Muscle, Skeletal Receptor Tyrosine-Protein Kinase (MUSK) Mouse Recombinant Protein

This gene encodes a member of the protein tyrosine kinase family. The encoded protein is a type 1 receptor-like protein located in muscle membrane that is activated by the heparan sulfate proteoglycan agrin released by nerve cells. The encoded protein activates signaling cascades responsible for multiple aspects of motor neuron and muscle development, including organization of the postsynaptic membrane, synaptic gene transcription, patterning of skeletal muscle, anchoring of acetylcholinesterase, and guidance of motor axons. Alternatively spliced transcript variants encoding different isoforms have been described. [provided by RefSeq, Jul 2008]

MUSK: a receptor tyrosine kinase that is essential for the establishment and maintenance of the neuromuscular junction (NMJ). Its activation by agrin, a neuronally derived heparan-sulfate proteoglycan, and the agrin receptor (LRP4), leads to clustering of acetylcholine receptors on the postsynaptic side of the NMJ. Its activation by agrin requires Dok7, which interacts with the cytoplasmic portion of MuSK and activates its tyrosine kinase activity.

Protein type: Protein kinase, tyrosine (receptor); Kinase, protein; Membrane protein, integral; EC 2.7.10.1; Protein kinase, TK; TK group; Musk family

Cellular Component: postsynaptic membrane; cell projection; membrane; integral to plasma membrane; integral to membrane; plasma membrane; synapse; cell junction; neuromuscular junction; receptor complex; external side of plasma membrane

Molecular Function: transferase activity; protein binding; protein-tyrosine kinase activity; transferase activity, transferring phosphorus-containing groups; nucleotide binding; kinase activity; transmembrane receptor protein tyrosine kinase activity; protein kinase binding; ATP binding; protein kinase activity; PDZ domain binding

Biological Process: positive regulation of synaptic transmission, cholinergic; peptidyl-tyrosine phosphorylation; protein amino acid autophosphorylation; multicellular organismal development; positive regulation of synaptic growth at neuromuscular junction; signal transduction; receptor clustering; protein amino acid phosphorylation; memory; positive regulation of peptidyl-tyrosine phosphorylation; regulation of transcription, DNA-dependent; positive regulation of neuron apoptosis; regulation of synaptic growth at neuromuscular junction; positive regulation of protein amino acid phosphorylation; cell differentiation; response to electrical stimulus; phosphorylation; neuromuscular junction development