메뉴 건너뛰기




Volumn 62, Issue 2, 2004, Pages 268-275

Structural bases for the chemical regulation of Connexin43 channels

Author keywords

Connexin; Cx43; Gap junction regulation; Gap junctions

Indexed keywords

AMINO ACID; ANTIBODY; CONNEXIN 43; GAP JUNCTION PROTEIN;

EID: 1942470893     PISSN: 00086363     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cardiores.2003.12.030     Document Type: Review
Times cited : (88)

References (39)
  • 1
    • 0034671950 scopus 로고    scopus 로고
    • Regulation of gap junctions by phosphorylation of connexins
    • Lampe P.D., Lau A.F. Regulation of gap junctions by phosphorylation of connexins. Arch. Biochem. Biophys. 384:2000;205-215.
    • (2000) Arch. Biochem. Biophys. , vol.384 , pp. 205-215
    • Lampe, P.D.1    Lau, A.F.2
  • 2
    • 0035806979 scopus 로고    scopus 로고
    • Gap junction protein connexin-43 interacts directly with microtubules
    • Giepmans B.N., Verlaan I., Hengeveld T.et al. Gap junction protein connexin-43 interacts directly with microtubules. Curr. Biol. 11:2001;1364-1368.
    • (2001) Curr. Biol. , vol.11 , pp. 1364-1368
    • Giepmans, B.N.1    Verlaan, I.2    Hengeveld, T.3
  • 3
    • 0032557460 scopus 로고    scopus 로고
    • Direct association of the gap junction protein connexin-43 with ZO-1 in cardiac myocytes
    • Toyofuku T., Yabuki M., Otsu K., Kuzuya T., Hori M., Tada M. 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
  • 4
    • 0035895649 scopus 로고    scopus 로고
    • Conduction slowing and sudden arrhythmic death in mice with cardiac-restricted inactivation of Connexin43
    • Gutstein D.E., Morley G.E., Tamaddon H.et al. Conduction slowing and sudden arrhythmic death in mice with cardiac-restricted inactivation of Connexin43. Circ. Res. 88:2001;333-339.
    • (2001) Circ. Res. , vol.88 , pp. 333-339
    • Gutstein, D.E.1    Morley, G.E.2    Tamaddon, H.3
  • 5
    • 0031687130 scopus 로고    scopus 로고
    • Cx43 gap junctions in cardiac development
    • Lo C.W., Wessels A. Cx43 gap junctions in cardiac development. Trends Cardiovasc. Med. 8:1998;264-269.
    • (1998) Trends Cardiovasc. Med. , vol.8 , pp. 264-269
    • Lo, C.W.1    Wessels, A.2
  • 6
    • 0035704411 scopus 로고    scopus 로고
    • Emerging issues of connexin channels: Biophysics fills the gap
    • Harris A.L. 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
  • 7
    • 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., Taffet S., Stoner L., Delmar M., Vallano M.L., Jalife J. 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
  • 8
    • 0030050142 scopus 로고    scopus 로고
    • Intramolecular interactions mediate pH regulation of Cx43 channels
    • Morley G.E., Taffet S.M., Delmar M. Intramolecular interactions mediate pH regulation of Cx43 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
  • 9
    • 0017743723 scopus 로고
    • Inactivation of the sodium current: II. Gating current experiments
    • Armstrong C.M., Bezanilla F. Inactivation of the sodium current: II. Gating current experiments. J. Gen. Physiol. 70:1977;567-590.
    • (1977) J. Gen. Physiol. , vol.70 , pp. 567-590
    • Armstrong, C.M.1    Bezanilla, F.2
  • 10
    • 0025245612 scopus 로고
    • Restoration of inactivation in mutants of Shaker potassium channels by a peptide derived from ShB
    • Zagotta W.N., Hoshi T., Aldrich R.W. Restoration of inactivation in mutants of Shaker potassium channels by a peptide derived from ShB. Science. 250:1990;568-571.
