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Molecular and Cellular Biology, January 2006, p. 19-27, Vol. 26, No. 1
0270-7306/06/$08.00+0     doi:10.1128/MCB.26.1.19-27.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Reconstitution of the Reelin Signaling Pathway in Fibroblasts Demonstrates that Dab1 Phosphorylation Is Independent of Receptor Localization in Lipid Rafts

Max F. Perutz Laboratories, Department of Medical Biochemistry, University Departments at the Vienna Biocenter, Medical University of Vienna, Vienna, Austria

Received 6 October 2005/ Accepted 11 October 2005

The Reelin signaling pathway operates in migrating neurons and is indispensable for their correct positioning during embryonic brain development. Many biochemical and cell biological studies to dissect the Reelin pathway at the molecular level are hampered by the lack of a cell line harboring a functional Reelin signaling pathway. Here we present fibroblast cell lines in which all required functional components of the pathway have been reconstituted. These cells react upon Reelin treatment in the same way as primary neurons. We have subsequently used these cell lines to study the subcellular localization of ApoER2 and the VLDL receptor and could demonstrate that receptor-mediated Dab1 phosphorylation does not depend on lipid rafts and that phosphorylated Dab1 remains bound to the receptor tail when the pathway is activated by Reelin.

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