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XB-ART-1033
J Cell Biol 2005 Dec 05;1715:785-97. doi: 10.1083/jcb.200502141.
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RanBP3 enhances nuclear export of active (beta)-catenin independently of CRM1.

Hendriksen J , Fagotto F , van der Velde H , van Schie M , Noordermeer J , Fornerod M .


Abstract
beta-Catenin is the nuclear effector of the Wnt signaling cascade. The mechanism by which nuclear activity of beta-catenin is regulated is not well defined. Therefore, we used the nuclear marker RanGTP to screen for novel nuclear beta-catenin binding proteins. We identified a cofactor of chromosome region maintenance 1 (CRM1)-mediated nuclear export, Ran binding protein 3 (RanBP3), as a novel beta-catenin-interacting protein that binds directly to beta-catenin in a RanGTP-stimulated manner. RanBP3 inhibits beta-catenin-mediated transcriptional activation in both Wnt1- and beta-catenin-stimulated human cells. In Xenopus laevis embryos, RanBP3 interferes with beta-catenin-induced dorsoventral axis formation. Furthermore, RanBP3 depletion stimulates the Wnt pathway in both human cells and Drosophila melanogaster embryos. In human cells, this is accompanied by an increase of dephosphorylated beta-catenin in the nucleus. Conversely, overexpression of RanBP3 leads to a shift of active beta-catenin toward the cytoplasm. Modulation of beta-catenin activity and localization by RanBP3 is independent of adenomatous polyposis coli protein and CRM1. We conclude that RanBP3 is a direct export enhancer for beta-catenin, independent of its role as a CRM1-associated nuclear export cofactor.

PubMed ID: 16314428
PMC ID: PMC2171279
Article link: J Cell Biol


Species referenced: Xenopus laevis
Genes referenced: acvr1 cip2a cnga1 ctnnb1 il1r1 myc nkd1 odc1 prl.2 ran ranbp3 rps6ka3 sia1 tcf4 wnt1 xpo1


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References [+] :
Andrews, A rapid micropreparation technique for extraction of DNA-binding proteins from limiting numbers of mammalian cells. 1991, Pubmed