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Rapsyn is required for MuSK signaling and recruits synaptic components to a MuSK-containing scaffold
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of outstanding interest. This paper demonstrates that MuSK remains at postsynaptic sites in rapsyn-deficient mice and that rapsyn is required to couple agrin-induced MuSK activation to AChR phosphorylation. This paper also implicates the existence of a transmembrane protein, RATL, which links the ectodomain of MuSK to cytoplasmic rapsyn.
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Apel ED, Glass DJ, Moscoso LM, Yancopoulos GD, Sanes JR. Rapsyn is required for MuSK signaling and recruits synaptic components to a MuSK-containing scaffold. of outstanding interest Neuron. 18:1997;623-635 This paper demonstrates that MuSK remains at postsynaptic sites in rapsyn-deficient mice and that rapsyn is required to couple agrin-induced MuSK activation to AChR phosphorylation. This paper also implicates the existence of a transmembrane protein, RATL, which links the ectodomain of MuSK to cytoplasmic rapsyn.
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of special interest. This paper demonstrates that complexes containing AChRs and MuSK can be isolated from muscle cells and provides evidence that MuSK is not directly responsible for the phosphorylation of the AChR β subunit.
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Fuhrer C, Sugiyama JE, R.G Taylor, Hall ZW. Association of muscle-specific kinase MuSK with the acetylcholine receptor in mammalian muscle. of special interest EMBO J. 16:1997;4951-4960 This paper demonstrates that complexes containing AChRs and MuSK can be isolated from muscle cells and provides evidence that MuSK is not directly responsible for the phosphorylation of the AChR β subunit.
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Functional interaction of Src family kinases with the acetylcholine receptor in C2 myotubes
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of special interest. This paper shows that Src and Fyn kinases co-purify with the AChR and that in vitro, Src can bind and phosphorylate the AChR β subunit, supporting a model in which Src directly phosphorylates the receptor, allowing Fyn to bind in a phosphotyrosine-dependent manner.
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of special interest. The authors show that clamping intracellular calcium levels prevents agrin-induced AChR clustering without blocking AChR phosphorylation, supporting a model in which a calcium-regulated step acts either downstream of, or parallel to, AChR phosphorylation in the clustering pathway.
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Megeath LJ, Fallon JR. Intracellular calcium regulates agrin-induced acetylcholine receptor clustering. of special interest J Neurosci. 18:1998;672-678 The authors show that clamping intracellular calcium levels prevents agrin-induced AChR clustering without blocking AChR phosphorylation, supporting a model in which a calcium-regulated step acts either downstream of, or parallel to, AChR phosphorylation in the clustering pathway.
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Laminin and α-dystroglycan mediate acetylcholine receptor aggregation via a MuSK-independent pathway
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of special interest. Together with [33], this paper provides evidence for a laminin-dependent, agrin - MuSK-independent pathway for AChR clustering. Evidence is provided for a role for α-dystroglycan in this process.
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