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Volumn 19, Issue 10, 1999, Pages 3752-3760

Altered formation of hemichannels and gap junction channels caused by C- terminal connexin-32 mutations

Author keywords

Connexin; Gap junction channel formation; Hereditary motor sensory neuropathy; Voltage gating; X linked Charcot Marie Tooth disease; Xenopus oocyte

Indexed keywords

CONNEXIN 32;

EID: 0344171987     PISSN: 02706474     EISSN: None     Source Type: Journal    
DOI: 10.1523/jneurosci.19-10-03752.1999     Document Type: Article
Times cited : (115)

References (56)
  • 1
    • 0032563605 scopus 로고    scopus 로고
    • Functional gap junctions in the Schwann cell myelin sheath
    • Balice-Gordon RJ, Bone LJ, Scherer SS (1998) Functional gap junctions in the Schwann cell myelin sheath. J Cell Biol 142:1095-1104.
    • (1998) J Cell Biol , vol.142 , pp. 1095-1104
    • Balice-Gordon, R.J.1    Bone, L.J.2    Scherer, S.S.3
  • 3
    • 0030814751 scopus 로고    scopus 로고
    • Species-specific voltage-gating properties of connexin-45 junctions expressed in Xenopus oocytes
    • Barrio LC, Capel J, Jarillo JA, Castro C, Revilla A (1997) Species-specific voltage-gating properties of connexin-45 junctions expressed in Xenopus oocytes. Biophys J 73:757-769.
    • (1997) Biophys J , vol.73 , pp. 757-769
    • Barrio, L.C.1    Capel, J.2    Jarillo, J.A.3    Castro, C.4    Revilla, A.5
  • 8
    • 0028018967 scopus 로고
    • Null mutations of connexin32 in patients with X-linked Charcot-Marie-Tooth disease
    • Bruzzone R, White TW, Scherer SS, Fischbeck KH, Paul DL (1994) Null mutations of connexin32 in patients with X-linked Charcot-Marie-Tooth disease. Neuron 13:1253-1260.
    • (1994) Neuron , vol.13 , pp. 1253-1260
    • Bruzzone, R.1    White, T.W.2    Scherer, S.S.3    Fischbeck, K.H.4    Paul, D.L.5
  • 9
    • 0029974655 scopus 로고    scopus 로고
    • Connections with connexins: The molecular basis of direct intercellular signaling
    • Bruzzone R, White TW, Paul DL (1996) Connections with connexins: The molecular basis of direct intercellular signaling. Eur J Biochem 238:1-27.
    • (1996) Eur J Biochem , vol.238 , pp. 1-27
    • Bruzzone, R.1    White, T.W.2    Paul, D.L.3
  • 10
    • 0023389969 scopus 로고
    • Opening of single junction channels during the formation of electrical coupling between embryonic muscle cells
    • Chow I, Young SH (1987) Opening of single junction channels during the formation of electrical coupling between embryonic muscle cells. Dev Biol 122:332-337.
    • (1987) Dev Biol , vol.122 , pp. 332-337
    • Chow, I.1    Young, S.H.2
  • 11
    • 0025798576 scopus 로고
    • Cell/cell channel formation involved disulfide exchange
    • Dahl G, Levine E, Rabadan-Diehl C, Werner R (1991) Cell/cell channel formation involved disulfide exchange. Eur J Biochem 197:141-144.
    • (1991) Eur J Biochem , vol.197 , pp. 141-144
    • Dahl, G.1    Levine, E.2    Rabadan-Diehl, C.3    Werner, R.4
  • 12
    • 0028089678 scopus 로고
    • Attempts to define functional domains of gap junction proteins with synthetic peptides
    • Dahl G, Nonner W, Werner R (1994) Attempts to define functional domains of gap junction proteins with synthetic peptides. Biophys J 67:1816-1822.
    • (1994) Biophys J , vol.67 , pp. 1816-1822
    • Dahl, G.1    Nonner, W.2    Werner, R.3
  • 14
    • 0026567947 scopus 로고
    • Hemi-gap-junction channels in solitary horizontal cell of catfish retina
    • DeVries SH, Schwartz EA (1992) Hemi-gap-junction channels in solitary horizontal cell of catfish retina. J Physiol (Lond) 445:201-230.
