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Volumn 159, Issue 2, 2002, Pages 349-359

Identification of amino acid residues lining the pore of a gap junction channel

Author keywords

Accessibility; Connexin32; Pore lining; SCAM; Xenopus oocyte expression

Indexed keywords

AMINO ACID; CYSTEINE; GAP JUNCTION PROTEIN;

EID: 0037191101     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200207060     Document Type: Article
Times cited : (76)

References (41)
  • 1
    • 0027987062 scopus 로고
    • Identification of acetylcholine receptor channel-lining residues in the entire M2 segment of the α subunit
    • Akabas, M.H., C. Kaufmann, P. Archdeacon, and A. Karlin. 1994. Identification of acetylcholine receptor channel-lining residues in the entire M2 segment of the α subunit. Neuron. 13:919-927.
    • (1994) Neuron , vol.13 , pp. 919-927
    • Akabas, M.H.1    Kaufmann, C.2    Archdeacon, P.3    Karlin, A.4
  • 2
    • 0034120338 scopus 로고    scopus 로고
    • The influence of surface charges on the conductance of the human connexin37 gap junction channel
    • Banach, K., S.V. Ramanan, and P.R. Brink. 2000. The influence of surface charges on the conductance of the human connexin37 gap junction channel. Biophys. J. 78:752-760.
    • (2000) Biophys. J. , vol.78 , pp. 752-760
    • Banach, K.1    Ramanan, S.V.2    Brink, P.R.3
  • 4
    • 0032579554 scopus 로고    scopus 로고
    • Isoform composition of connexin channels determines selectivity among second messengers and uncharged molecules
    • Bevans, C.G., M. Kordel, S.K. Rhee, and A.L. Harris. 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
  • 5
    • 0019319352 scopus 로고
    • Evidence for fixed charge in the nexus
    • Brink, P.R., and M.M. Dewey. 1980. Evidence for fixed charge in the nexus. Nature. 285:101-102.
    • (1980) Nature , vol.285 , pp. 101-102
    • Brink, P.R.1    Dewey, M.M.2
  • 7
    • 0344171987 scopus 로고    scopus 로고
    • Altered formation of hemichannels and gap junction channels caused by C-terminal connexin-32 mutations
    • Castro, C., J.M. Gomez-Hernandez, K. Silander, and L.C. Barrio. 1999. Altered formation of hemichannels and gap junction channels caused by C-terminal connexin-32 mutations. J. Neurosci. 19:3752-3760.
    • (1999) J. Neurosci. , vol.19 , pp. 3752-3760
    • Castro, C.1    Gomez-Hernandez, J.M.2    Silander, K.3    Barrio, L.C.4
  • 11
    • 0033224243 scopus 로고    scopus 로고
    • Selective transfer of endogenous metabolites through gap junctions composed of different connexins
    • Goldberg, G.S., P.D. Lampe, and B.J. Nicholson. 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
  • 12
    • 0018782409 scopus 로고
    • Structure and biochemistry of mouse hepatic gap junctions
    • Henderson, D., H. Eibl, and K. Weber. 1979. Structure and biochemistry of mouse hepatic gap junctions. J. Mol. Biol. 132:193-218.
    • (1979) J. Mol. Biol. , vol.132 , pp. 193-218
    • Henderson, D.1    Eibl, H.2    Weber, K.3
  • 13
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using polymerase chain reaction
    • Ho, S.N., R.M. Hunt, J.K. Horton, J.K. Pullen, and L.R. Pease. 1989. Site-directed mutagenesis by overlap extension using polymerase chain reaction. Gene. 77:51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, R.M.2    Horton, J.K.3    Pullen, J.K.4    Pease, L.R.5
  • 16
    • 0032321487 scopus 로고    scopus 로고
    • Substituted cysteine accessibility method
    • Pt. B., P.M. Conn, editor. Academic Press Inc., San Diego, CA
    • Karlin, A., and M.H. Akabas. 1998. Substituted cysteine accessibility method. In Methods in Enzymology; Ion Channels. Pt. B. Vol. 293, P.M. Conn, editor. Academic Press Inc., San Diego, CA. 123-145.
    • (1998) Methods in Enzymology; Ion Channels , vol.293 , pp. 123-145
    • Karlin, A.1    Akabas, M.H.2
  • 17
    • 0035186795 scopus 로고    scopus 로고
    • Human diseases: Clues to cracking the connexin code?
    • Kelsell, D.P., J. Dunlop, and M.B. Hodgins. 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
  • 18
    • 0034728347 scopus 로고    scopus 로고
