Bettendorff, Lucien ; Université de Liège - ULiège > Département des sciences biomédicales et précliniques > Biochimie et physiologie humaine et pathologique
Changeux, Jean-Pierre
Language :
English
Title :
Specific phosphorylation of Torpedo 43 rapsyn by endogenous kinase(s) with thiamine triphosphate as the phosphate donor
Publication date :
2000
Journal title :
FASEB Journal
ISSN :
0892-6638
eISSN :
1530-6860
Publisher :
Federation of American Society for Experimental Biology, Bethesda, United States - Maryland
Nghiêm, H. O., and Changeux, J. P. (1993) The 43 KDa protein (43 K). In Guidebook To The Cytoskeletal, Extracellular Matrix and Adhesion Proteins (Vale, R., and Kreis, T., eds) pp. 95-97, Sambrook & Tooze, Oxford
Nghiêm, H. O. (1999) The 43 K protein or 43K-rapsyn protein. In Guidebook to the Extracellular Matrix, Anchor and Adhesion Proteins, 2nd edition (Kreis, T., and Vale, R., eds) pp. 67-71, Sambrook & Tooze, Oxford University Press
Sobel, A., Weber, M., and Changeux, J. P. (1977) Large scale purification of the acetylcholine receptor protein in its membrane-bound and detergent extracted forms from Torpedo marmorata electric organ. Eur. J. Biochem. 80, 215-224
Neubig, R. R., Krodel, E. K., Boyd, N. D., and Cohen, J. B. (1979) Acetylcholine and local anesthetic binding to Torpedo nicotinic postsynaptic membranes after removal of nonreceptor peptides. Proc. Natl. Acad. Sci. USA 76, 690-694
Nghiêm, H .O., Cartaud, J., Dubreuil, C., Kordeli, C., Buttin, G., and Changeux, J. P. (1983) Production and characterization of a monoclonal antibody directed against the 43,000 M.W. ν1 polypeptide from Torpedo marmorata electric organ. Proc. Natl. Acad, Sci. USA 80, 6403-6407
Sealork, R., Wray, B. E., and Froehner, S. C. (1984) Ultrastructural localization of the Mr 43,000 protein and the acetylcholine receptor in Torpedo postsynaptic membranes using monoclonal antibodies. J. Cell Biol. 98, 2239-2244
Froehner, S. C., Gulbrandsen, V., Hyman, C., Jeng, A. Y., Neubig, R. R., and Cohen, J. B. (1981) Immunofluorescence localization at the mammalian neuromuscular junction of the Mr 43,000 protein of Torpedo postsynaptic Membranes. Proc. Natl. Acad. Sci. USA 78, 5230-5234
Gautam, M., Noakes, P. G., Mudd J., Nichol, M., Chu, G. C., Sanes, J. R., and Merlie, J. P. (1995) Failure of postsynaptic specialization to develop at neuromuscular junctions of rapsyndeficient mice. Nature (London) 377, 232-236
Krikorian, J. G., and Bloch, R. J. (1992) Treatments that extract the 43K protein from acetylcholine receptor clusters modify the conformation of cytoplasmic domains of all subunits of the receptor. J. Biol. Chem. 267, 9118-9128
Huganir, R. L., and Greengard, P. (1990) Regulation of neurotransmitter receptor desensitization by protein phosphorylation. Neuron 5, 555-567
Walsh, D. A., Newsholme, P., Cawley, K. C., Van, P. S., and Angelos, K. L. (1991) Motifs of protein phosphorylation and mechanisms of reversible covalent regulation. Physiol. Rev. 71, 285-304
Cohen, P., Campbell, D. G., Dent, P., Gomez, N., Lavoinne, A., Nakielny, S., Stokoe, D., Sutherland, C., and Traverse, S. (1992) Dissection of the protein kinase cascades involved in insulin and nerve growth factor action. Biochem. Soc. Trans. 20, 671-674
Roche, K. W., Tingley, W. G., and Huganir, R. L. (1994) Glutamate receptor phosphorylation and synaptic plasticity. Curr. Opin. Neurol. 4, 383-388
Karin, M., and Hunter, T. (1995) Transcriptional control by protein phosphorylation: signal transmission from the cell surface to the nucleus. Curr. Biol. 5/7, 747-757
