Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 285, Issue 45, Pages 34932-34938Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M110.119651
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Funding
- Center for Molecular Medicine, University of Cologne
- Cologne Excellence Cluster on Cellular Stress Responses in Aging-associated Diseases
- Bundesministerium fur Bildung und Forschung-Deutsches Zentrum fur Luft- und Raumfahrt [MD-NET R23]
- National Institutes of Health [GMS076561]
- American Heart Association
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Nesprins and emerin are structural nuclear envelope proteins that tether nuclei to the cytoskeleton. In this work, we identified the cytoskeleton-associated alpha-N/E-catenins as novel nesprin-2-binding partners. The association involves the C termini of nesprin-2 giant and alpha-N/E-catenins. alpha-E/T/N-catenins are known primarily for their roles in cadherin-mediated cell-cell adhesion. Here, we show that, in addition, alpha-catenin forms complexes with nesprin-2 that include beta-catenin and emerin. We demonstrate that the depletion of nesprin-2 reduces both the amount of active beta-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.
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