Summary
δ -Catenin was first cloned in a yeast two-hybrid system as an interactor with the loop region of presenilin 1. δ-Catenin is a mammalian brain protein in the Armadillo (Arm) repeat superfamily with sequence similarity to the adherens junction protein p120ctn. δ-Catenin can be immunoprecipitated as a complex with other components of the adherens junction, including cadherin and β-catenin, from transfected cells and brain. The ectopic expression of δ-catenin in MDCK cells altered their morphology, induced the elaboration of lamellipodia, interfered with monolayer formation, and increased scattering in response to hepatocyte growth factor treatment. Interestingly, δ-catenin can also be immunoprecipitated in a complex with certain synaptic proteins. Together these findings suggest that δ-catenin may serve as a linker that joins the synapse and the adherens junction. The interaction with cadherin involves direct contact between the highly conserved juxtamembrane region of the cadherin carboxy terminus and the Arm-repeat of δ-catenin. The interaction with synaptic elements may involve the PDZ binding domain. In developing mouse brain, staining with δ-catenin antibodies is prominent towards the apical boundary of the neuroepithelial cells in the ventricular zone. In mature brain, δ-catenin is localized to the dendrites. Staining is particularly prominent in the apical dendrites of pyramidal cells. Armadillo/β catenin is also present in the presenilin 1 immunocomplex; however, this interaction is not direct. The interaction between Armadillo/β-catenin and presenilin 1 requires a third protein, which may be δ-catenin. Presenilin may mediate the delivery of a multi-protein complex to the region of the adherens and synaptic junctions.
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Kosik, K.S., Medina, M., Ochiishi, T., Martinez, M.C., Lu, Q. (2002). δ-Catenin, Presenilin, and the Synaptic-Adherens Junction Complex. In: Christen, Y., Israël, A., De Strooper, B., Checler, F. (eds) Notch from Neurodevelopment to Neurodegeneration: Keeping the Fate. Research and Perspectives in Alzheimer’s Disease. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-55996-9_11
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DOI: https://doi.org/10.1007/978-3-642-55996-9_11
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