Abstract
It has been 10 years since the first report of serum immunoglobulin G (IgG) against the muscle-specific tyrosine kinase (MuSK) in a subgroup of patients with myasthenia gravis (MG). From the initial clinical observations, it soon became evident that these antibodies (Abs) identify a clinical entity that differs in several aspects from MG with Abs to the acetylcholine receptor (AChR). MuSK is a 100-kDa protein, specifically expressed at the postsynaptic membrane of neuromuscular junction where it colocalizes with AChR.1 MuSK was an ideal candidate antigen in anti-AChR negative MG, as it is a transmembrane protein (thus accessible to circulating Abs) that plays a crucial role in neuromuscular junction development and maintenance. MuSK had long been known to be essential for AChR clustering; further studies have shed light on interacting proteins and molecular pathways involved in this process. At the postsynaptic membrane, MuSK is associated with the low-density lipoprotein receptor-related protein 4 (Lrp4). Binding of nerve-secreted agrin to Lrp4 activates MuSK by phosphorylation, and phosphorylated MuSK triggers a complex intracellular signaling pathway that, through Dok-7 recruitment and activation of nonreceptor tyrosine kinases and GTPases, leads to AChR assembly and stabilization.1 Another important, and relatively newly …
Published Version
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