    • (1992) J Physiol (Lond) , vol.445 , pp. 201-230
    • DeVries, S.H.1    Schwartz, E.A.2
  • 15
    • 0026535991 scopus 로고
    • Immunolocalization and expression of functional and nonfunctional cell-to-cell channels from wild-type and mutant rat heart connexin43 cDNA
    • Durham B, Liu S, Taffet S, Trabda-Janik E, Delmar M, Tetryshyn R, Zheng S, Perzova R, Vallano ML (1992) Immunolocalization and expression of functional and nonfunctional cell-to-cell channels from wild-type and mutant rat heart connexin43 cDNA. Circ Res 70:1233-1243.
    • (1992) Circ Res , vol.70 , pp. 1233-1243
    • Durham, B.1    Liu, S.2    Taffet, S.3    Trabda-Janik, E.4    Delmar, M.5    Tetryshyn, R.6    Zheng, S.7    Perzova, R.8    Vallano, M.L.9
  • 16
    • 0029738650 scopus 로고    scopus 로고
    • Xenopus connexin38 forms hemi-gap-junctional channels in nonjunctional plasma membrane of Xenopus oocytes
    • Ebihara L (1996) Xenopus connexin38 forms hemi-gap-junctional channels in nonjunctional plasma membrane of Xenopus oocytes. Biophys J 96:742-748.
    • (1996) Biophys J , vol.96 , pp. 742-748
    • Ebihara, L.1
  • 17
    • 0028918702 scopus 로고
    • Distinct behavior of connexin56 and connexin46 gap junctional channels can be predicted from the behavior of their hemi-gap-junctional channels
    • Ebihara L, Berthoud VM, Beyer EC (1995) Distinct behavior of connexin56 and connexin46 gap junctional channels can be predicted from the behavior of their hemi-gap-junctional channels. Biophys J 68:1796-1803.
    • (1995) Biophys J , vol.68 , pp. 1796-1803
    • Ebihara, L.1    Berthoud, V.M.2    Beyer, E.C.3
  • 19
    • 0031001091 scopus 로고    scopus 로고
    • Cell-free synthesis and assembly of connexins into functional gap junction membrane channels
    • Falk MM, Buehler LK, Kumar NM, Gilula NB (1997) Cell-free synthesis and assembly of connexins into functional gap junction membrane channels. EMBO J 16:2703-2716.
    • (1997) EMBO J , vol.16 , pp. 2703-2716
    • Falk, M.M.1    Buehler, L.K.2    Kumar, N.M.3    Gilula, N.B.4
  • 20
    • 0032498942 scopus 로고    scopus 로고
    • The pattern of disulfide linkages in the extracellular loop regions of Cx32 suggest a model for the docking interfaces of gap junctions
    • Foote CI, Xhu X, Zhou L, Nicholson BJ (1998) The pattern of disulfide linkages in the extracellular loop regions of Cx32 suggest a model for the docking interfaces of gap junctions. J Cell Biol 140:1187-1197.
    • (1998) J Cell Biol , vol.140 , pp. 1187-1197
    • Foote, C.I.1    Xhu, X.2    Zhou, L.3    Nicholson, B.J.4
  • 21
    • 0029165125 scopus 로고
    • Preparation, characterization, and structure of half gap junctional layers split with urea and EGTA
    • Ghoshroy S, Goodenough DA, Sosinsky GE (1995) Preparation, characterization, and structure of half gap junctional layers split with urea and EGTA. J Membr Biol 146:15-28.
    • (1995) J Membr Biol , vol.146 , pp. 15-28
    • Ghoshroy, S.1    Goodenough, D.A.2    Sosinsky, G.E.3
  • 22
    • 0015493414 scopus 로고
    • Metabolic coupling, ionic coupling and cell contacts
    • Gilula NB, Reves OR, Steinbach A (1982) Metabolic coupling, ionic coupling and cell contacts. Nature 235:262-265.
    • (1982) Nature , vol.235 , pp. 262-265
    • Gilula, N.B.1    Reves, O.R.2    Steinbach, A.3
  • 24
    • 0016194153 scopus 로고
    • The splitting of hepatocyte gap junctions and zonulae occludentes with hypertonic disaccharides
    • Goodenough DA, Gilula NB (1974) The splitting of hepatocyte gap junctions and zonulae occludentes with hypertonic disaccharides. J Cell Biol 61:575-590.
    • (1974) J Cell Biol , vol.61 , pp. 575-590
    • Goodenough, D.A.1    Gilula, N.B.2
  • 25
    • 0024110268 scopus 로고
    • Topological distribution of two connexin32 antigenic sites in intact and split rodent hepatocyte gap junctions
    • Goodenough DA, Paul DL, Jesaitis L (1988) Topological distribution of two connexin32 antigenic sites in intact and split rodent hepatocyte gap junctions. J Cell Biol 107:1817-1824.
