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Guénette, S. et al.

Guénette, Chang, Hiesberger, Richardson, Eckman, Eckman, Hammer, Herz,

Essential roles for the FE65 amyloid precursor protein-interacting proteins in brain development.

Targeted deletion of two members of the FE65 family of adaptor proteins, FE65 and FE65L1, results in cortical dysplasia. Heterotopias resembling those found in cobblestone lissencephalies in which neuroepithelial cells migrate into superficial layers of the developing cortex, aberrant cortical projections and loss of infrapyramidal mossy fibers arise in FE65/FE65L1 compound null animals, but not in single gene knockouts. The disruption of pial basal membranes underlying the heterotopias and poor organization of fibrillar laminin by isolated meningeal fibroblasts from double knockouts suggests that FE65 proteins are involved in basement membrane assembly. A similar phenotype is observed in triple mutant mice lacking the APP family members APP, APLP1 and APLP2, all of which interact with FE65 proteins, suggesting that this phenotype may be caused by decreased transmission of an APP-dependent signal through the FE65 proteins. The defects observed in the double knockout may also involve the family of Ena/Vasp proteins, which participate in actin cytoskeleton remodeling and interact with the WW domains of FE65 proteins.[1]

References

Essential roles for the FE65 amyloid precursor protein-interacting proteins in brain development. Guénette, S., Chang, Y., Hiesberger, T., Richardson, J.A., Eckman, C.B., Eckman, E.A., Hammer, R.E., Herz, J. EMBO J. (2006) [Pubmed]

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