    • (1990) Science , vol.250 , pp. 568-571
    • Zagotta, W.N.1    Hoshi, T.2    Aldrich, R.W.3
  • 11
    • 0032514173 scopus 로고    scopus 로고
    • A particle-receptor model for the insulin-induced closure of Connexin43 channels
    • Homma N., Alvarado J.L., Coombs W.et al. A particle-receptor model for the insulin-induced closure of Connexin43 channels. Circ. Res. 83:1998;27-32.
    • (1998) Circ. Res. , vol.83 , pp. 27-32
    • Homma, N.1    Alvarado, J.L.2    Coombs, W.3
  • 12
    • 0033535338 scopus 로고    scopus 로고
    • Dissection of the molecular basis of pp60(v-src) induced gating of connexin 43 gap junction channels
    • Zhou L., Kasperek E.M., Nicholson B.J. Dissection of the molecular basis of pp60(v-src) induced gating of connexin 43 gap junction channels. J. Cell Biol. 144:1999;1033-1045.
    • (1999) J. Cell Biol. , vol.144 , pp. 1033-1045
    • Zhou, L.1    Kasperek, E.M.2    Nicholson, B.J.3
  • 14
    • 0034716923 scopus 로고    scopus 로고
    • Coexpression of connexins 40 and 43 enhances the pH sensitivity of gap junctions: A model for synergistic interactions among connexins
    • Gu H., Ek-Vitorin J.F., Taffet S.M., Delmar M. Coexpression of connexins 40 and 43 enhances the pH sensitivity of gap junctions: a model for synergistic interactions among connexins. Circ. Res. 86:2000;e98-e103.
    • (2000) Circ. Res. , vol.86 , pp. 98-e103
    • Gu, H.1    Ek-Vitorin, J.F.2    Taffet, S.M.3    Delmar, M.4
  • 15
    • 0037040828 scopus 로고    scopus 로고
    • Role of the carboxyl terminal of Connexin43 in transjunctional fast voltage gating
    • Moreno A.P., Chanson M., Anumonwo J.et al. Role of the carboxyl terminal of Connexin43 in transjunctional fast voltage gating. Circ. Res. 90:2002;450-457.
    • (2002) Circ. Res. , vol.90 , pp. 450-457
    • Moreno, A.P.1    Chanson, M.2    Anumonwo, J.3
  • 16
    • 0035853435 scopus 로고    scopus 로고
    • The carboxyl terminal domain regulates the unitary conductance and voltage dependence of Connexin40 gap junction channels
    • Anumonwo J.M.B., Taffet S.M., Gu H., Chanson M., Moreno A.P., Delmar M. 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.B.1    Taffet, S.M.2    Gu, H.3    Chanson, M.4    Moreno, A.P.5    Delmar, M.6
  • 17
    • 0036629196 scopus 로고    scopus 로고
    • Protein microarrays to detect protein-protein interactions using red and green fluorescent proteins
    • Kukar T., Eckenrode S., Gu Y.et al. Protein microarrays to detect protein-protein interactions using red and green fluorescent proteins. Anal. Biochem. 306:2002;50-54.
    • (2002) Anal. Biochem. , vol.306 , pp. 50-54
    • Kukar, T.1    Eckenrode, S.2    Gu, Y.3
  • 19
    • 0037183978 scopus 로고    scopus 로고
    • PH-dependent intramolecular binding and structure involving Cx43 cytoplasmic domains
    • Duffy H.S., Sorgen P.L., Girvin M.E.et al. pH-dependent intramolecular binding and structure involving Cx43 cytoplasmic domains. J. Biol. Chem. 277:2002;36706-36714.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36706-36714
    • Duffy, H.S.1    Sorgen, P.L.2    Girvin, M.E.3
  • 20
    • 0008565479 scopus 로고    scopus 로고
    • Plasmon resonance spectroscopy: Probing molecular interactions within membranes
    • Salamon Z., Brown M.F., Tollin G. Plasmon resonance spectroscopy: probing molecular interactions within membranes. Trends Biochem. Sci. 24:1999;213-219.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 213-219