    • Effects of aromatic residues at the ends of transmembrane α-helices on helix interactions with lipid bilayers
    • Mall, S., R. Broadbridge, R.P. Sharma, A.G. Lee, and J.M. East. 2000. Effects of aromatic residues at the ends of transmembrane α-helices on helix interactions with lipid bilayers. Biochemistry. 39:2071-2078.
    • (2000) Biochemistry , vol.39 , pp. 2071-2078
    • Mall, S.1    Broadbridge, R.2    Sharma, R.P.3    Lee, A.G.4    East, J.M.5
  • 19
    • 0024095587 scopus 로고
    • Topology of the 32-kd liver gap junction protein determined by site-directed antibody localizations
    • Milks, L.C., N.M. Kumar, R. Houghten, N. Unwin, and N.B. Gilula. 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
  • 21
    • 0030777706 scopus 로고    scopus 로고
    • Changes in permeability caused by connexin 32 mutations underlie X-linked Charcot-Marie-tooth disease
    • Oh, S., Y. Ri, M.V.L. Bennett, B. Trexler, V.K. Verselis, and T.A. Bargiello. 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, B.4    Verselis, V.K.5    Bargiello, T.A.6
  • 22
    • 0032888052 scopus 로고    scopus 로고
    • Molecular determinants of electrical rectification of single channel conductance in gap junctions formed by connexins 26 and 32
    • Oh, S., J.B. Rubin, M.V.L. Bennett, V.K. Verselis, and T.A. Bargiello. 1999. Molecular determinants of electrical rectification of single channel conductance in gap junctions formed by connexins 26 and 32. J. Gen. Physiol. 114:339-364.
    • (1999) J. Gen. Physiol. , vol.114 , pp. 339-364
    • Oh, S.1    Rubin, J.B.2    Bennett, M.V.L.3    Verselis, V.K.4    Bargiello, T.A.5
  • 23
    • 0022531305 scopus 로고
    • Molecular cloning of cDNA for rat liver gap junction protein
    • Paul, D.L. 1986. Molecular cloning of cDNA for rat liver gap junction protein. J Cell Biol. 103:123-124.
    • (1986) J. Cell Biol. , vol.103 , pp. 123-124
    • Paul, D.L.1
  • 24
    • 0026352039 scopus 로고
    • Connexin 46, a novel lens gap junction protein induces voltage-gated currents in nonjunctional plasma membrane of Xenopus oocytes
    • Paul, D.L., L. Ebihara, L.J. Takemoto, K.I. Swenson, and D.A. Goodenough. 1991. Connexin 46, 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
  • 25
    • 0035012765 scopus 로고    scopus 로고
    • Innexins get into the gap
    • Phelan, P., and T.A. Starrich. 2001. Innexins get into the gap. Bioessays. 23:388-396.
    • (2001) Bioessays , vol.23 , pp. 388-396
    • Phelan, P.1    Starrich, T.A.2
  • 27
    • 0033063884 scopus 로고    scopus 로고
    • The role of a conserved proline residue in mediating conformational changes associated with voltage gating of Cx32 gap junctions
    • Ri, Y., J.A. Ballesteros, C.K. Abrams, S. Oh, V.K. Verselis, H. Weinstein, and T.A. Bargiello. 1999. The role of a conserved proline residue in mediating conformational changes associated with voltage gating of Cx32 gap junctions. Biophys. J. 76:2887-2898.
    • (1999) Biophys. J. , vol.76 , pp. 2887-2898
    • Ri, Y.1    Ballesteros, J.A.2    Abrams, C.K.3    Oh, S.4    Verselis, V.K.5    Weinstein, H.6    Bargiello, T.A.7
  • 28
    • 0011241097 scopus 로고    scopus 로고
    • Mechanistic differences between chemical and electrical gating of gap junctions
    • C. Peracchia, editor. Academic Press Inc., San Diego, CA
    • Skerrett, I.M., J.F. Smith, and B.J. Nicholson. 1999. Mechanistic differences between chemical and electrical gating of gap junctions. In Current Topics in Membranes. C. Peracchia, editor. Academic Press Inc., San Diego, CA. 249-269.
    • (1999) Current Topics in Membranes , pp. 249-269
    • Skerrett, I.M.1    Smith, J.F.2    Nicholson, B.J.3
  • 29
    • 0035221185 scopus 로고    scopus 로고
    • Applying the Xenopus oocyte expression system to the analysis of gap junction proteins
    • Connexin methods and protocols. R. Bruzzone and C. Giaume, editors. Humana Press, NJ
    • Skerrett, I.M., M. Merritt, L. Zhou, H. Zhu, F.-L. Cao, J.F. Smith, and B.J. Nicholson. 2000. Applying the Xenopus oocyte expression system to the analysis of gap junction proteins. In Methods in Molecular Biology. Connexin methods and protocols. R. Bruzzone and C. Giaume, editors. Humana Press, NJ. 225-249.
