Nesprin-2 interacts with {alpha}-catenin and regulates Wnt signaling at the nuclear envelope

B7 EMING Neumann S, Schneider M, Daugherty RL, Gottardi CJ, Eming SA, Beijer A, Noegel AA, Karakesisoglou I, J Biol Chem. 2010 Nov 5;285(45):34932-8.

Abstract:

Nesprins and emerin are structural nuclear envelope proteins that tether nuclei to the cytoskeleton. In this work, we identified the cytoskeleton-associated α-N/E-catenins as novel nesprin-2-binding partners. The association involves the C termini of nesprin-2 giant and α-N/E-catenins. α-E/T/N-catenins are known primarily for their roles in cadherin-mediated cell-cell adhesion. Here, we show that, in addition, α-catenin forms complexes with nesprin-2 that include β-catenin and emerin. We demonstrate that the depletion of nesprin-2 reduces both the amount of active β-catenin inside the nucleus and T-cell factor/lymphoid-enhancing factor-dependent transcription. Taken together, these findings suggest novel nesprin-2 functions in cellular signaling. Moreover, we propose that, in contrast to emerin, nesprin-2 is a positive regulator of the Wnt signaling pathway.

PubMed

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