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Volumn 194, Issue 1, 2003, Pages 59-76

Sequence and phylogenetic analyses of 4 TMS junctional proteins of animals: Connexins, innexins, claudins and occludins

Author keywords

Claudins; Connexins; Evolution; Gap junctions; Innexins; Intercellular communication; Occludins; Tight junctions

Indexed keywords

CLAUDIN; CYSTEINE; GAP JUNCTION PROTEIN; INNEXIN; OCCLUDIN; UNCLASSIFIED DRUG;

EID: 0042386241     PISSN: 00222631     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00232-003-2026-8     Document Type: Article
Times cited : (74)

References (64)
  • 2
    • 0034038626 scopus 로고    scopus 로고
    • Multiple domains of occludin are involved in the regulation of paracellular permeability
    • Balda, M.S., Flores-Maldonado, C., Cereijido, M., Matter, K. 2000. Multiple domains of occludin are involved in the regulation of paracellular permeability. J. Cell. Biochem. 78:85-96
    • (2000) J. Cell. Biochem. , vol.78 , pp. 85-96
    • Balda, M.S.1    Flores-Maldonado, C.2    Cereijido, M.3    Matter, K.4
  • 3
    • 0000210839 scopus 로고    scopus 로고
    • Gating connexin 43 channels reconstituted in lipid vesicles by mitogen-activated protein kinase phosphorylation
    • Bevans, C.G., Kordel, M., Rhee, S.K., Harris, A.L. 1998. Gating connexin 43 channels reconstituted in lipid vesicles by mitogen-activated protein kinase phosphorylation. J. Biol. Chem. 274:5581-5587.
    • (1998) J. Biol. Chem. , vol.274 , pp. 5581-5587
    • Bevans, C.G.1    Kordel, M.2    Rhee, S.K.3    Harris, A.L.4
  • 4
    • 0023551497 scopus 로고
    • Connexin 43: A protein from rat heart homologous to a gap junction protein from liver
    • Beyer, E.G., Paul, D.L., Goodenough, D.A. 1987. Connexin 43: A protein from rat heart homologous to a gap junction protein from liver. J. Cell Biol. 105:2621-2629
    • (1987) J. Cell Biol. , vol.105 , pp. 2621-2629
    • Beyer, E.G.1    Paul, D.L.2    Goodenough, D.A.3
  • 6
    • 0036085515 scopus 로고    scopus 로고
    • Claudins create charge-selective channels in the paracellular pathway between epithelial cells
    • Colegio, O.R., Van Itallie, C.M., McCrea, H.J., Rahner, C., Anderson, J.M. 2002. Claudins create charge-selective channels in the paracellular pathway between epithelial cells. Am. J. Physiol. 283:C142-C147
    • (2002) Am. J. Physiol. , vol.283
    • Colegio, O.R.1    Van Itallie, C.M.2    McCrea, H.J.3    Rahner, C.4    Anderson, J.M.5
  • 7
    • 0033199904 scopus 로고    scopus 로고
    • Xenopus laevis occludin. Identification of in vitro phosphorylation sites by protein kinase CK2 and association with cingulin
    • Cordenonsi, M., Turco, F., D'atri, F., Hammar, E., Martinucci, G., Meggio, F., Citi, S. 1999. Xenopus laevis occludin. Identification of in vitro phosphorylation sites by protein kinase CK2 and association with cingulin. Eur. J. Biochem. 264:374-384
    • (1999) Eur. J. Biochem. , vol.264 , pp. 374-384
    • Cordenonsi, M.1    Turco, F.2    D'atri, F.3    Hammar, E.4    Martinucci, G.5    Meggio, F.6    Citi, S.7
  • 8
    • 0033620627 scopus 로고    scopus 로고
    • Drosophila has several genes for gap junction proteins
    • Curtin, K.D., Zhang, Z., Wyman, R.J. 1999. Drosophila has several genes for gap junction proteins. Gene 232:191-201
    • (1999) Gene , vol.232 , pp. 191-201
    • Curtin, K.D.1    Zhang, Z.2    Wyman, R.J.3
  • 10
    • 0035991935 scopus 로고    scopus 로고
    • Molecular complexity of vertebrate tight junctions
    • D'Atri, P., Citi, S. 2002. Molecular complexity of vertebrate tight junctions. Mol. Membrane Biol. 19:103-112
    • (2002) Mol. Membrane Biol. , vol.19 , pp. 103-112
    • D'Atri, P.1    Citi, S.2
