Regulation of the interaction of nicotinic acetylcholine receptors with the cytoskeleton by agrin-activated protein tyrosine kinase

doi:10.1083/jcb.128.6.1121

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Regulation of the interaction of nicotinic acetylcholine receptors with the cytoskeleton by agrin-activated protein tyrosine kinase

BG Wallace
Department of Physiology, University of Colorado Health Sciences Center, Denver 80262.

Agrin induces the accumulation of nicotinic acetylcholine receptors (AChRs) in the myofiber membrane at synaptic sites in vertebrate skeletal muscle and causes an increase in tyrosine phosphorylation of the AChR beta subunit. To examine further the mechanism of agrin- induced AChR phosphorylation and the relationship between changes in protein phosphorylation and AChR aggregation, the effect of the protein tyrosine phosphatase inhibitor sodium pervanadate was tested on chick myotubes in culture. Pervanadate caused an increase in the phosphotyrosine content of a variety of proteins, including the AChR. Pervanadate also prevented agrin-induced AChR aggregation and slowed the rate at which AChRs were extracted from intact myotubes by mild detergent treatment. The rate at which phosphorylation of the AChR beta subunit and receptor detergent extractability changed following pervanadate-induced phosphatase inhibition was increased by agrin, indicating that agrin activates a protein tyrosine kinase rather than inhibiting a protein tyrosine phosphatase. The present results, taken together with previous findings on the inhibition of agrin-induced AChR aggregation by protein kinase inhibitors, demonstrate that protein tyrosine phosphorylation regulates the formation and stability of AChR aggregates, apparently by strengthening the interaction between AChRs and the cytoskelton.
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Mohamed, A. S., Swope, S. L. (1999). Phosphorylation and Cytoskeletal Anchoring of the Acetylcholine Receptor by Src Class Protein-tyrosine Kinases. ACTIVATION BY RAPSYN. J. Biol. Chem. 274: 20529-20539 [Abstract] [Full Text]
Wang, Y. G., Lipsius, S. L. (1998). Genistein elicits biphasic effects on L-type Ca2+ current in feline atrial myocytes. Am. J. Physiol. Heart Circ. Physiol. 275: H204-H212 [Abstract] [Full Text]
Dai, Z., Benjamin Peng, H. (1998). A Role of Tyrosine Phosphatase in Acetylcholine Receptor Cluster Dispersal and Formation. JCB 141: 1613-1624 [Abstract] [Full Text]
Cartaud, A., Coutant, S., Petrucci, T. C., Cartaud, J. (1998). Evidence for in Situ and in Vitro Association between beta -Dystroglycan and the Subsynaptic 43K Rapsyn Protein. CONSEQUENCE FOR ACETYLCHOLINE RECEPTOR CLUSTERING AT THE SYNAPSE. J. Biol. Chem. 273: 11321-11326 [Abstract] [Full Text]
Nawrotzki, R, Loh, N., Ruegg, M., Davies, K., Blake, D. (1998). Characterisation of alpha-dystrobrevin in muscle. J. Cell Sci. 111: 2595-2605 [Abstract]
Holmes, T. C., Berman, K., Swartz, J. E., Dagan, D., Levitan, I. B. (1997). Expression of Voltage-Gated Potassium Channels Decreases Cellular Protein Tyrosine Phosphorylation. J. Neurosci. 17: 8964-8974 [Abstract] [Full Text]
Molokanova, E., Trivedi, B., Savchenko, A., Kramer, R. H. (1997). Modulation of Rod Photoreceptor Cyclic Nucleotide-Gated Channels by Tyrosine Phosphorylation. J. Neurosci. 17: 9068-9076 [Abstract] [Full Text]
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Glass, D. J., Apel, E. D., Shah, S., Bowen, D. C., DeChiara, T. M., Stitt, T. N., Sanes, J. R., Yancopoulos, G. D. (1997). Kinase domain of the muscle-specific receptor tyrosine kinase (MuSK) is sufficient for phosphorylation but not clustering of acetylcholine receptors: Required role for the MuSK�ectodomain?. Proc. Natl. Acad. Sci. USA 94: 8848-8853 [Abstract] [Full Text]
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Glass, D.J., DeChiara, T.M., Stitt, T.N., DiStefano, P.S., Valenzuela, D.M., Yancopoulos, G.D. (1996). The Receptor Tyrosine Kinase MuSK Is Required for Neuromuscular Junction Formation and Is a Functional Receptor for Agrin. Cold Spring Harb Symp Quant Biol 61: 435-444 [Abstract]