Mediates SOST-dependent inhibition of bone formation (By similarity). Functions as a specific facilitator of SOST-mediated inhibition of Wnt signaling (By similarity). Plays a key role in the formation and the maintenance of the neuromuscular junction (NMJ), the synapse between motor neuron and skeletal muscle. Directly binds AGRIN and recruits it to the MUSK signaling complex. Mediates the AGRIN-induced phosphorylation of MUSK, the kinase of the complex. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Alternatively, may be involved in the negative regulation of the canonical Wnt signaling pathway, being able to antagonize the LRP6-mediated activation of this pathway. More generally, has been proposed to function as a cell surface endocytic receptor binding and internalizing extracellular ligands for degradation by lysosomes. Plays an essential role in the process of digit differentiation. Homooligomer. Interacts with MUSK; the heterodimer forms an AGRIN receptor complex that binds AGRIN resulting in activation of MUSK (PubMed:18848351). Interacts (via the extracellular domain) with SOST; the interaction facilitates the inhibition of Wnt signaling (By similarity). Interacts with MESD; the interaction promotes glycosylation of LRP4 and its cell-surface expression (By similarity). Expressed in different regions of the brain, mainly in the olfactory bulb, at lower level in the cerebral cortex and hippocampus. N-glycosylation is required for cell surface location. Belongs to the LDLR family.