  • 11
    • 0037178703 scopus 로고    scopus 로고
    • Connexin diversity: Discriminating the message
    • Delmar, M. 2002. Connexin diversity: discriminating the message. Circ. Res. 91:85-86
    • (2002) Circ. Res. , vol.91 , pp. 85-86
    • Delmar, M.1
  • 13
    • 0017716638 scopus 로고
    • A study of communication specificity between cells in culture
    • Epstein, M.L., Gilula, N.B. 1977. A study of communication specificity between cells in culture. J. Cell Biol. 75:769-787
    • (1977) J. Cell Biol. , vol.75 , pp. 769-787
    • Epstein, M.L.1    Gilula, N.B.2
  • 14
    • 0035991948 scopus 로고    scopus 로고
    • Gap junctions: Structure and function
    • Evans, W.H., Martin, P.E.M. 2002a. Gap junctions: structure and function. Mol. Membrane Biol. 19:121-136
    • (2002) Mol. Membrane Biol. , vol.19 , pp. 121-136
    • Evans, W.H.1    Martin, P.E.M.2
  • 15
    • 0036793384 scopus 로고    scopus 로고
    • Lighting up gap junction channels in a flash
    • Evans, W.H., Martin, P.E. 2002b. Lighting up gap junction channels in a flash. Bioessays 24:876-880
    • (2002) Bioessays , vol.24 , pp. 876-880
    • Evans, W.H.1    Martin, P.E.2
  • 16
    • 0025025261 scopus 로고
    • Progressive alignment and phylogenetic tree construction of protein sequences
    • Feng, D.-F., Doolittle, R.F. 1990. Progressive alignment and phylogenetic tree construction of protein sequences. Methods Enzymol. 183:375-387
    • (1990) Methods Enzymol. , vol.183 , pp. 375-387
    • Feng, D.-F.1    Doolittle, R.F.2
  • 17
    • 0344959602 scopus 로고    scopus 로고
    • Developmental expression and molecular characterization of two gap junction channel proteins during embryogenesis in the grasshopper Schistocerca americana
    • Ganfornina, M.D., Sanchez, D., Herrera, M., Bastiani, M.J. 1999. Developmental expression and molecular characterization of two gap junction channel proteins during embryogenesis in the grasshopper Schistocerca americana. Dev. Genet. 24:137-150
    • (1999) Dev. Genet. , vol.24 , pp. 137-150
    • Ganfornina, M.D.1    Sanchez, D.2    Herrera, M.3    Bastiani, M.J.4
  • 19
    • 0037206173 scopus 로고    scopus 로고
    • Self-regulation of rat liver GAP junction by phosphorylation
    • Ghosh, P., Ghosh, S., Das, S. 2002. Self-regulation of rat liver GAP junction by phosphorylation. Biochim. Biophys. Acta 1564:500-504
    • (2002) Biochim. Biophys. Acta , vol.1564 , pp. 500-504
    • Ghosh, P.1    Ghosh, S.2    Das, S.3
  • 20
    • 0036301036 scopus 로고    scopus 로고
    • Isolation and characterization of gap junctions from tissue culture cells
    • Hand, G.M., Muller, D.J., Nicholson, B.J., Engel, A., Sosinsky, G.E. 2002. Isolation and characterization of gap junctions from tissue culture cells. J. Mol. Biol. 315:587-600
    • (2002) J. Mol. Biol. , vol.315 , pp. 587-600
    • Hand, G.M.1    Muller, D.J.2    Nicholson, B.J.3    Engel, A.4    Sosinsky, G.E.5
  • 21
    • 0035704411 scopus 로고    scopus 로고
    • Emerging issues of connexin channels: Biophysics fills the gap
    • Harris, A.L. 2001. Emerging issues of connexin channels: biophysics fills the gap. Q. Rev. Biophys. 34:325-472
    • (2001) Q. Rev. Biophys. , vol.34 , pp. 325-472
    • Harris, A.L.1
  • 22
    • 0035102580 scopus 로고    scopus 로고
    • The roles of claudin superfamily proteins in paracellular transport
    • Heiskala, M., Peterson, P.A., Yang, Y. 2001. The roles of claudin superfamily proteins in paracellular transport. Traffic 2:93-98
    • (2001) Traffic , vol.2 , pp. 93-98
    • Heiskala, M.1    Peterson, P.A.2    Yang, Y.3
  • 23
    • 0036796629 scopus 로고    scopus 로고
    • Anti-convulsant actions of gap junctional blockers in an in vitro seizure model