    • (1988) J Cell Biol , vol.107 , pp. 1817-1824
    • Goodenough, D.A.1    Paul, D.L.2    Jesaitis, L.3
  • 26
    • 0028079860 scopus 로고
    • Bovine connexin44, a lens gap junction protein: Molecular cloning, immunological characterization and functional expression
    • Gupta VK, Berthoud VM, Atal N, Jarillo JA, Barrio LC, Beyer EC (1994) Bovine connexin44, a lens gap junction protein: molecular cloning, immunological characterization and functional expression. Invest Ophthalmol Vis Sci 35:3747-3758.
    • (1994) Invest Ophthalmol Vis Sci , vol.35 , pp. 3747-3758
    • Gupta, V.K.1    Berthoud, V.M.2    Atal, N.3    Jarillo, J.A.4    Barrio, L.C.5    Beyer, E.C.6
  • 27
    • 0025085880 scopus 로고
    • X-linked dominant hereditary motor and sensory neuropathy
    • Hahn AF, Brown WF, Koopman WJ, Feasby TE (1990) X-linked dominant hereditary motor and sensory neuropathy. Brain 113:1511-1525.
    • (1990) Brain , vol.113 , pp. 1511-1525
    • Hahn, A.F.1    Brown, W.F.2    Koopman, W.J.3    Feasby, T.E.4
  • 28
    • 0029829022 scopus 로고    scopus 로고
    • Incompatibility of connexin 40 and 43 hemichannels in gap junctions between mammalian cells is determined by intracellular domains
    • Haubrich S, Schwarz HJ, Bukauskas F, Lichtenberg-Frate H, Traub O, Weingart R, Willecke K (1996) Incompatibility of connexin 40 and 43 hemichannels in gap junctions between mammalian cells is determined by intracellular domains. Mol Biol Cell 7:1995-2006.
    • (1996) Mol Biol Cell , vol.7 , pp. 1995-2006
    • Haubrich, S.1    Schwarz, H.J.2    Bukauskas, F.3    Lichtenberg-Frate, H.4    Traub, O.5    Weingart, R.6    Willecke, K.7
  • 29
    • 0026095474 scopus 로고
    • Atomic force microscopy and dissection of gap junctions
    • Hoh JH, Lal R, John SA, Revel J-P, Arnsdorf MF (1991) Atomic force microscopy and dissection of gap junctions. Science 235:1405-1408.
    • (1991) Science , vol.235 , pp. 1405-1408
    • Hoh, J.H.1    Lal, R.2    John, S.A.3    Revel, J.-P.4    Arnsdorf, M.F.5
  • 30
    • 0027163746 scopus 로고
    • Structure of the extracellular surface of the gap junction by atomic force microscopy
    • Hoh JH, Sosinsky GE, Revel J-P, Hansma PK (1993) Structure of the extracellular surface of the gap junction by atomic force microscopy. Biophys J 65:149-163.
    • (1993) Biophys J , vol.65 , pp. 149-163
    • Hoh, J.H.1    Sosinsky, G.E.2    Revel, J.-P.3    Hansma, P.K.4
  • 32
    • 0029977888 scopus 로고    scopus 로고
    • Correlation between connexin 32 gene mutations and clinical phenotype in X-linked dominant Charcot-Marie-Tooth neuropathy
    • Ionasescu VV, Ionasescu R, Searby C (1996) Correlation between connexin 32 gene mutations and clinical phenotype in X-linked dominant Charcot-Marie-Tooth neuropathy. Am J Med Genet 63:486-491.
    • (1996) Am J Med Genet , vol.63 , pp. 486-491
    • Ionasescu, V.V.1    Ionasescu, R.2    Searby, C.3
  • 33
    • 0023033171 scopus 로고
    • Cloning and characterization of human and rat liver cDNAs coding for a gap junction protein
    • Kumar NM, Gilula NB (1986) Cloning and characterization of human and rat liver cDNAs coding for a gap junction protein. J Cell Biol 103:767-776.
    • (1986) J Cell Biol , vol.103 , pp. 767-776
    • Kumar, N.M.1    Gilula, N.B.2
  • 35
    • 0031281674 scopus 로고    scopus 로고
    • Degradation of connexin43 gap junctions involves both the proteasome and lysosome
    • Laing JG, Tadros PN, Westphale EM, Beyer EC (1997) Degradation of connexin43 gap junctions involves both the proteasome and lysosome. Exp Cell Res 236:482-492.
