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Reelin is an extracellular matrix serine protease that facilitates the layering of neurons in the cerebral cortex and cerebellum. It is synthesized by the Cajal-Retzius cells and other pioneer neurons located in the telencephalic marginal zone and by granule cells of the external granular layer of the cerebellum. It regulates microtubule function in neurons as well as neuronal migration for example that of sympathetic preganglionic neurons in the spinal cord. It modulates cell adhesion. Binding to the extracellular domains of lipoprotein receptors VLDLR and LRP8 induces tyrosine phosphorylation of disabled homolog 1 and modulation of TAU phosphorylation. Its 3460 amino acid pro-petide is coded by the RELN gene at 7q22.1 which if dysfunctional results in lissencephaly 2 (LIS2, Norman-Roberts lissencephaly) manifest by:

RELN expression is reduced in schizophrenia and may be associated negatively with some lymphoedema and poor haemostatis. It protects against neuronal death and may have a role in neurodegenerative diseases such as Alzheimer's disease.

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