    • Jahromi, S.S., Wentlandt, K., Piran, S., Carlen, P.L. 2002. Anti-convulsant actions of gap junctional blockers in an in vitro seizure model. J. Neurophysiol. 88:1893-1902
    • (2002) J. Neurophysiol. , vol.88 , pp. 1893-1902
    • Jahromi, S.S.1    Wentlandt, K.2    Piran, S.3    Carlen, P.L.4
  • 24
    • 0000210839 scopus 로고    scopus 로고
    • Gating connexin 43 channels reconstituted in lipid vesicles by mitogen activated protein kinase phosphorylation
    • Kim, D.Y., Kam, Y., Koo, S.K., Joe, C.O. 1999. Gating connexin 43 channels reconstituted in lipid vesicles by mitogen activated protein kinase phosphorylation. J. Biol. Chem. 274:5581
    • (1999) J. Biol. Chem. , vol.274 , pp. 5581
    • Kim, D.Y.1    Kam, Y.2    Koo, S.K.3    Joe, C.O.4
  • 26
    • 0036208599 scopus 로고    scopus 로고
    • Differential expression patterns of claudins, tight junction membrane proteins, in mouse nephron segments
    • Kiuchi-Saishin, Y., Gotoh, S., Furuse, M., Takasuga, A., Tano, Y., Tsukita, S. 2002. Differential expression patterns of claudins, tight junction membrane proteins, in mouse nephron segments. J. Am. Soc. Nephrol. 13:875-886
    • (2002) J. Am. Soc. Nephrol. , vol.13 , pp. 875-886
    • Kiuchi-Saishin, Y.1    Gotoh, S.2    Furuse, M.3    Takasuga, A.4    Tano, Y.5    Tsukita, S.6
  • 28
    • 0030028301 scopus 로고    scopus 로고
    • The gap junction communication channel
    • Kumar, N.M., 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
  • 29
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., Doolittle, R.F. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 31
    • 0036690912 scopus 로고    scopus 로고
    • Tight junctions and compositionally related junctional structures in mammalian stratified epithelia and cell cultures derived therefrom
    • Langbein, L., Grund, C., Kuhn, C., Praetzel, S., Kartenbeck, J., Brandner, J.M., Moll, I., Franke, W.W. 2002. Tight junctions and compositionally related junctional structures in mammalian stratified epithelia and cell cultures derived therefrom. Eur. J. Cell Biol. 81:419-435
    • (2002) Eur. J. Cell Biol. , vol.81 , pp. 419-435
    • Langbein, L.1    Grund, C.2    Kuhn, C.3    Praetzel, S.4    Kartenbeck, J.5    Brandner, J.M.6    Moll, I.7    Franke, W.W.8
  • 32
    • 0033021324 scopus 로고    scopus 로고
    • Flexible programs for the prediction of average amphipathicity of multiply aligned homologous proteins: Application to integral membrane transport proteins
    • Le, T., Tseng, T.T., Saier, M.H., Jr. 1999. Flexible programs for the prediction of average amphipathicity of multiply aligned homologous proteins: Application to integral membrane transport proteins. Mol. Membr. Biol. 16:173-179
    • (1999) Mol. Membr. Biol. , vol.16 , pp. 173-179
    • Le, T.1    Tseng, T.T.2    Saier M.H., Jr.3
  • 33
    • 0023652370 scopus 로고
    • The cell-to-cell channel of gap junctions
    • Loewenstein, W.R. 1987. The cell-to-cell channel of gap junctions. Cell 48:725-726
    • (1987) Cell , vol.48 , pp. 725-726
    • Loewenstein, W.R.1
  • 34
    • 0035503028 scopus 로고    scopus 로고
    • Expression of Clostridium perfringens enterotoxin receptors claudin-3 and claudin-4 in prostate cancer epithelium
    • Long, H., Crean, C.D., Lee, W.H., Cummings, O.W., Gabig, T.G. 2001. Expression of Clostridium perfringens enterotoxin receptors claudin-3 and claudin-4 in prostate cancer epithelium. Cancer Res. 61:7878-7881
    • (2001) Cancer Res. , vol.61 , pp. 7878-7881
    • Long, H.1    Crean, C.D.2    Lee, W.H.3    Cummings, O.W.4    Gabig, T.G.5
  • 35
    • 0035754495 scopus 로고    scopus 로고
    • Distribution and dynamics of gap junction channels revealed in living cells
