Summary: (from NCBI-Entrez) ..[read more]This gene encodes a large secreted extracellular matrix protein thought to control cell-cell interactions critical for cell positioning and neuronal migration during brain development. This protein may be involved in schizophrenia, autism, bipolar disorde
Dulabon L, et al. (Neuron. 2000) found that reelin binds alpha3beta1 integrin and inhibits neuronal migration. Absence of alpha3beta1 leads to a reduction of Dab1, a signaling protein acting downstream of Reelin.
D'Arcangelo G, et al. (Neuron. 1999) found that reelin is a ligand for lipoprotein receptors. After binding to VLDLR on the cell surface, Reelin is internalized into vesicles. In dissociated neurons, apoE reduces the level of Reelin-induced tyrosine phosphorylation of Dab1.
LRP8 (apoER2) exhibits 6-fold higher affinity for Reelin than the very low density lipoprotein receptor (VLDLR), which also functions as a Reelin receptor Acidic amino acid residues in complement-type repeat domains 1 and 3 of apoER2 are required for Reelin binding. Reelin associates with two or more receptor molecules simultaneously to achieve high-affinity interaction. This finding indicates that aggregation of apoER2 by multivalent ligands such as Reelin may be the structural basis for signal transduction (Andersen et al. 2003).