Proteins implicated in Alzheimer’s disease, including amyloid precursor protein and ApoE receptors, interact with each other and with a signalling molecule called agrin to influence the development of the neuromuscular junction.

The crystal structure of Norrie Disease Protein in complex with the extracellular cysteine-rich domain of Frizzled4 receptor and sucrose octasulfate reveals binding sites for Frizzled4, low density lipoprotein receptor related protein 5/6, and proteoglycan.

The cell surface receptor LRP4, long recognized for postsynaptic functions, also plays a role as a presynaptic determinant of synapse formation by functioning through a downstream kinase pathway.

Tyrosine phosphorylation of the intracellular domain of LRP1 serves as a molecular switch to regulate cellular cholesterol homeostasis through nuclear hormone receptor-mediated regulation of the cellular cholesterol exporter ABCA1.

Phosphorylation of the Wnt receptor LRP6 directly inhibits glycogen synthase kinase-3 by acting as a pseudosubstrate that stabilizes an active conformation of the enzyme, identical to autoinhibition by phosphorylation of its N terminus.

Metabolites, such as acylcarnitines, accumulate in Drosophila heads when endocytosis is blocked and reflects an increased need for sleep.

Modular tetravalent antibodies can be engineered to stimulate signaling through any combination of Frizzled and LRP receptors to drive organoid growth and mobilize endogenous stem cells in vivo.

Biophysical binding and structural prediction studies reveal that Tetraspanin12 directly binds the ligand Norrin, in a manner that is negatively cooperative with Norrin-Fzd4 binding and competitive with Norrin-LRP5/6 binding.

Enriched environment stimulates neuron generation in the hippocampus by a novel pathway involving Agrin, Lrp4, and Ror2.

A novel folding machinery assists transmembrane proteins from the cytosolic side of the endoplasmic reticulum.