Expression of the gap junction protein connexin43 in embryonic chick lens: Molecular cloning, ultrastructural localization, and post-translational phosphorylation
Tóm tắt
Từ khóa
Tài liệu tham khảo
Atkinson, M.M., Menko, A.S., Johnson, R.G., Sheppard, J.R., Sheridan, J.D. 1981. Rapid and reversible reduction of junctional permeability in cells infected with a temperature-sensitive mutant of avian sarcoma virus.J. Cell Biol. 91:573–578
Azarnia, R., Reddy, S., Kmiecik, T.C., Shalloway, D., Loewenstein, W.R. 1988. The cellularsrc gene product regulates junctional cell-to-cell communication.Science 239:398–401
Benedetti, E.L., Dunia, I., Bloemendal, H. 1974. Development of junctions during differentiation of lens fibers.Proc. Natl. Acad. Sci. USA 71:5073–5077
Beyer, E.C., Goodenough, D.A., Paul, D.L. 1988. The connexins, a family of related gap junction proteins.In: Gap Junctions. E.L. Hertzberg and R.G. Johnson, editors. pp. 167–175. Alan R. Liss, New York
Beyer, E.C., Kistler, J., Paul, D.L., Goodenough, D.A. 1989. Antisera directed against connexin43 peptides react with a 43-kD protein localized to gap junctions in myocardium and other tissues.J. Cell Biol. 108:595–605
Beyer, E.C., Paul, D.L., Goodenough, D.A. 1987. Connexin43: A protein from rat heart homologous to a gap junction protein from liver.J. Cell Biol. 105:2621–2629
Burt, J.M., Spray, D.C. 1988a. Inotropic agents modulate gap junctional conductance between cardiac myocytes.Am. J. Physiol. 254:H1206-H1210
Burt, J.M., Spray, D.C. 1988b. Single-channel events and gating behavior of the cardiac gap junction channel.Proc. Natl. Acad. Sci. USA 85:3431–3434
Chirgwin, J.M., Przybyla, A.E., MacDonald, R.J., Rutter, W.J. 1979. Isolation of biologically active ribonucleic acid from sources enriched in ribonnuclease.Biochemistry 18:5294–5299
Ebihara, L., Beyer, E.C., Swenson, K.I., Paul, D.L., Goodenough, D.A. 1989. Cloning and expression of aXenopus embryonic gap juction protein.Science 243:1194–1195
Feinberg, A.P., Vogelstein, B. 1983. A technique for radiolabelling DNA restriction endonuclease fragments to high specific activity.Anal. Biochem. 132:6–13
FitzGerald, P.G., Goodenough, D.A. 1986. Rat lens cultures: MIP expression and domains of intercellular coupling.Invest. Ophthalmol. Vis. Sci. 27:755–771
Flagg-Newton, J.L., Dahl, G., Loewenstein, W.R. 1981. Cell junction and cyclic AMP: I. Upregulation of junctional membrane permeability and junctional membrane particles by administration of cyclic nucleotide or phosphodiesterase inhibitor.J. Membrane Biol. 63:105–121
Gimlich, R.L., Kumar, N.M., Gilula, N.B. 1988. Sequence and developmental expression of mRNA coding for a gap junction protein inXenopus.J. Cell Biol. 107:1065–1073
Goodenough, D.A., Dick, J.S.B., II, Lyons, J.E. 1980. Lens metabolic cooperation: A study of mouse lens transport and permeability visualized with freeze-substitution autoradiography and electron microscopy.J. Cell Biol. 86:576–589
Goodenough, D.A., Paul, D.L., Jesaitis, L. 1988. Topological distribution of two connexin32 antigenic sites in intact and split rodent hepatocyte gap junctions.J. Cell Biol. 107:1817–1824
Goodenough, D.A., Revel, J.P. 1971. The permeability of isolated and in situ mouse hepatic gap junctions studied with enzymatic tracers.J. Cell Biol. 50:81–91
Gruijters, W.T.M., Kistler, J., Bullivant, S., Goodenough, D.A. 1987. Immunolocalization of MP70 in lens fiber 16–17nm intercellular junctions.J. Cell Biol. 104:565–572
Helms, C., Graham, M.Y., Dutchik, J.E., Olson, M.V. 1985. A new method for purifying Lambda DNA from phage lysates.DNA 4:39–49
Kistler, J., Christie, D., Bullivant, S. 1988. Homologies between gap junction proteins in lens, heart and liver.Nature (London) 331:721–723
Kistler, J., Kirkland, B., Bullivant, S. 1985. Identification of a 70,000-D protein in lens membrane junctional domains.J. Cell Biol. 101:28–35
Kumar, N.M., Gilula, N.B. 1986. Cloning and characterization of human and rat liver cDNAs coding for a gap junction protein.J. Cell Biol. 103:767–776
Kyte, J., Doolittle, R.F. 1982. A simple method for displaying the hydropathic character of a protein.J. Mol. Biol. 157:105–132
Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.Nature (London) 227:680–685
Loewenstein, W.R. 1985. Regulation of cell-to-cell communication by phosphorylation.Biochem. Soc. Symp. London 50:43–58
McLean, I.W., Nakane, P.K. 1974. Periodate-lysine-paraformaldehyde fixative. A new fixative for immunoelectron microscopy.J. Histochem. Cytochem. 22:1077–1083
Meijer, L., Arion, D., Golsteyn, R., Pines, J., Brizuela, L., Hunt, T., Beach, D. 1989. Cyclin is a component of the sea urchin egg M-phase specific histone H1 kinase.EMBO J. 8:2275–2282
Melton, D.A., Krieg, P.A., Rebagliatti, M.R., Maniatis, T., Zinn, K., Green, M.R. 1984. Efficient in vitro synthesis of biologically active RNA and RNA hybridization probes from plasmids containing a bacteriophage SP6 promotor.Nucleic Acids Res. 12:7035–7056
Menko, A.S., Klukas, K.A., Johnson, R.G. 1984. Chicken embryo lens cultures mimic differentiation in the lens.Dev. Biol. 103:129–141
Menko, A.S., Klukas, K.A., Liu, T.-F., Quade, B., Sas, D.F., Preus, D.M., Johnson, R.G. 1987. Junctions between lens cells in differentiating cultures: Structure, formation, intercellular permeability, and junctional protein expression.Dev. Biol. 123:307–320
Miller, T.M., Goodenough, D.A. 1985. Gap junction structures after experimental alteration of junctional channel conductance.J. Cell Biol. 101:1741–1748
Miller, T.M., Goodenough, D.A. 1986. Evidence for two physiologically distinct gap junctions expressed by the chick lens epithelial cell.J. Cell Biol. 102:194–199
Moria, A.O., Draetta, G., Beach, D., Wang, J.Y.J. 1989. Reversable tyrosine phosphorylation of cdc2: Dephosporylation accompanies activation during entry into mitosis.Cell 58:193–203
Musil, L.S., Carr, C., Cohen, J.B., Merlie, J.P. 1988. Acetylcholine receptor associated 43K protein contains covalently bound myristate.J. Cell Biol. 107:1113–1121
Nicholson, B.J., Zhang, J. 1988. Multiple protein components in a single gap junction: Cloning of a second hepatic gap junction protein (Mr 21,000).In: Gap Junctions. E.L. Hertzberg and R.G. Johnson, editors. pp. 207–218. Alan R. Liss, New York
Patchinsky, T., Hunter, T., Esch, F.S., Cooper, J.A., Sefton, B.M. 1982. Analysis of the sequence of amino acids surrounding sites of tyrosine phosphorylation.Proc. Natl. Acad. Sci. USA 79:973–977
Paul, D.L. 1986. Molecular cloning of cDNA for rat liver gap junction protein.J. Cell Biol. 103:123–134
Paul, D.L., Goodenough, D.A. 1983. Preparation, characterization, and localization of antisera against bovine MP26, an integral protein from lens fiber plasma membrane.J. Cell Biol. 96:625–632
Peracchia, C. 1978. Calcium effects on gap junction structure and cell coupling.Nature London 271:669–671
Rae, J.L., Kuszak, J.R. 1983. The electrical coupling of epithelium and fibers in the frog lens.Exp. Eye Res. 36:317–326
Ralston, R., Bishop, J.M. 1985. The product of the protooncogenec-src is modified during the cellular response to plateletderived growth factor.Proc. Natl. Acad. Sci USA 82:7845–7849
Saez, J.C., Spray, D.C., Nairn, A.C., Hertzberg, E., Greengard, P., Bennett, M.V.L. 1986. cAMP increases junctional conductance and stimulates phosphorylation of the 27-kDa principal gap junction polypeptide.Proc. Natl. Acad. Sci USA 83:2473–2477
Sanger, F., Nicklen, S., Coulsen, A.R. 1977. DNA sequencing with chain terminating inhibitors.Proc. Natl. Acad. Sci. USA 79:441–445
Schuetze, S.M., Goodenough, D.A. 1982. Dye transfer between cells of the embryonic chick lens becomes less sensitive to CO2-treatment with development.J. Cell Biol. 92:694–705
Swenson, K.I., Jordan, J.R., Beyer, E.C., Paul, D.L. 1989. Formation of gap junctions by expression of connexins inXenopus oocyte pairs.Cell 57:145–155
Traub, O., Look, J., Paul, D., Willecke, K. 1987. Cyclic adenosine monophosphate stimulates biosynthesis and phosphorylation of the 26kDa gap junction protein in cultured mouse hepatocytes.Eur. J. Cell Biol. 43:48–54
Wiener, E.C., Loewenstein, W.R. 1983. Correction of cell-cell communication defect by introduction of a protein kinase into mutant cells.Nature (London) 305:433–435