메뉴 건너뛰기




Volumn 251, Issue 2, 1999, Pages 285-298

Stimulated phosphorylation of intracellular connexin43

Author keywords

Connexin43; Gap junctions; Golgi; Phorbol esters; Vanadates

Indexed keywords

BREFELDIN A; CONNEXIN 43; MOLYBDIC ACID; MONOCLONAL ANTIBODY; PERVANADATE; PHORBOL 13 ACETATE 12 MYRISTATE; UNCLASSIFIED DRUG; ZYMED 13 8300;

EID: 0033567979     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.1999.4574     Document Type: Article
Times cited : (43)

References (45)
  • 1
    • 0018382741 scopus 로고
    • Junctional intercellular communication and the control of growth
    • Loewenstein W. R. Junctional intercellular communication and the control of growth. Biochim. Biophys. Acta. 560:1979;1-65.
    • (1979) Biochim. Biophys. Acta , vol.560 , pp. 1-65
    • Loewenstein, W.R.1
  • 2
    • 0029742875 scopus 로고    scopus 로고
    • The role of gap junction membrane channels in development
    • Lo C. W. The role of gap junction membrane channels in development. J. Bioenerg. Biomembr. 28:1996;379-385.
    • (1996) J. Bioenerg. Biomembr. , vol.28 , pp. 379-385
    • Lo, C.W.1
  • 3
    • 0029738724 scopus 로고    scopus 로고
    • Size and selectivity of gap junction channels formed from different connexins
    • Veenstra R. D. Size and selectivity of gap junction channels formed from different connexins. J. Bioenerg. Biomembr. 28:1996;327-337.
    • (1996) J. Bioenerg. Biomembr. , vol.28 , pp. 327-337
    • Veenstra, R.D.1
  • 4
    • 0029950947 scopus 로고    scopus 로고
    • Role of connexin genes in growth control
    • Yamasaki H., Naus C. C. G. Role of connexin genes in growth control. Carcinogenesis. 17:1996;1199-1213.
    • (1996) Carcinogenesis , vol.17 , pp. 1199-1213
    • Yamasaki, H.1    Naus, C.C.G.2
  • 5
    • 0025287594 scopus 로고
    • Expression of the gap junction protein connexin43 in embryonic chick lens: Molecular cloning, ultrastructural localization, and post-translational phosphorylation
    • Musil L. S., Beyer E. C., Goodenough D. A. Expression of the gap junction protein connexin43 in embryonic chick lens: Molecular cloning, ultrastructural localization, and post-translational phosphorylation. J. Membr. Biol. 116:1990;163-175.
    • (1990) J. Membr. Biol. , vol.116 , pp. 163-175
    • Musil, L.S.1    Beyer, E.C.2    Goodenough, D.A.3
  • 6
    • 0031563776 scopus 로고    scopus 로고
    • Selective monoclonal antibody recognition and cellular localization of an unphosphorylated form of connexin43
    • Nagy J. I., Li W. E. I., Roy C., Doble B. W., Gilchrist J. S., Kardami E., Hertzberg E. L. Selective monoclonal antibody recognition and cellular localization of an unphosphorylated form of connexin43. Exp. Cell Res. 236:1997;127-136.
    • (1997) Exp. Cell Res. , vol.236 , pp. 127-136
    • Nagy, J.I.1    Li, W.E.I.2    Roy, C.3    Doble, B.W.4    Gilchrist, J.S.5    Kardami, E.6    Hertzberg, E.L.7
  • 7
    • 0025155347 scopus 로고
    • Differential phosphorylation of the gap junction protein connexin43 in junctional communication-competent and -deficient cell lines
    • Musil L. S., Cunningham B. A., Edelman G. M., Goodenough D. A. Differential phosphorylation of the gap junction protein connexin43 in junctional communication-competent and -deficient cell lines. J. Cell Biol. 111:1990;2077-2088.
    • (1990) J. Cell Biol. , vol.111 , pp. 2077-2088
    • Musil, L.S.1    Cunningham, B.A.2    Edelman, G.M.3    Goodenough, D.A.4
  • 8
    • 0029878244 scopus 로고    scopus 로고
    • Regulation of cardiac gap junction channel permeability and conductance by several phosphorylating conditions
    • Kwak B. R., Jongsma H. J. Regulation of cardiac gap junction channel permeability and conductance by several phosphorylating conditions. Mol. Cell Biochem. 157:1996;93-99.