    • (1997) Exp Cell Res , vol.236 , pp. 482-492
    • Laing, J.G.1    Tadros, P.N.2    Westphale, E.M.3    Beyer, E.C.4
  • 37
    • 0017889553 scopus 로고
    • Quantum jumps of conductance during formation of membrane channels at cell-to-cell junction
    • Loewenstein WR, Kanno Y, Scolar SJ (1981) Quantum jumps of conductance during formation of membrane channels at cell-to-cell junction. Nature 274:133-136.
    • (1981) Nature , vol.274 , pp. 133-136
    • Loewenstein, W.R.1    Kanno, Y.2    Scolar, S.J.3
  • 38
    • 0021329979 scopus 로고
    • Detergent sensitivity and splitting of isolated liver gap junctions
    • Manjunath CK, Goings GE, Page E (1984) Detergent sensitivity and splitting of isolated liver gap junctions. J Membr Biol 78:147-155.
    • (1984) J Membr Biol , vol.78 , pp. 147-155
    • Manjunath, C.K.1    Goings, G.E.2    Page, E.3
  • 39
    • 0026671599 scopus 로고
    • Inhibition of gap junction and adherens junction assembly by connexin and N-CAM antibodies
    • Meyer RA, Laird DW, Revel J-P, Johnson R (1992) Inhibition of gap junction and adherens junction assembly by connexin and N-CAM antibodies. J Cell Biol 119:179-189.
    • (1992) J Cell Biol , vol.119 , pp. 179-189
    • Meyer, R.A.1    Laird, D.W.2    Revel, J.-P.3    Johnson, R.4
  • 40
    • 0027364529 scopus 로고
    • Multisubunits assembly of a integral plasma membrane channel protein, gap junction connexin43, occurs after exit from the ER
    • Musil LS, Goodenough DA (1993) Multisubunits assembly of a 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
  • 42
    • 0030777706 scopus 로고    scopus 로고
    • Changes in permeability caused by connexin 32 mutations underlie X-linked Charcot-Marie-Tooth disease
    • Oh S, Ri Y, Bennett MVL, Trexler EB, Verselis VK, Bargiello TA (1997) Changes in permeability caused by connexin 32 mutations underlie X-linked Charcot-Marie-Tooth disease. Neuron 19:927-938.
    • (1997) Neuron , vol.19 , pp. 927-938
    • Oh, S.1    Ri, Y.2    Bennett, M.V.L.3    Trexler, E.B.4    Verselis, V.K.5    Bargiello, T.A.6
  • 43
    • 0029977355 scopus 로고    scopus 로고
    • Connexin 32 mutations from X-linked Charcot-Marie-Tooth disease patients: Functional defects and dominant negative effects
    • Omari Y, Mesnil M, Yamasaki H (1996) Connexin 32 mutations from X-linked Charcot-Marie-Tooth disease patients: functional defects and dominant negative effects. Mol Biol Cell 7:907-916.
    • (1996) Mol Biol Cell , vol.7 , pp. 907-916
    • Omari, Y.1    Mesnil, M.2    Yamasaki, H.3
  • 44
    • 0026352039 scopus 로고
    • Connexin46, a novel lens gap junction protein, induces voltage-gated currents in nonjunctional plasma membrane of Xenopus oocytes
    • Paul DL, Ebihara L, Takemoto LJ, Swenson KI, Goodenough DA (1991) Connexin46, a novel lens gap junction protein, induces voltage-gated currents in nonjunctional plasma membrane of Xenopus oocytes. J Cell Biol 115:1077-1089.
    • (1991) J Cell Biol , vol.115 , pp. 1077-1089
    • Paul, D.L.1    Ebihara, L.2    Takemoto, L.J.3    Swenson, K.I.4    Goodenough, D.A.5
  • 45
    • 0031012580 scopus 로고    scopus 로고
    • Three-dimensional structure of the gap junction connexon
    • Perkins G, Goodenough DA, Sosinsky GE (1997) Three-dimensional structure of the gap junction connexon. Biophys J 72:533-544.
