Lrp4 is a Receptor for Agrin and Forms a Complex with MuSK
By Natalie Kim, A. L. Stiegler, T. Cameron, Peter T. Hallock, A. Gomez, Julie H. Huang, S. Hubbard, Michael Loran Dustin, S. Burden. Cell, 2008
665 citations recorded by the source corpus.
SUMMARY Neuromuscular synapse formation requires a complex exchange of signals between motor neurons and skeletal muscle fibers, leading to the accumulation of postsynaptic proteins, including acetylcholine receptors in the muscle membrane and specialized release sites, or active zones in the presynaptic nerve terminal. MuSK, a receptor tyrosine kinase that is expressed in skeletal muscle, and Agrin, a motor neuron-derived ligand that stimulates MuSK phosphorylation, play critical roles in synaptic differentiation, as synapses do not form in their absence, and mutations in MuSK or downstream effectors are a major cause of a group of neuromuscular disorders, termed congenital myasthenic syndromes (CMS). How Agrin activates MuSK and stimulates synaptic differentiation is not known and remains a fundamental gap in our understanding of signaling at neuromuscular synapses. Here, we report that Lrp4, a member of the LDLR family, is a receptor for Agrin, forms a complex with MuSK and mediates MuSK activation by Agrin.
Subfields: Cell Biology, Molecular Biology, Neurology
View Paper: https://www.semanticscholar.org/paper/061c1f54a2f4191210db0beb8bf6fc97546909e6
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Cell Biology
In Molecular Biology
In Neurology
Citations in the corpus
- Apolipoprotein E and its receptors in Alzheimer's disease: pathways, pathogenesis and therapy (2009, background): “and in neuromuscular synapse formation by serving as a receptor for agri”