    • Lopez, P., Balicki, D., Buehler, L.K., Falk, M.M., Chen, S.C. 2001. Distribution and dynamics of gap junction channels revealed in living cells. Cell Adhes. Commun. 8:237-242
    • (2001) Cell Adhes. Commun. , vol.8 , pp. 237-242
    • Lopez, P.1    Balicki, D.2    Buehler, L.K.3    Falk, M.M.4    Chen, S.C.5
  • 37
    • 0034177273 scopus 로고    scopus 로고
    • Clostridium perfringens enterotoxin and intestinal tight junctions
    • McClane, B.A. 2000. Clostridium perfringens enterotoxin and intestinal tight junctions. Trends Microbiol. 8:145-146
    • (2000) Trends Microbiol. , vol.8 , pp. 145-146
    • McClane, B.A.1
  • 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., 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
    • 0035173548 scopus 로고    scopus 로고
    • Immunolocalization of occludin and claudin-1 to tight junctions in intact CNS vessels of mammalian retina
    • Morcos, Y., Hosie, M.J., Bauer, H.C., Chan-Ling, T. 2001. Immunolocalization of occludin and claudin-1 to tight junctions in intact CNS vessels of mammalian retina. J. Neurocytol. 30:107-123
    • (2001) J. Neurocytol. , vol.30 , pp. 107-123
    • Morcos, Y.1    Hosie, M.J.2    Bauer, H.C.3    Chan-Ling, T.4
  • 40
    • 0031771296 scopus 로고    scopus 로고
    • CHR, a novel family of prokaryotic proton motive force-driven transporters probably containing chromate/sulfate antiporters
    • Nies, D.H., Koch, S., Wachi, S., Peitzsch, N., Saier, M.H., Jr. 1998. CHR, a novel family of prokaryotic proton motive force-driven transporters probably containing chromate/sulfate antiporters. J. Bacteriol. 180:5799-5802
    • (1998) J. Bacteriol. , vol.180 , pp. 5799-5802
    • Nies, D.H.1    Koch, S.2    Wachi, S.3    Peitzsch, N.4    Saier M.H., Jr.5
  • 41
    • 0029977355 scopus 로고    scopus 로고
    • Connexin 32 mutations from X-linked Charcot-Marie tooth disease patients: Functional defects and dominant negative effects
    • Omori, 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
    • Omori, Y.1    Mesnil, M.2    Yamasaki, H.3
  • 44
    • 0035012765 scopus 로고    scopus 로고
    • Innexins get into the gap
    • Phelan, P., Stanch, T.A. 2001. Innexins get into the gap. Bioessays 23:388-396
    • (2001) Bioessays , vol.23 , pp. 388-396
    • Phelan, P.1    Stanch, T.A.2
  • 45
    • 0036180091 scopus 로고    scopus 로고
    • Cloning and molecular characterization of the first innexin of the phylum annelida - Expression of the gene during development
    • Potenza, N., del Gaudio, R., Rivieccio, L., Russo, G.M., Geraci, G. 2002. Cloning and molecular characterization of the first innexin of the phylum annelida - expression of the gene during development. J. Mol. Evol. 54:312-321
    • (2002) J. Mol. Evol. , vol.54 , pp. 312-321
    • Potenza, N.1    Del Gaudio, R.2    Rivieccio, L.3    Russo, G.M.4    Geraci, G.5
  • 47
    • 0033821267 scopus 로고    scopus 로고
    • Vectorial metabolism and the evolution of transport systems
    • Saier, M.H., Jr. 2000. Vectorial metabolism and the evolution of transport systems. J. Bacteriol. 182:5029-5035
    • (2000) J. Bacteriol. , vol.182 , pp. 5029-5035
    • Saier M.H., Jr.1
  • 48
    • 0035224834 scopus 로고    scopus 로고
    • Evolution of transport proteins
    • J.K. Setlow, editor. Kluwer Academic/Plenum Publishers, New York
    • Saier, M.H., Jr. 2001. Evolution of transport proteins. In: Genetic Engineering. Principles and Methods, Vol. 23. J.K. Setlow, editor, pp. 1-9. Kluwer Academic/Plenum Publishers, New York
    • (2001) Genetic Engineering. Principles and Methods , vol.23 , pp. 1-9
    • Saier M.H., Jr.1
  • 49
    • 0036300466 scopus 로고    scopus 로고