    • Salamon, Z.1    Brown, M.F.2    Tollin, G.3
  • 21
    • 0038491346 scopus 로고    scopus 로고
    • Phospholipid-associated annexin A2-S100A10 heterotetramer and its subunits: Characterization of the interaction with tissue plasminogen activator, plasminogen, and plasmin
    • MacLeod T.J., Kwon M., Filipenko N.R., Waisman D.M. Phospholipid- associated annexin A2-S100A10 heterotetramer and its subunits: characterization of the interaction with tissue plasminogen activator, plasminogen, and plasmin. J. Biol. Chem. 278:2003;25577-25584.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25577-25584
    • MacLeod, T.J.1    Kwon, M.2    Filipenko, N.R.3    Waisman, D.M.4
  • 22
    • 0035754533 scopus 로고    scopus 로고
    • Functional demonstration of connexin-protein binding using surface plasmon resonance
    • Duffy H.S., Delmar M., Coombs W.C.et al. Functional demonstration of connexin-protein binding using surface plasmon resonance. J. Cell Adhes. Commun. 8:2001;225-229.
    • (2001) J. Cell Adhes. Commun. , vol.8 , pp. 225-229
    • Duffy, H.S.1    Delmar, M.2    Coombs, W.C.3
  • 23
    • 0032548467 scopus 로고    scopus 로고
    • Formation of the b subunit dimer is necessary for interaction with F1-ATPase
    • Sorgen P.L., Bubb M.R., McCormick K.A., Edison A.S., Cain B.D. Formation of the b subunit dimer is necessary for interaction with F1-ATPase. Biochemistry. 37:1998;923-932.
    • (1998) Biochemistry , vol.37 , pp. 923-932
    • Sorgen, P.L.1    Bubb, M.R.2    McCormick, K.A.3    Edison, A.S.4    Cain, B.D.5
  • 24
    • 58149362694 scopus 로고
    • An improved diffusion-ordered spectroscopy experiment incorporating bipolar-gradient pulse
    • Wu D., Chen A., Johnson C.S. Jr. An improved diffusion-ordered spectroscopy experiment incorporating bipolar-gradient pulse. J. Magn. Reson., Ser. A. 115:1995;260-264.
    • (1995) J. Magn. Reson., Ser. A. , vol.115 , pp. 260-264
    • Wu, D.1    Chen, A.2    Johnson, C.S.Jr.3
  • 26
    • 0018905597 scopus 로고
    • Structure of the junction between communicating cells
    • Unwin P.N., Zampighi G. Structure of the junction between communicating cells. Nature. 283:1980;545-549.
    • (1980) Nature , vol.283 , pp. 545-549
    • Unwin, P.N.1    Zampighi, G.2
  • 27
    • 0021139243 scopus 로고
    • Two configurations of a channel-forming membrane protein
    • Unwin P.N., Ennis P.D. Two configurations of a channel-forming membrane protein. Nature. 307:1984;609-613.
    • (1984) Nature , vol.307 , pp. 609-613
    • Unwin, P.N.1    Ennis, P.D.2
  • 28
    • 1942430281 scopus 로고
    • Structural domains in gap junctions: Implications for the control of intercellular communication
    • M.V.L. Bennett, & D.C. Spray. New York: Cold Spring Harbor Laboratory
    • Makowski L. Structural domains in gap junctions: implications for the control of intercellular communication. Bennett M.V.L., Spray D.C. Gap junctions. 1985;5-12 Cold Spring Harbor Laboratory, New York.
    • (1985) Gap Junctions , pp. 5-12
    • Makowski, L.1
  • 29
    • 0025374128 scopus 로고
    • Diffraction diagnosis of protein folding in gap junction connexons
    • Tibbitts T.T., Caspar D.L., Phillips W.C., Goodenough D.A. Diffraction diagnosis of protein folding in gap junction connexons. Biophys. J. 57:1990;1025-1036.
    • (1990) Biophys. J. , vol.57 , pp. 1025-1036
    • Tibbitts, T.T.1    Caspar, D.L.2    Phillips, W.C.3    Goodenough, D.A.4