Carr, C., McCourt, D., and Cohen, J. (1987) The 43-kilodalton protein of Torpedo nicotinic postsynaptic membranes: purification and determination of primary structure. Biochemistry 26, 7090-7102
Hill, J. A., Nghiêm, H. O., and Changeux, J. P. (1991) Serine-specific phosphorylation of nicotinic receptor-associated 43K protein. Biochemistry 30, 5579-5585
Glass, D. J., and Yancopoulos, G. D. (1997) Sequential roles of agrin, MuSK and rapsyn during neuromuscular junction formation. Curr. Opin. Neurobiol. 7, 379-384
Cooper, J. R., and Pincus, J. H. (1979) The role of thiamine in the nervous tissue. Neurochem. Res. 4, 223-239
Yamashita, H., Zhang, Y. X., and Nakamura, S. (1993) The effects of thiamin and its phosphate esters on dopamine release in the rat striatum. Neurosci. Lett. 158, 229-231
Bettendorff, L. (1994) Thiamine in excitable tissues: reflections on a non-cofactor role. Metab. Brain Dis. 9, 183-210
Bettendorff, L., Peeters, M., Wins, P., and Schoffeniels, E. (1993) Metabolism of thiamine triphosphate in rat brain: correlation with chloride permeability. J. Neurochem. 60, 423-434
Kawasaki, T. (1992) Vitamin B1: Thiamine. In Modern Chromatographic Analysis of Vitamins (De Leenhert, A. P., Lambert, W. E., and Nelis, H. J., eds) pp. 319-354, Marcel Dekker, New York
Bettendorff, L., Peeters, M., Jouan, C., Wins, P., and Schoffeniels, E. (1991) Determination of thiamin and its phosphate esters in cultured neurons and astrocytes using an ion-pair reversed phase high performance liquid chromatographic method. Anal. Biochem. 198, 52-59
Eder, L., and Dunant, Y. (1980) Thiamine and cholinergic transmission in the electric organ of Torpedo. I. Cellular localization and functional changes of thiamine and thiamine phosphate esters. J. Neurochem. 35, 1278-1286
Egi, Y., Koyama, S., Shikata, H., Yamada, K., and Kawasaki, T. (1986) Content of thiamine phosphate esters in mammalian tissues - an extremely high concentration of thiamine triphosphate in pig skelelal muscle. Biochem. Int. 12, 385-390
Bettendorff, L., Michel-Cahay, C., Grandfils, C., De Rycker, C., and Schoffeniels, E. (1987) Thiamine triphosphate and membrane-associated thiamine phosphatases in the electric organ of Electrophorus electricus. J. Neurochem. 49, 495-502
Grandfils, C., Bettendorff, L., de Rycker, C., and Schoffeniels, E. (1988) Synthesis of (gamma-32P) thiamine triphosphate. Anal. Biochem. 169, 274-278
Miles, E. W. (1977) Modifications of histidyl residues in proteins by diethylpyrocarbonate. In Methods Enzymology (Hirs, C. H. W., and Timasheff, S. N., eds) Vol. 47, part E, pp. 431-442, Academic Press, N.Y.
Cortay, J. C., Rieul, B., Duclos, B., and Cozzone, A. J. (1986) Characterization of the phosphoproteins of Escherichia coli cells by electrophoretic analysis. Eur. J. Biochem. 159, 227-237
Turner, A. M., and Mann, N. H. (1986) Protein phosphorylation in Rhodomicrobium vannielii. J. Gen. Microbiol. 132, 3433-3440
Kamps, M. P., and Sefton, B. M. (1989) Acid and base hydrolysis of phosphoproteins bound to immobilon facilitates analysis of phosphoamino acids in gel-fractionated proteins. Anal. Biochem. 176, 22-27
Cooper, J. A., Sefton, B. H., and Hunter, T. (1983) Detection and quantification of phosphotyrosine in proteins. In Methods in Enzymology (Corbin, J. D., and Hardman, J. G., eds) Vol. 99, part F, pp. 387-402, Academic Press, New York
Smith, R. A., Halpern, R. M., Bruegger, B. B., Dunlap, A. K., and Fricke, O. (1978) Chromosomal protein phosphorylation on basic amino acids. In Methods Cell Biol. (Stein, G., Stein, J., and Kleinsmith, L. J., eds) Vol. 19, pp. 153-159, Academic Press, N.Y.
