Reelin is a ligand for lipoprotein receptors

Gabriella D'Arcangelo, Ramin Homayouni, Lakhu Keshvara, Dennis S. Rice, Michael Sheldon, Tom Curran

Research output: Contribution to journalArticlepeer-review

631 Scopus citations

Abstract

A signaling pathway involving the extracellular protein Reelin and the intracellular adaptor protein Disabled-1 (Dab1) controls cell positioning during mammalian brain development. Here, we demonstrate that Reelin binds directly to lipoprotein receptors, preferably the very low-density lipoprotein receptor (VLDLR) and apolipoprotein E receptor 2 (ApoER2). Binding requires calcium, and it is inhibited in the presence of apoE. Furthermore, the CR-50 monoclonal antibody, which inhibits Reelin function, blocks the association of Reelin with VLDLR. 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. These data suggest that Reelin directs neuronal migration by binding to VLDLR and ApoER2.

Original languageEnglish (US)
Pages (from-to)471-479
Number of pages9
JournalNeuron
Volume24
Issue number2
DOIs
StatePublished - Oct 1999

All Science Journal Classification (ASJC) codes

  • Neuroscience(all)

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