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Structural mechanisms of the agrin-LRP4-MuSK signaling pathway in neuromuscular junction differentiation

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Published:1st Sep 2013

Author: Zong Y, Jin R.

Source: Cellular and Molecular Life Sciences

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Ref.:Cell Mol Life Sci. 2013 Sep;70(17):3077-88.

DOI:10.1007/s00018-012-1209-9

Structural mechanisms of the agrin-LRP4-MuSK signaling pathway in neuromuscular junction differentiation

The neuromuscular junction (NMJ) is the most extensively studied model of neuronal synaptogenesis. Acetylcholine receptor (AChR) clustering on the postsynaptic membrane is a cardinal event in the differentiation of NMJs. AChR clustering and postsynaptic differentiation is orchestrated by sophisticated interactions among three proteins: the neuron-secreted proteoglycan agrin, the co-receptor LRP4, and the muscle-specific receptor tyrosine kinase MuSK. LRP4 and MuSK act as scaffolds for multiple binding partners, resulting in a complex and dynamic network of interacting proteins that is required for AChR clustering. In this review, we discuss the structural basis for NMJ postsynaptic differentiation mediated by the agrin-LRP4-MuSK signaling pathway.

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