Nesprin-2 interacts with α-catenin and regulates Wnt signaling at the nuclear envelope

Sascha Neumann, Maria Schneider, Rebecca L. Daugherty, Cara J. Gottardi, Sabine A. Eming, Asa Beijer, Angelika A. Noegel, Iakowos Karakesisoglou

Research output: Contribution to journalArticle

45 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)34932-34938
Number of pages7
JournalJournal of Biological Chemistry
Volume285
Issue number45
DOIs
StatePublished - Nov 5 2010

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Neumann, S., Schneider, M., Daugherty, R. L., Gottardi, C. J., Eming, S. A., Beijer, A., Noegel, A. A., & Karakesisoglou, I. (2010). Nesprin-2 interacts with α-catenin and regulates Wnt signaling at the nuclear envelope. Journal of Biological Chemistry, 285(45), 34932-34938. https://doi.org/10.1074/jbc.M110.119651