    • (1996) Mol. Cell Biochem. , vol.157 , pp. 93-99
    • Kwak, B.R.1    Jongsma, H.J.2
  • 9
    • 0026464786 scopus 로고
    • Cardiac gap junctions: Three distinct single channel conductances and their modulation by phosphorylating treatments
    • Takens-Kwak B. R., Jongsma H. J. Cardiac gap junctions: Three distinct single channel conductances and their modulation by phosphorylating treatments. Pfügers Arch. 422:1992;198-200.
    • (1992) Pfügers Arch. , vol.422 , pp. 198-200
    • Takens-Kwak, B.R.1    Jongsma, H.J.2
  • 10
    • 0026769766 scopus 로고
    • Phosphorylation shifts unitary conductance and modifies voltage dependent kinetics of human connexin43 gap junction channels
    • Moreno A. P., Fishman G. I., Spray D. C. Phosphorylation shifts unitary conductance and modifies voltage dependent kinetics of human connexin43 gap junction channels. Biophys. J. 62:1992;51-53.
    • (1992) Biophys. J. , vol.62 , pp. 51-53
    • Moreno, A.P.1    Fishman, G.I.2    Spray, D.C.3
  • 11
    • 19244369210 scopus 로고
    • Modulation of gap junctional intercellular communication by phosphorylation: Effects of growth factors, kinase activators and phosphatase inhibitors
    • Mikalsen S.-O., Husøy T., Sanner T. Modulation of gap junctional intercellular communication by phosphorylation: Effects of growth factors, kinase activators and phosphatase inhibitors. Prog. Clin. Biol. Res. 391:1995;425-438.
    • (1995) Prog. Clin. Biol. Res. , vol.391 , pp. 425-438
    • Mikalsen, S.-O.1    Husøy, T.2    Sanner, T.3
  • 12
    • 0031824861 scopus 로고    scopus 로고
    • Platelet-derived growth factor-induced disruption of gap junctional communication and phosphorylation of connexin43 involves protein kinase C and mitogen-activated protein kinase
    • Hossain M. Z., Ao P., Boynton A. L. Platelet-derived growth factor-induced disruption of gap junctional communication and phosphorylation of connexin43 involves protein kinase C and mitogen-activated protein kinase. J. Cell. Physiol. 176:1998;332-341.
    • (1998) J. Cell. Physiol. , vol.176 , pp. 332-341
    • Hossain, M.Z.1    Ao, P.2    Boynton, A.L.3
  • 13
    • 0027067884 scopus 로고
    • Epidermal growth factor disrupts gap-junctional communication and induces phosphorylation of connexin43 on serine
    • Lau A. F., Kanemitsu M. Y., Kurata W. E., Danesh S., Boynton A. L. Epidermal growth factor disrupts gap-junctional communication and induces phosphorylation of connexin43 on serine. Mol. Biol. Cell. 3:1992;865-874.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 865-874
    • Lau, A.F.1    Kanemitsu, M.Y.2    Kurata, W.E.3    Danesh, S.4    Boynton, A.L.5
  • 14
    • 0025830454 scopus 로고
    • Phorbol ester induces phosphorylation and down-regulation of connexin 43 in WB cells
    • Oh S. Y., Grupen C. G., Murray A. W. Phorbol ester induces phosphorylation and down-regulation of connexin 43 in WB cells. Biochim. Biophys. Acta. 1094:1991;243-245.
    • (1991) Biochim. Biophys. Acta , vol.1094 , pp. 243-245
    • Oh, S.Y.1    Grupen, C.G.2    Murray, A.W.3
  • 15
    • 0030022421 scopus 로고    scopus 로고
    • Characterization of the mitogen-activated protein kinase phosphorylation sites on the connexin-43 gap junction protein
    • Warn-Cramer B. J., Lampe P. D., Kurata W. E., Kanemitsu M. Y., Loo L. W. M., Eckhart W., Lau A. F. Characterization of the mitogen-activated protein kinase phosphorylation sites on the connexin-43 gap junction protein. J. Biol. Chem. 271:1996;3779-3786.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3779-3786
    • Warn-Cramer, B.J.1    Lampe, P.D.2    Kurata, W.E.3    Kanemitsu, M.Y.4    Loo, L.W.M.5    Eckhart, W.6    Lau, A.F.7
  • 17
    • 0025261843 scopus 로고
    • Phosphorylation of connexin43 gap junction protein in uninfected and Rous sarcoma virus-transformed mammalian fibroblasts
    • Crow D. S., Beyer E. C., Paul D. L., Kobe S. S., Lau A. F. Phosphorylation of connexin43 gap junction protein in uninfected and Rous sarcoma virus-transformed mammalian fibroblasts. Mol. Cell. Biol. 10:1990;1754-1763.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1754-1763
    • Crow, D.S.1    Beyer, E.C.2    Paul, D.L.3    Kobe, S.S.4    Lau, A.F.5
  • 18
    • 0025670419 scopus 로고
    • Tyrosine phosphorylation of a gap junction protein correlates with inhibition of cell-to-cell communication
    • Filson A. J., Azarnia R., Beyer E. C., Loewenstein W. R., Brugge J. S. Tyrosine phosphorylation of a gap junction protein correlates with inhibition of cell-to-cell communication. Cell Growth Differ. 1:1990;661-668.