Wei, Y. F., and Matthews, H. R. (1991) Identification of phosphohistidine in proteins and purification of proteinhistidine kinases. In Methods in Enzymology (Hunter, T., and Sefton, B. M., eds) Vol. 200, part A, pp. 388-414, Academic Press, San Diego
Towbin, H., Staehelin, T., and Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354
Nghiêm, H. O. (1988) Miniaturization of the immunoblot technique, rapid screening for the detection of monoclonal and polyclonal antibodies. J. Immunol. Methods 111, 137-141
Nghiêm, H. O., J. Hill, and Changeux, J. P. (1991) Developmental changes in the subcellular distribution of the 43K (ν1) polypeptide in Turpedo marmorata electrocyte: support for a role in acetylcholine receptor stabilization. Devolopment 113, 1059-1067
Krebs, E. J., and Beavo, J. A. (1979) Phosphorylation-dephosphorylation of enzymes. In Annu. Rev. Biochem. (Snell, E. E., Boyer, P. D., Meister, A., and Richardson, C. C., eds) Vol. 48, pp. 923-959, Annu. Rev. Inc., Palo Alto
Hunter, T., and Cooper, J. A. (1985) Protein-tyrosine kinases. In Annual Review of Biochemistry (Richardson, C. C., Boyer, P .D., Dawid, I. B., and Meister, A., eds) Vol. 54, pp. 897-930, Annu. Rev. Inc., Palo Alto
Bairoch, A., Bucher, P., and Hofmann, K. (1997) The prosite database, its status in 1997. Nucleic Acids Res. 25, 217-221
Kreegipuu, A., Blom, N., and Brunak, S. (1999) PhosphoBase. a database of phosphorylation sites: release 2.0. Nucleic Acids Res. 27, 237-239
Scotland, P. B., Colledge, M., Melnikova, I., Zhengshan, D., and Froehner, S. C. (1993) Clustering of the acetylcholine receptor by the 43-kD protein: involvement of the zinc finger domain. J. Cell Biol. 123, 719-728
Swope, S. L., and Huganir, R. I., (1993) Molecular cloning of two abundant protein tyrosine kinases in Torpedo electric organ that associate with the acetylcholine receptor. J. Biol. Chem. 268, 25152-25161
Qu, Z., Apel, E. D., Doherty, C. A., Hoffman, P. W., Merlie, J. P., and Huganir, R. L. (1996) The synapse-associated protein rapsyn regulates tyrosine phosphorylation of proteins colocalized at nicotinic acetylcholine receptor clusters. Mol. Cell. Neurosci. 8, 171-184
Duclos, B., Marcandier, S., and Cozzone, A. J. (1991) Chemical properties and separation of phosphoamino acids by thin-layer Chromatography and/or electrophoresis. In Methods in Enzymology (Hunter, T., and Sefton, B. M., eds) Vol. 201, part B, pp. 10-21, Academic Press, San Diego
Mesnildrey, S., Agou, F., Karlsson, A., Deville Bonne, D., and Veron, M. (1998) Coupling between catalysis and oligomeric structure in nucleoside diphosphate kinase. J. Biol. Chem. 273, 4436-4442
Parks, R. E. J., and Agarwal, R. P. (1973) Nucleoside diphosphokinases. In The Enzymes (Boyer, E. D., ed) Vol. 8, part A, pp. 307-334, Academic Press, New York
Huang, E. P. (1997) Metal ions and synaptic transmission: think zinc. Proc. Natl. Acad. Sci. USA 94, 13386-13387
Bezakova, G., and Bloch, R. J. (1998) The zinc finger domain of the 43 kDa receptor-associated protein, rapsyn. Role in nAChR clustering. Mol. Cell, Neurosci. 11, 274-288
Wang, Z. Z., Mathias, A., Gautam, M., and Hall, Z. W. (1999) Metabolic stabilization of muscle nicotinic acetylcholine receptor by rapsyn. J. Neurosci. 19, 1998-2007
Burns, A. L., Benson, D., Howard, M. J., and Marjiotta, J. F. (1997) Chick ciliary ganglion neurons contain transcripts coding for acetylcholine receptor-associated protein at synapses (rapsyn). J. Neurosci. 17, 5016-5026
Buckel, A., Beeson, D., James, M., and Vincent, A. (1996) Cloning of cDNA encoding human rapsyn and mapping of the rapsyn gene locus to chromosome 11p11.2-p11.1 Genomics 35, 613-616
Frail, D. E., McLanghlin, L. L., Mudd, J., and Merlie, J. P. (1988) Identification of the mouse muscle 43,000-dalton acetylcholiue receptor-associated protein (RAPsyn) by cDNA cloning. J. biol. Chem. 263, 15602-15607
Frail, D. E., Mudd, J., Shah. V., Carr, C., Cohen, J. B., and Merlie, J. P. (1987) cDNAS for the postsynaptic 43-kDa protein of Torpedo electric organ encode two proteins with different carboxyl termini. Proc. Natl. Acad. Sci. USA 84, 6302-0306
Baldwin, T. J., Theriot, J. A., Yoshihara, C. M., and Burden, S. J. (1988) Regulation of transcript encoding the 43K subsynaptic protein during development and after denervation. Development 104, 557-564
