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Rb binding protein Che-1 interacts with Tau in cerebellar granule neurons. Modulation during neuronal apoptosis.

Barbato C., Corbi N., Canu N., Fanciulli M., Serafino A., Ciotti M., Libri V., Bruno T., Amadoro G., De Angelis R., Calissano P., Passananti C.

Che-1 is a recently identified human Rb binding protein that inhibits the Rb growth-suppressing function and regulates cell proliferation. Che-1 contacts the Rb and competes with HDAC1 for Rb-binding site, removing HDAC1 from the Rb/E2F cell cycle-regulated promoters. We have investigated the expression of Che-1 in neuronal cells and we showed that Che-1 directly interacts with Tau. Tau is a microtubule-associated protein involved in the assembly and stabilization of neuronal microtubules network that plays a crucial role modulating neuronal morphogenesis, axonal shape, and transport. In rat cerebellar granule neurons (CGNs) Che-1 partially colocalizes with Tau in the cytoplasm. Che-1 binds the amino-terminal region of Tau protein, which is not involved in microtubule interactions. Tau and Che-1 endogenous proteins coimmunoprecipitate from CGNs cellular lysates. In addition, Che-1/Tau interaction was demonstrated both in overexpressing COS-7 cells and CGNs by FRET analysis. Finally, we observed that Tau/Che-1 interaction is modulated during neuronal apoptosis.

Mol. Cell. Neurosci. 24:1038-1050(2003) [PubMed] [Europe PMC]

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