    • (1990) Cell Growth Differ. , vol.1 , pp. 661-668
    • Filson, A.J.1    Azarnia, R.2    Beyer, E.C.3    Loewenstein, W.R.4    Brugge, J.S.5
  • 20
    • 0031026378 scopus 로고    scopus 로고
    • Induction of phosphotyrosine in the gap junction protein, connexin43
    • Mikalsen S.-O., Husøy T., Vikhamar G., Sanner T. Induction of phosphotyrosine in the gap junction protein, connexin43. FEBS Lett. 401:1997;271-275.
    • (1997) FEBS Lett. , vol.401 , pp. 271-275
    • Mikalsen, S.-O.1    Husøy, T.2    Vikhamar, G.3    Sanner, T.4
  • 21
    • 0029176855 scopus 로고
    • Gap junction turnover, intracellular trafficking, and phosphorylation of connexin43 in brefeldin A-treated rat mammary tumor cells
    • Laird D. W., Castillo M., Kasprzak L. Gap junction turnover, intracellular trafficking, and phosphorylation of connexin43 in brefeldin A-treated rat mammary tumor cells. J. Cell Biol. 131:1995;1193-1203.
    • (1995) J. Cell Biol. , vol.131 , pp. 1193-1203
    • Laird, D.W.1    Castillo, M.2    Kasprzak, L.3
  • 22
    • 0027297994 scopus 로고
    • Trapping an intermediate form of connexin43 in the Golgi
    • Puranam K. L., Laird D. W., Revel J. P. Trapping an intermediate form of connexin43 in the Golgi. Exp. Cell Res. 206:1993;85-92.
    • (1993) Exp. Cell Res. , vol.206 , pp. 85-92
    • Puranam, K.L.1    Laird, D.W.2    Revel, J.P.3
  • 23
    • 0025789648 scopus 로고
    • Biochemical analysis of connexin43 intracellular transport, phosphorylation, and assembly into gap junctional plaques
    • Musil L. S., Goodenough D. A. Biochemical analysis of connexin43 intracellular transport, phosphorylation, and assembly into gap junctional plaques. J. Cell Biol. 115:1991;1357-1374.
    • (1991) J. Cell Biol. , vol.115 , pp. 1357-1374
    • Musil, L.S.1    Goodenough, D.A.2
  • 25
    • 0032540221 scopus 로고    scopus 로고
    • Properties of pervanadate and permolbydate: Connexin43, phosphatase inhibition, and thiol reactivity as model systems
    • Mikalsen S.-O., Kaalhus O. Properties of pervanadate and permolbydate: Connexin43, phosphatase inhibition, and thiol reactivity as model systems. J. Biol. Chem. 273:1998;10036-10045.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10036-10045
    • Mikalsen, S.-O.1    Kaalhus, O.2
  • 27
    • 0030881006 scopus 로고    scopus 로고
    • Effects of peroxisome proliferators and 12-O-tetradecanoyl phorbol-13-acetate on intercellular communication and connexin43 in two hamster fibroblast systems
    • Cruciani V., Mikalsen S.-O., Vasseur P., Sanner T. Effects of peroxisome proliferators and 12-O-tetradecanoyl phorbol-13-acetate on intercellular communication and connexin43 in two hamster fibroblast systems. Int. J. Cancer. 73:1997;240-248.
    • (1997) Int. J. Cancer , vol.73 , pp. 240-248
    • Cruciani, V.1    Mikalsen, S.-O.2    Vasseur, P.3    Sanner, T.4
  • 28
    • 0028227859 scopus 로고
    • Two inhibitors of gap junctional intercellular communication, TPA and endosulfan: Different effects on phosphorylation of connexin 43 in the rat liver epithelial cell line, IAR 20
    • Kenne K., Fransson-Steen R., Honkasalo S., Wärngård L. Two inhibitors of gap junctional intercellular communication, TPA and endosulfan: Different effects on phosphorylation of connexin 43 in the rat liver epithelial cell line, IAR 20. Carcinogenesis. 15:1994;1161-1165.