    • (1997) Biophys J , vol.72 , pp. 533-544
    • Perkins, G.1    Goodenough, D.A.2    Sosinsky, G.E.3
  • 46
    • 0008196501 scopus 로고    scopus 로고
    • Structural considerations for connexon docking
    • (Werner R, ed). Amsterdam: IOS
    • Perkins G, Goodenough DA, Sosinsky GE (1998) Structural considerations for connexon docking. In: Gap junction (Werner R, ed), pp 13-17. Amsterdam: IOS.
    • (1998) Gap Junction , pp. 13-17
    • Perkins, G.1    Goodenough, D.A.2    Sosinsky, G.E.3
  • 47
    • 0028018109 scopus 로고
    • A connexin-32 mutation associated with Charcot-Marie-Tooth disease does not affect channel formation in oocytes
    • Rabadan-Diehl C, Dahl G, Werner R (1994) A connexin-32 mutation associated with Charcot-Marie-Tooth disease does not affect channel formation in oocytes. FEBS Lett 351:90-94.
    • (1994) FEBS Lett , vol.351 , pp. 90-94
    • Rabadan-Diehl, C.1    Dahl, G.2    Werner, R.3
  • 49
    • 0032100768 scopus 로고    scopus 로고
    • Connexin32 mutations associated with X-linked Charcot-Marie-Tooth disease show two distinct behaviors: Loss of function and altered gating properties
    • Ressot C, Gomés D, Dautigny A, Pham-Dinh D, Bruzzone R (1998) Connexin32 mutations associated with X-linked Charcot-Marie-Tooth disease show two distinct behaviors: loss of function and altered gating properties. J Neurosci 18:4063-4075.
    • (1998) J Neurosci , vol.18 , pp. 4063-4075
    • Ressot, C.1    Gomés, D.2    Dautigny, A.3    Pham-Dinh, D.4    Bruzzone, R.5
  • 50
    • 0014097086 scopus 로고
    • Hexagonal array of subunits in intercellular junctions of the mouse heart and liver
    • Revel J-P, Karnovsky MJ (1967) Hexagonal array of subunits in intercellular junctions of the mouse heart and liver. J Cell Biol 33:C7-C12.
    • (1967) J Cell Biol , vol.33
    • Revel, J.-P.1    Karnovsky, M.J.2
  • 51
    • 0030930298 scopus 로고    scopus 로고
    • Screening for Cx32 mutations in Charcot-Marie-Tooth disease families with possible X-linked inheritance
    • Silander K, Meretoja P, Pihko H, Jovonen V, Issakainen J, Aula P, Savontaus M-L (1997) Screening for Cx32 mutations in Charcot-Marie-Tooth disease families with possible X-linked inheritance. Hum Genet 100:391-397.
    • (1997) Hum Genet , vol.100 , pp. 391-397
    • Silander, K.1    Meretoja, P.2    Pihko, H.3    Jovonen, V.4    Issakainen, J.5    Aula, P.6    Savontaus, M.-L.7
  • 52
    • 0029942648 scopus 로고    scopus 로고
    • Novel mutations in the connexin 32 gene associated with X-linked Charcot-Marie-Tooth disease
    • Tan CC, Ainsworth PJ, Hahn AF, MacLeod P (1996) Novel mutations in the connexin 32 gene associated with X-linked Charcot-Marie-Tooth disease. Hum Mutat 7:167-171.
    • (1996) Hum Mutat , vol.7 , pp. 167-171
    • Tan, C.C.1    Ainsworth, P.J.2    Hahn, A.F.3    MacLeod, P.4
  • 53
    • 0025374128 scopus 로고
    • Diffraction diagnosis of protein folding in gap junction connexons
    • Tibbitts TT, Casper LD, Phillips WC, Goodenough DA (1990) Diffraction diagnosis of protein folding in gap junction connexons. Biophys J 57:1025-1036.
    • (1990) Biophys J , vol.57 , pp. 1025-1036
    • Tibbitts, T.T.1    Casper, L.D.2    Phillips, W.C.3    Goodenough, D.A.4
  • 55
    • 0030888343 scopus 로고    scopus 로고
    • Conductances and selective permeability of connexon-43 gap junction channels examined in neonatal rat heart cells
    • Valiunas V, Bukauskas F, Weingart R (1997) Conductances and selective permeability of connexon-43 gap junction channels examined in neonatal rat heart cells. Circ Res 80:708-719.
    • (1997) Circ Res , vol.80 , pp. 708-719
    • Valiunas, V.1    Bukauskas, F.2    Weingart, R.3
  • 56
    • 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 TW, Bruzzone R, Wolfram S, Paul DL, Goodenough DA (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


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