  • 43
    • 0035226626 scopus 로고    scopus 로고
    • Connexin disorders of the skin
    • Richard, G. (2001). Connexin disorders of the skin. Adv. Dermatol. 17, 243-277.
    • (2001) Adv. Dermatol. , vol.17 , pp. 243-277
    • Richard, G.1
  • 46
    • 0037728362 scopus 로고    scopus 로고
    • Divergent effects of two sequence variants of GJB3 (G12D and R32W) on the function of connexin 31 in vitro
    • Rouan, F., Lo, C., Fertala, A., Wahl, M., Rodeck, U., Uitto, J. and Richard, G. (2003). Divergent effects of two sequence variants of GJB3 (G12D and R32W) on the function of connexin 31 in vitro. Exp. Dermatol. 12, 191-197.
    • (2003) Exp. Dermatol. , vol.12 , pp. 191-197
    • Rouan, F.1    Lo, C.2    Fertala, A.3    Wahl, M.4    Rodeck, U.5    Uitto, J.6    Richard, G.7
  • 47
    • 0034961003 scopus 로고    scopus 로고
    • Transdominant inhibition of connexin-43 by mutant connexin-26: Implications for dominant connexin disorders affecting epidermal differentiation
    • Rouan, F., White, T. W., Brown, N., Taylor, A. M., Lucke, T. W., Paul, D. L., Munro, C. S., Uitto, J., Hodgins, M. B. and Richard, G. (2001). Transdominant inhibition of connexin-43 by mutant connexin-26: implications for dominant connexin disorders affecting epidermal differentiation. J. Cell Sci. 114, 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
  • 48
    • 0026666944 scopus 로고
    • Molecular analysis of voltage dependence of heterotypic gap junctions formed by connexins 26 and 32
    • Rubin, J. B., Verselis, V. K., Bennett, M. V. and Bargiello, T. A. (1992). Molecular analysis of voltage dependence of heterotypic gap junctions formed by connexins 26 and 32. Biophys. J. 62, 183-195.
    • (1992) Biophys. J. , vol.62 , pp. 183-195
    • Rubin, J.B.1    Verselis, V.K.2    Bennett, M.V.3    Bargiello, T.A.4
  • 49
  • 50
    • 0031765429 scopus 로고    scopus 로고
    • Diverse functions of vertebrate gap junctions
    • Simon, A. M. and Goodenough, D. A. (1998). Diverse functions of vertebrate gap junctions. Trends Cell Biol. 8, 477-483.
    • (1998) Trends Cell Biol. , vol.8 , pp. 477-483
    • Simon, A.M.1    Goodenough, D.A.2
  • 52
    • 0028964217 scopus 로고
    • The gap junction proteins beta 1-connexin (connexin-32) and beta 2-connexin (connexin-26) can form heteromeric hemichannels
    • Stauffer, K. A. (1995). The gap junction proteins beta 1-connexin (connexin-32) and beta 2-connexin (connexin-26) can form heteromeric hemichannels. J. Biol. Chem. 270, 6768-6772.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6768-6772
    • Stauffer, K.A.1
  • 54
    • 0033178439 scopus 로고    scopus 로고
    • Identification of amino acid residues within GABA(A) receptor beta subunits that mediate both homomeric and heteromeric receptor expression
    • Taylor, P. M., Thomas, P., Gorrie, G. H., Connolly, C. N., Smart, T. G. and Moss, S. J. (1999). Identification of amino acid residues within GABA(A) receptor beta subunits that mediate both homomeric and heteromeric receptor expression. J. Neurosci. 19, 6360-6371.
    • (1999) J. Neurosci. , vol.19 , pp. 6360-6371
    • Taylor, P.M.1    Thomas, P.2    Gorrie, G.H.3    Connolly, C.N.4    Smart, T.G.5    Moss, S.J.6
  • 55
    • 0033582686 scopus 로고    scopus 로고
    • Three-dimensional structure of a recombinant gap junction membrane channel
    • Unger, V. M., Kumar, N. M., Gilula, N. B. and Yeager, M. (1999). Three-dimensional structure of a recombinant gap junction membrane channel. Science 283, 1176-1180.
