Regulation of tyrosine phosphorylation of the nicotinic acetylcholine receptor at the rat neuromuscular lunction

作者: Zhican Qu , Elizabeth Moritz , Richard L. Huganir

DOI: 10.1016/0896-6273(90)90049-L

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摘要: Abstract The nicotinic acetylcholine receptor (AChR) from the electric organ of T. californica is highly phosphorylated on tyrosine residues in vivo. In contrast, phosphorylation AM rat myotube cultures barely detectable. To determine whether this low level AChR muscle cell due to a lack neuronal innervation, we examined diaphragm Immunofluorescent double labeling cryostat sections using antibodies specific for phosphotyrosine or showed direct colocalization with at neuromuscular junction. Using anti-phosphotyrosine antibodies, immunoblots partially purified demonstrated that contains high levels phosphotyrosine. Denervation induced time-dependent decrease AChR, as measured by immunocytochemical and immunoblot techniques. Tyrosine occurred late development junction, between postnatal days 7 14. These studies suggest innervation regulates may play an important role developmental regulation AChR.

参考文章(45)
R L Huganir, E Racker, Properties of proteoliposomes reconstituted with acetylcholine receptor from Torpedo californica. Journal of Biological Chemistry. ,vol. 257, pp. 9372- 9378 ,(1982) , 10.1016/S0021-9258(18)34079-1
ZW Hall, PD Gorin, L Silberstein, C Bennett, A postnatal change in the immunological properties of the acetylcholine receptor at rat muscle endplates The Journal of Neuroscience. ,vol. 5, pp. 730- 734 ,(1985) , 10.1523/JNEUROSCI.05-03-00730.1985
Y Gu, Z W Hall, Characterization of acetylcholine receptor subunits in developing and in denervated mammalian muscle. Journal of Biological Chemistry. ,vol. 263, pp. 12878- 12885 ,(1988) , 10.1016/S0021-9258(18)37643-9
GH Yee, RL Huganir, Determination of the sites of cAMP-dependent phosphorylation on the nicotinic acetylcholine receptor. Journal of Biological Chemistry. ,vol. 262, pp. 16748- 16753 ,(1987) , 10.1016/S0021-9258(18)49318-0
A Safran, R Sagi-Eisenberg, D Neumann, S Fuchs, Phosphorylation of the acetylcholine receptor by protein kinase C and identification of the phosphorylation site within the receptor delta subunit. Journal of Biological Chemistry. ,vol. 262, pp. 10506- 10510 ,(1987) , 10.1016/S0021-9258(18)60990-1
M M Smith, J P Merlie, J C Lawrence, Ca2+-dependent and cAMP-dependent control of nicotinic acetylcholine receptor phosphorylation in muscle cells. Journal of Biological Chemistry. ,vol. 264, pp. 12813- 12819 ,(1989) , 10.1016/S0021-9258(18)51559-3
P C Cotton, J S Brugge, Neural tissues express high levels of the cellular src gene product pp60c-src. Molecular and Cellular Biology. ,vol. 3, pp. 1157- 1162 ,(1983) , 10.1128/MCB.3.6.1157
M Sudol, H Hanafusa, Cellular proteins homologous to the viral yes gene product. Molecular and Cellular Biology. ,vol. 6, pp. 2839- 2846 ,(1986) , 10.1128/MCB.6.8.2839
P. F. Maness, M. Aubry, C. G. Shores, L. Frame, K. H. Pfenninger, c-src gene product in developing rat brain is enriched in nerve growth cone membranes Proceedings of the National Academy of Sciences of the United States of America. ,vol. 85, pp. 5001- 5005 ,(1988) , 10.1073/PNAS.85.14.5001