Ramarao, M. K., and Cohen, J. (1998) Mechanism of nicotinic nAChR cluster formation by rapsyn. Proc. Natl. Acad. Sci. USA 95, 4007-4012
Kato, J., Yamamoto, T., Yamada, K., and Ohtake, H. (1993) Cloning, sequence and characterization of the polyphosphate kinase-encoding gene (ppk) of Klebsellia aeroegenes. Gene 137, 237-242
Tinsley, C. R., and Gotschlich, E. C. (1995) Cloning and characterization of the meningococcal polyphosphate kinase gene: production of polyphosphate synthesis mutants. Infect. Immun. 63, 1624-1630
Kumble, K. D., Ahn, K., and Kornberg, A. (1996) Phosphohistidyl active sites in polyphosphate kinase of E. coli. Proc. Natl. Acad. Sci. USA 93, 14391-14395
Stock, J. B., Stock, A. M., and Mottonen, J. M. (1990) Signal transduction in bacteria. Nature (London) 344, 395-400
Alex, L. A., and Simon, M. I. (1994) Protein histidine kinases and signal transduction in prokaryoles and eukaryotes. Trends Genet. 10, 133-138
Huganir, R. L., and Greengard, P. (1983) cAMP-dependent protein kinase phosphorylates the nicotinic acetylcholine receptor. Proc. Natl. Acad. Sci. USA 80, 1130-1134
Huganir R. L., Miles, K., and Greengard, P. (1984) Phosphorylation of the nicotinic acetylcholine receptor by an endogenous tyrosine-specific protein kinase. Proc. Natl. Acad. Sci. USA 81, 6968-6972
Safran, A., Sagi-Eisenberg, R., Neumann, D., and Fuchs, S. (1987) Phosphorylation of the acetylcholine receptor by protein kinase C and identification of the phopshorylation site within the δ subunit. J. Biol. Chem. 262, 10506-10510
Hopfield, J. F., Tank, D. W., Greengard, P., and Huganir, R. L. (1988) Functional modulation of acetylcholine receptor by tyrosine phosphorylation. Nature (London) 336, 677-680
Qu, Z., Moritz, E., and Huganir, R. L. (1990) Regulation of tyrosine phosphorylation of the nicotinic acetylcholine receptor at the rat neuromuscular junction. Neuron 2, 367-378
Wallace, B. G., Qu, Z., and Huganir, R. L. (1991) Agrin induces phosphorylation of the nicotinic acetylcholine receptor. Neuron 6, 869-878
Rüegg, U. T., and Burgess, G. M. (1989) Staurosporine. K-252 and UCN-01, potent but non specific inhibitors of protein kinases. Trends Pharmacol. Sci. 10, 218-220
Wallace, B. G. (1994) Staurosporine inhibits agrin-induced acetylcholine receptor phosphorylation and aggregation. J. Cell Biol. 125, 661-668
McMahan U. J. (1990) The agrin hypothesis. In Brain, Vol. 55, pp. 407-418. Cold Spring Harbor Syrup. Quant. Biol., Cold Spring Harbor, New York
Ferns, M. J., and Hall, Z. W. (1992) How many agrins does it take to make a synapse? Cell 70, 1-3
Gautam, M., Noakes, P. G., Moscoso, L., Rupp, F., Scheller, R. H., Merlie, J. P., and Sanes, J. R. (1996) Defective neuromuscular synaptogenesis in agrin-deficient mutant mice. Cell 85, 525-535
Apel, E. D., Roberds, S. L., Campbell, K. P., and Merlie, J. P. (1995) Rapsyn may function as a link between the acetylcholine receptor and the agrin-binding dystrophin-associated glycoprotein complex. Neuron 15, 115-126
Gillespie, S. K. H., Balasubramanian, S., Fung, E. T., and Huganir, R. L. (1996) Rapsyn clusters and activates the synapse-specific receptor tyrosine kinase MuSK. Neuron 16, 953-962
Glass, D. J., Bowen, D. C., Stitt, T. N., Radziejewski, C., Bruno, J., Ryan, T. E., Gies, D. R., Shah, S., Mattsson, K., Burden, S. J., DiStefano, P. S., Valenzuela, D. M., DeChiara, T. M., and Yancopoulos, G. D. (1996) Agrin acts via a MuSK receptor complex. Cell 85, 513-50
Bettendorff, L., Schoffeniels, E., Naquet, R., Silva, B. C., Riche, D., and Menini, C. (1989) Phosphorylated thiamine derivatives and cortical activity in the baboon Papio papio: effect of intermittent light stimulation. J. Neurochem. 53, 80-87
Nauti, A., Patrini, C., Reggiani, C., Merighi, A., Bellazzi, R., and Rindi, G. (1997) In vivo study of the kinetics of thiamine and its phosphoesters in the deafferented rat cerebellum. Metab. Brain Dis. 12, 145-160
Yang, S. H., Armson, P. F., Cha, J., and Phillips, W. D. (1997) Clustering of GABAA receptors by rapsyn/43kD protein in vivo. Mol. Cell Neurosci. 8, 430-438
Matthews, H. R. (1995) Protein kinases and phosphatases that act on histidine, lysine, or arginine residues in eukaryotic proteins: a possible regulator of the mitogen-activated protein kinase cascade. Pharmacol. Ther. 67, 323-350