    • (1994) Carcinogenesis , vol.15 , pp. 1161-1165
    • Kenne, K.1    Fransson-Steen, R.2    Honkasalo, S.3    Wärngård, L.4
  • 29
    • 0029801146 scopus 로고    scopus 로고
    • Modulation of gap junctional intercellular communication by EGF in human kidney epithelial cells
    • Rivedal E., Mollerup S., Haugen A., Vikhamar G. Modulation of gap junctional intercellular communication by EGF in human kidney epithelial cells. Carcinogenesis. 17:1996;2321-2328.
    • (1996) Carcinogenesis , vol.17 , pp. 2321-2328
    • Rivedal, E.1    Mollerup, S.2    Haugen, A.3    Vikhamar, G.4
  • 30
    • 0032191620 scopus 로고    scopus 로고
    • +-ATPase (ductin) is accompanied by down-regulation of gap junctional intercellular communication and translocation of connexin 43 in NIH3T3 cells
    • +-ATPase (ductin) is accompanied by down-regulation of gap junctional intercellular communication and translocation of connexin 43 in NIH3T3 cells. Oncogene. 17:1998;1673-1680.
    • (1998) Oncogene , vol.17 , pp. 1673-1680
    • Saito, T.1    Schlegel, R.2    Andresson, T.3    Yuge, L.4    Yamamoto, M.5    Yamasaki, H.6
  • 31
    • 0029069304 scopus 로고
    • Inhibition of rat liver gap junction intercellular communication by tumor-promoting agents in vivo: Association with aberrant localization of connexin proteins
    • Krutovskikh V. A., Mesnil M., Mazzoleni G., Yamasaki H. Inhibition of rat liver gap junction intercellular communication by tumor-promoting agents in vivo: Association with aberrant localization of connexin proteins. Lab. Invest. 72:1995;571-577.
    • (1995) Lab. Invest. , vol.72 , pp. 571-577
    • Krutovskikh, V.A.1    Mesnil, M.2    Mazzoleni, G.3    Yamasaki, H.4
  • 32
    • 85012338112 scopus 로고
    • Viral membrane proteins acquire galactose in trans Golgi cisternae during intracellular transport
    • Griffiths G., Brands R., Burke B., Louvard D., Warren G. Viral membrane proteins acquire galactose in trans Golgi cisternae during intracellular transport. J. Cell Biol. 95:1982;781-792.
    • (1982) J. Cell Biol. , vol.95 , pp. 781-792
    • Griffiths, G.1    Brands, R.2    Burke, B.3    Louvard, D.4    Warren, G.5
  • 33
    • 0020610629 scopus 로고
    • Lectin-binding sites as markers of Golgi subcompartments: Proximal-to-distal maturation of oligosaccharides
    • Tartakoff A. M., Vassalli P. Lectin-binding sites as markers of Golgi subcompartments: Proximal-to-distal maturation of oligosaccharides. J. Cell Biol. 97:1983;1243-1248.
    • (1983) J. Cell Biol. , vol.97 , pp. 1243-1248
    • Tartakoff, A.M.1    Vassalli, P.2
  • 34
    • 0031585179 scopus 로고    scopus 로고
    • A characterization of permolybdate and its effect on cellular tyrosine phosphorylation, gap junctional intercellular communication and phosphorylation status of the gap junction protein, connexin43
    • Mikalsen S.-O., Kaalhus O. A characterization of permolybdate and its effect on cellular tyrosine phosphorylation, gap junctional intercellular communication and phosphorylation status of the gap junction protein, connexin43. Biochim. Biophys. Acta. 1356:1997;207-220.
    • (1997) Biochim. Biophys. Acta , vol.1356 , pp. 207-220
    • Mikalsen, S.-O.1    Kaalhus, O.2
  • 35
    • 0030582203 scopus 로고    scopus 로고
    • A characterization of pervanadate, an inducer of cellular tyrosine phosphorylation and inhibitor of gap junctional intercellular communication
    • Mikalsen S.-O., Kaalhus O. A characterization of pervanadate, an inducer of cellular tyrosine phosphorylation and inhibitor of gap junctional intercellular communication. Biochim. Biophys. Acta. 1290:1996;308-318.