    • (1999) Science , vol.283 , pp. 1176-1180
    • Unger, V.M.1    Kumar, N.M.2    Gilula, N.B.3    Yeager, M.4
  • 57
    • 0029738724 scopus 로고    scopus 로고
    • Size and selectivity of gap junction channels formed from different connexins
    • Veenstra, R. D. (1996). Size and selectivity of gap junction channels formed from different connexins. J. Bioenerg. Biomembr. 28, 327-337.
    • (1996) J. Bioenerg. Biomembr. , vol.28 , pp. 327-337
    • Veenstra, R.D.1
  • 58
    • 0026595697 scopus 로고
    • The N-terminal domains of acetylcholine receptor subunits contain recognition signals for the initial steps of receptor assembly
    • Verrall, S. and Hall, Z. W. (1992). The N-terminal domains of acetylcholine receptor subunits contain recognition signals for the initial steps of receptor assembly. Cell 68, 23-31.
    • (1992) Cell , vol.68 , pp. 23-31
    • Verrall, S.1    Hall, Z.W.2
  • 59
    • 0008228272 scopus 로고    scopus 로고
    • Molecular dissection of a basic COOH-terminal domain of Cx32 that inhibits gap junction gating sensitivity
    • Wang, X. G. and Peracchia, C. (1998). Molecular dissection of a basic COOH-terminal domain of Cx32 that inhibits gap junction gating sensitivity. Am. J. Physiol. 275, C1384-C1390.
    • (1998) Am. J. Physiol. , vol.275
    • Wang, X.G.1    Peracchia, C.2
  • 60
    • 0029743057 scopus 로고    scopus 로고
    • Multiple connexin proteins in single intercellular channels: Connexin compatibility and functional consequences
    • White, T. W. and Bruzzone, R. (1996). Multiple connexin proteins in single intercellular channels: connexin compatibility and functional consequences. J. Bioenerg. Biomembr. 28, 339-350.
    • (1996) J. Bioenerg. Biomembr. , vol.28 , pp. 339-350
    • White, T.W.1    Bruzzone, R.2
  • 61
    • 0033002783 scopus 로고    scopus 로고
    • Genetic diseases and gene knockouts reveal diverse connexin functions
    • White, T. W. and Paul, D. L. (1999). Genetic diseases and gene knockouts reveal diverse connexin functions. Annu. Rev. Physiol. 61, 283-310.
    • (1999) Annu. Rev. Physiol. , vol.61 , pp. 283-310
    • White, T.W.1    Paul, D.L.2
  • 63
    • 0036451762 scopus 로고    scopus 로고
    • Diverse trafficking abnormalities of Connexin32 mutants causing CMTX
    • Yum, S. W., Kleopa, K. A., Shumas, S. and Scherer, S. S. (2002). Diverse trafficking abnormalities of Connexin32 mutants causing CMTX. Neurobiol. Dis. 11, 43-52.
    • (2002) Neurobiol. Dis. , vol.11 , pp. 43-52
    • Yum, S.W.1    Kleopa, K.A.2    Shumas, S.3    Scherer, S.S.4
  • 64
    • 0023644895 scopus 로고
    • Topological analysis of the major protein in isolated intact rat liver gap junctions and gap junction-derived single membrane structures
    • Zimmer, D. B., Green, C. R., Evans, W. H. and Gilula, N. B. (1987). Topological analysis of the major protein in isolated intact rat liver gap junctions and gap junction-derived single membrane structures. J. Biol. Chem. 262, 7751-7763.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7751-7763
    • Zimmer, D.B.1    Green, C.R.2    Evans, W.H.3    Gilula, N.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.