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Exp Cell Res. 2003 Nov 1;290(2):447-56.

Translocation of beta-catenin into the nucleus independent of interactions with FG-rich nucleoporins.

Author information

1
Neuroscience Program, Weill Graduate School of Medical Sciences of Cornell University, New York, NY 10021, USA.

Abstract

beta-Catenin nuclear import has been found to be independent of classical nuclear localization signal (NLS) nuclear import factors. Here, we test the hypothesis that beta-catenin interacts directly with nuclear pore proteins to mediate its own transport. We show that beta-catenin, unlike importin-beta, does not interact detectably with Phe/Gly(FG)-repeat-rich nuclear pore proteins or nucleoporins (Nups). Moreover, unlike NLS-containing proteins, beta-catenin nuclear import is not inhibited by wheat germ agglutinin (WGA) or excess importin-beta. These results suggest beta-catenin nuclear translocation does not involve direct interactions with FG-Nups. However, beta-catenin has two regions that can target it to the nucleus, and its import is cold sensitive, indicating that beta-catenin nuclear import is still an active process. Transport is blocked by a soluble form of the C-cadherin cytoplasmic domain, suggesting that masking of the nuclear targeting signal may be a mechanism of regulating beta-catenin subcellular localization.

PMID:
14568002
DOI:
10.1016/s0014-4827(03)00370-7
[Indexed for MEDLINE]

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