    • (1996) Biochim. Biophys. Acta , vol.1290 , pp. 308-318
    • Mikalsen, S.-O.1    Kaalhus, O.2
  • 36
    • 0024591235 scopus 로고
    • Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: Evidence for membrane cycling from Golgi to ER
    • Lippincott-Schwartz J., Yuan L. C., Bonifacino J. S., Klausner R. D. Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: Evidence for membrane cycling from Golgi to ER. Cell. 56:1989;801-813.
    • (1989) Cell , vol.56 , pp. 801-813
    • Lippincott-Schwartz, J.1    Yuan, L.C.2    Bonifacino, J.S.3    Klausner, R.D.4
  • 37
    • 0031281674 scopus 로고    scopus 로고
    • Degradation of connexin43 gap junctions involves both the proteasome and the lysosome
    • Laing J. G., Tadros P. N., Westphale E. M., Beyer E. C. Degradation of connexin43 gap junctions involves both the proteasome and the lysosome. Exp. Cell Res. 236:1997;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
  • 39
    • 0029060788 scopus 로고
    • Mutations of the connexin43 gap-junction gene in patients with heart malformations and defects of laterality
    • Britz-Cunningham S. H., Shah M. M., Zuppan C. W., Fletcher W. H. Mutations of the connexin43 gap-junction gene in patients with heart malformations and defects of laterality. N. Engl. J. Med. 332:1995;1323-1329.
    • (1995) N. Engl. J. Med. , vol.332 , pp. 1323-1329
    • Britz-Cunningham, S.H.1    Shah, M.M.2    Zuppan, C.W.3    Fletcher, W.H.4
  • 40
    • 0028168365 scopus 로고
    • Changes in gap-junction permeability, phosphorylation, and number mediated by phorbol ester and non-phorbol-ester tumor promoters in rat liver epithelial cells
    • Matesic D. F., Rupp H. L., Bonney W. J., Ruch R. J., Trosko J. E. Changes in gap-junction permeability, phosphorylation, and number mediated by phorbol ester and non-phorbol-ester tumor promoters in rat liver epithelial cells. Mol. Carcinog. 10:1994;226-236.
    • (1994) Mol. Carcinog. , vol.10 , pp. 226-236
    • Matesic, D.F.1    Rupp, H.L.2    Bonney, W.J.3    Ruch, R.J.4    Trosko, J.E.5
  • 41
    • 0028068399 scopus 로고
    • Modulation of gap junctions in senescent endothelial cells
    • Xie H. Q., Hu V. W. Modulation of gap junctions in senescent endothelial cells. Exp. Cell Res. 214:1994;172-176.
    • (1994) Exp. Cell Res. , vol.214 , pp. 172-176
    • Xie, H.Q.1    Hu, V.W.2
  • 42
    • 0030944270 scopus 로고    scopus 로고
    • A mitosis-specific phosphorylation of the gap junction protein connexin43 in human vascular cells: Biochemical characterization and localization
    • Xie H. Q., Laird D. W., Chang T. H., Hu V. W. A mitosis-specific phosphorylation of the gap junction protein connexin43 in human vascular cells: Biochemical characterization and localization. J. Cell Biol. 137:1997;203-210.
    • (1997) J. Cell Biol. , vol.137 , pp. 203-210
    • Xie, H.Q.1    Laird, D.W.2    Chang, T.H.3    Hu, V.W.4
  • 43
    • 0029005759 scopus 로고
    • Are protein-tyrosine phosphatases specific for phosphotyrosine
    • Zhang Z.-Y. Are protein-tyrosine phosphatases specific for phosphotyrosine. J. Biol. Chem. 270:1995;16052-16055.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16052-16055
    • Zhang, Z.-Y.1
  • 44
    • 0031841797 scopus 로고    scopus 로고
    • Immunorecognition, ultrastructure and phosphorylation status of astrocytic gap junctions and connexin43 in rat brain after cerebral focal ischaemia
    • Li W. E. I., Ochalski P. A. Y., Hertzberg E. L., Nagy J. I. Immunorecognition, ultrastructure and phosphorylation status of astrocytic gap junctions and connexin43 in rat brain after cerebral focal ischaemia. Eur. J. Neurosci. 10:1998;2444-2463.
    • (1998) Eur. J. Neurosci. , vol.10 , pp. 2444-2463
    • Li, W.E.I.1    Ochalski, P.A.Y.2    Hertzberg, E.L.3    Nagy, J.I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.