    • Shigella flexneri regulates tight junction-associated proteins in human intestinal epithelial cells
    • Sakaguchi, T., Kohler, H., Gu, X., McCormick, B.A., Reinecker, H.C. 2002. Shigella flexneri regulates tight junction-associated proteins in human intestinal epithelial cells. Cell Microbiol. 4:367-381
    • (2002) Cell Microbiol. , vol.4 , pp. 367-381
    • Sakaguchi, T.1    Kohler, H.2    Gu, X.3    McCormick, B.A.4    Reinecker, H.C.5
  • 53
    • 0033916033 scopus 로고    scopus 로고
    • Two Drosophila innexins are expressed in overlapping domains and cooperate to form gap-junction channels
    • Stebbings, L.A., Todman, M.G., Phelan, P., Bacon, J.P., Davies, J.A. 2000. Two Drosophila innexins are expressed in overlapping domains and cooperate to form gap-junction channels. Mol. Biol. Cell 11:2459-2470
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2459-2470
    • Stebbings, L.A.1    Todman, M.G.2    Phelan, P.3    Bacon, J.P.4    Davies, J.A.5
  • 55
    • 0035674837 scopus 로고    scopus 로고
    • Epithelial cell polarity and cell junctions in Drosophila
    • Tepass, U., Tanentzapf, G., Ward, R., Fehon, R. 2001. Epithelial cell polarity and cell junctions in Drosophila. Annu. Rev. Genet. 35:747-784
    • (2001) Annu. Rev. Genet. , vol.35 , pp. 747-784
    • Tepass, U.1    Tanentzapf, G.2    Ward, R.3    Fehon, R.4
  • 56
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J.D., Gibson, T.J., Plewniak, F., Jeanmougin, F., Higgins, D.G. 1997. The CLUSTAL X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25:4876-4882
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 58
    • 0034524084 scopus 로고    scopus 로고
    • The structure and function of claudins, cell adhesion molecules at tight junctions
    • Tsukita, S., Furuse, M. 2000. The structure and function of claudins, cell adhesion molecules at tight junctions. Ann. N. Y. Acad. Sci. 915:129-135
    • (2000) Ann. N. Y. Acad. Sci. , vol.915 , pp. 129-135
    • Tsukita, S.1    Furuse, M.2
  • 59
    • 0036773738 scopus 로고    scopus 로고
    • Claudin-based barrier in simple and stratified cellular sheets
    • Tsukita, S., Furuse, M. 2002. Claudin-based barrier in simple and stratified cellular sheets. Curr. Opin. Cell. Biol. 14:531
    • (2002) Curr. Opin. Cell. Biol. , vol.14 , pp. 531
    • Tsukita, S.1    Furuse, M.2
  • 60
    • 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. 1999. Three-dimensional structure of a recombinant gap junction membrane channel. Sci. Mag. 283:1176-1180
    • (1999) Sci. Mag. , vol.283 , pp. 1176-1180
    • Unger, V.M.1    Kumar, N.M.2    Gilula, N.B.3    Yeager, M.4
  • 61
    • 0033002783 scopus 로고    scopus 로고
    • Genetic diseases and gene knockouts reveal diverse connexin functions
    • White, T.W., 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
    • 0032143942 scopus 로고    scopus 로고
    • Synthesis, assembly and structure of gap junction intercellular channels
    • Yeager, M., Unger, V.M., Falk, M.M. 1998. Synthesis, assembly and structure of gap junction intercellular channels. Curr. Opin. Struct. Biol. 8:517-524
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 517-524
    • Yeager, M.1    Unger, V.M.2    Falk, M.M.3
  • 64
    • 0035087954 scopus 로고    scopus 로고
    • The AveHAS program for the determination of average hydrophobicity, amphipathicity, and similarity
    • Zhai, Y., Saier, M.H., Jr. 2001. The AveHAS program for the determination of average hydrophobicity, amphipathicity, and similarity. J. Mol. Microbiol. Biotechnol. 3:285-286
    • (2001) J. Mol. Microbiol. Biotechnol. , vol.3 , pp. 285-286
    • Zhai, Y.1    Saier M.H., Jr.2


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