  • 30
    • 0033582686 scopus 로고    scopus 로고
    • Three-dimensional structure of a recombinant gap junction membrane channel
    • Unger V.M., Kumar N.M., Gilula N.B., Yeager M. Three-dimensional structure of a recombinant gap junction membrane channel. Science. 283:1999;1176-1180.
    • (1999) Science , vol.283 , pp. 1176-1180
    • Unger, V.M.1    Kumar, N.M.2    Gilula, N.B.3    Yeager, M.4
  • 31
    • 0037191101 scopus 로고    scopus 로고
    • Identification of amino acid residues lining the pore of a gap junction channel
    • Skerrett I.M., Aronowitz J., Shin J.H.et al. Identification of amino acid residues lining the pore of a gap junction channel. J. Cell Biol. 159:2002;349-360.
    • (2002) J. Cell Biol. , vol.159 , pp. 349-360
    • Skerrett, I.M.1    Aronowitz, J.2    Shin, J.H.3
  • 32
    • 0036367764 scopus 로고    scopus 로고
    • Sequence-specific resonance assignment of the carboxyl terminal domain of Connexin43
    • Sorgen P.L., Duffy H.S., Cahill S.M.et al. Sequence-specific resonance assignment of the carboxyl terminal domain of Connexin43. J. Biomol. NMR. 23:2002;245-246.
    • (2002) J. Biomol. NMR , vol.23 , pp. 245-246
    • Sorgen, P.L.1    Duffy, H.S.2    Cahill, S.M.3
  • 33
    • 0035923431 scopus 로고    scopus 로고
    • First images of a glutamate receptor ion channel: Oligomeric state and molecular dimensions of GluRB homomers
    • Safferling M., Tichelaar W., Kummerle G.et al. First images of a glutamate receptor ion channel: oligomeric state and molecular dimensions of GluRB homomers. Biochemistry. 20(40):2001;13948-13953.
    • (2001) Biochemistry , vol.20 , Issue.40 , pp. 13948-13953
    • Safferling, M.1    Tichelaar, W.2    Kummerle, G.3
  • 34
    • 0037073789 scopus 로고    scopus 로고
    • Carboxyl-terminal sequences critical for inositol 1,4,5-trisphosphate receptor subunit assembly
    • Galvan D.L., Mignery G.A. Carboxyl-terminal sequences critical for inositol 1,4,5-trisphosphate receptor subunit assembly. J. Biol. Chem. 277:2002;48248-48260.
    • (2002) J. Biol. Chem. , vol.277 , pp. 48248-48260
    • Galvan, D.L.1    Mignery, G.A.2
  • 35
    • 0037179793 scopus 로고    scopus 로고
    • Multimerization of the ligand binding domains of cyclic nucleotide-gated channels
    • Matulef K., Zagotta W. Multimerization of the ligand binding domains of cyclic nucleotide-gated channels. Neuron. 36:2002;93-103.
    • (2002) Neuron , vol.36 , pp. 93-103
    • Matulef, K.1    Zagotta, W.2
  • 36
    • 0035896527 scopus 로고    scopus 로고
    • Interaction of c-Src with gap junction protein connexin-43. Role in the regulation of cell-cell communication
    • Giepmans B.N., Hengeveld T., Postma F.R., Moolenaar W.H. 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
  • 37
    • 0037035519 scopus 로고    scopus 로고
    • Connexin family members target to lipid raft domains and interact with caveolin-1
    • Schubert A.L., Schubert W., Spray D.C., Lisanti M.P. 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
  • 39
    • 0035833252 scopus 로고    scopus 로고
    • Modulation of mouse neural crest cell motility by N-cadherin and Connexin43 junctions
    • Xu X., Li W.E., Huang G.Y.et al. Modulation of mouse neural crest cell motility by N-cadherin and Connexin43 junctions. J. Cell Biol. 154:2001;217-230.
    • (2001) J. Cell Biol. , vol.154 , pp. 217-230
    • Xu, X.1    Li, W.E.2    Huang, G.Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.