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The Journal of Neuroscience, January 14, 2004, 24(2):514-521; doi:10.1523/JNEUROSCI.3408-03.2004
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Development/Plasticity/Repair
The Central Fragment of Reelin, Generated by Proteolytic Processing In Vivo, Is Critical to Its Function during Cortical Plate Development
Yves Jossin,1 Nina Ignatova,1 Thomas Hiesberger,2 Joachim Herz,2 Catherine Lambert de Rouvroit,3 andAndré M. Goffinet1 1Developmental Genetics Unit, University of Louvain Medical School, B1200 Brussels, Belgium, 2Department of Molecular Genetics, University of Texas Southwestern, Dallas, Texas 75390-9046, and 3Developmental Neurobiology Unit, Facultés Universitaires Notre-Dame de la Paix Medical School, B5000 Namur, Belgium
Reelin is a large extracellular protein that controls cortical development. It binds to lipoprotein receptors very-low-density lipoprotein receptor and apolipoprotein-E receptor type 2, thereby inducing phosphorylation of the adapter Dab1. In vivo, Reelin is cleaved into three fragments, but their respective function is unknown. Here we show the following: (1) the central fragment is necessary and sufficient for receptor binding in vitro and for Dab1 phosphorylation in neuronal cultures; (2) Reelin does not bind the protocadherin cadherin-related neuronal receptor (CNR1) as reported previously; (3) Reelin and its central fragment are equally able to rescue the reeler phenotype in a slice culture assay; and (4) anti-receptor antibodies can induce Dab1 phosphorylation but do not correct the reeler phenotype in slices. These observations show that the function of Reelin is critically dependent on the central fragment generated by processing but primarily independent of interactions with CNR1 and on the N-terminal region. They also indicate that events acting in parallel to Dab1 phosphorylation might be required for full activity.
Key words: cortical development; CNR1; Dab1; Reelin; ApoER2; VLDLR
Received July 21, 2003; revised October 14, 2003; accepted October 20, 2003.
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