    • (2000) Methods in Molecular Biology , pp. 225-249
    • Skerrett, I.M.1    Merritt, M.2    Zhou, L.3    Zhu, H.4    Cao, F.-L.5    Smith, J.F.6    Nicholson, B.J.7
  • 31
    • 4243369775 scopus 로고    scopus 로고
    • "Negative" physiology: What connexin-deficient mice reveal about the functional role of individual gap junction proteins
    • C. Peracchia, editor. Academic Press Inc., San Diego, CA
    • Spray, D.C., T. Kojima, E. Scemes, O. Suadicani, Y. Gao, S. Zhao, and A. Fort. 2000. "Negative" physiology: What connexin-deficient mice reveal about the functional role of individual gap junction proteins. In Gap Junctions The Molecular Basis of Cell Communication in Health and Disease. Vol 49. C. Peracchia, editor. Academic Press Inc., San Diego, CA. 1-22.
    • (2000) Gap Junctions The Molecular Basis of Cell Communication in Health and Disease , vol.49 , pp. 1-22
    • Spray, D.C.1    Kojima, T.2    Scemes, E.3    Suadicani, O.4    Gao, Y.5    Zhao, S.6    Fort, A.7
  • 33
    • 0027442575 scopus 로고
    • Identification of a proline residue as a transduction element involved in voltage gating of gap junctions
    • Suchyna, T.M., L.X. 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    Xu, L.X.2    Gao, F.3    Fourtner, C.R.4    Nicholson, B.J.5
  • 34
    • 0032764028 scopus 로고    scopus 로고
    • Different ionic selectivities for connexins 26 and 32 produce rectifying gap junction channels
    • Suchyna, T.M., J.M. Nitsche, M. Chilton, A.L. Harris, R. Veenstra, and B.J. Nicholson. 1999. Different ionic selectivities for connexins 26 and 32 produce rectifying gap junction channels. Biophys. J. 77:2968-2987.
    • (1999) Biophys. J. , vol.77 , pp. 2968-2987
    • Suchyna, T.M.1    Nitsche, J.M.2    Chilton, M.3    Harris, A.L.4    Veenstra, R.5    Nicholson, B.J.6
  • 35
    • 0033636361 scopus 로고    scopus 로고
    • The first extracellular loop domain is a major determinant of charge selectivity in connexin46 channels
    • Trexler E.B., F.F. Bukauskas, J. Kronengold, T.A. Bargiello, and V.K. Verselis. 2000. The first extracellular loop domain is a major determinant of charge selectivity in connexin46 channels. Biophys. J. 79:3036-3051.
    • (2000) Biophys. J. , vol.79 , pp. 3036-3051
    • Trexler, E.B.1    Bukauskas, F.F.2    Kronengold, J.3    Bargiello, T.A.4    Verselis, V.K.5
  • 36
    • 0033582686 scopus 로고    scopus 로고
    • Three-dimensional structure of a recombinant gap junction membrane channel
    • Unger, M.V., N.M. Kumar, N.B. Gilula, and M. Yeager. 1999. Three-dimensional structure of a recombinant gap junction membrane channel. Science. 283: 1176-1180.
    • (1999) Science , vol.283 , pp. 1176-1180
    • Unger, M.V.1    Kumar, N.M.2    Gilula, N.B.3    Yeager, M.4
  • 37
    • 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. and Biomembr. 28:327-337.
    • (1996) J. Bioenerg. and Biomembr. , vol.28 , pp. 327-337
    • Veenstra, R.D.1
  • 38
    • 0037059499 scopus 로고    scopus 로고
    • Unique and redundant connexin contributions to lens development
    • White, T.W. 2002. Unique and redundant connexin contributions to lens development. Science. 295:319-320.
    • (2002) Science , vol.295 , pp. 319-320
    • White, T.W.1
  • 39
    • 0032750784 scopus 로고    scopus 로고
    • γ-Aminobutyric acid increases the water accessibility of M3 membrane-spanning segment residues in γ-aminobutyric acid type A receptors
    • Williams, D.B., and M.H. Akabas. 1999. γ-Aminobutyric acid increases the water accessibility of M3 membrane-spanning segment residues in γ-aminobutyric acid type A receptors. Biophys. J. 77:2563-2574.
    • (1999) Biophys. J. , vol.77 , pp. 2563-2574
    • Williams, D.B.1    Akabas, M.H.2
  • 40
    • 0029932193 scopus 로고    scopus 로고
    • Structure of gap junction intercellular channels
    • Yeager, M., and B.J. Nicholson. 1996. Structure of gap junction intercellular channels. Curr. Opin. Struct. Biol. 6:183-192.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 183-192
    • Yeager, M.1    Nicholson, B.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.