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¹ Laboratory of Intracellular Signaling, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan
² Graduate School of Medicine, Kobe University, 7-5-1, Kusunokicho, Chuo-ku, Kobe-shi, Hyogo 650-0017, Japan
³ Division of Biochemistry, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan
⁴ Organ Development Research Laboratory, National Institute of Advanced Industrial Science and Technology, AIST Tsukuba Central 4, Tsukuba-shi, Ibaraki 305-8562, Japan
⁵ Department of Life Sciences (Biology), Graduate School of Arts and Sciences, University of Tokyo, 3-8-1, Komaba, Meguro-ku, Tokyo 153-8902, Japan
⁶ Department of Oral Histology, Matsumoto Dental University, 1780, Gobara, Hirooka, Shiojiri-shi, Nagano 399-0781, Japan
⁷ ICORP, Japan Science and Technology Agency (JST), 3-8-1, Komaba, Meguro-ku, Tokyo 153-8902, Japan

The Wnt signaling pathway is conserved across species, and is essential for early development. We previously identified nucleoredoxin (NRX) as a protein that interacts with dishevelled (Dvl) in vivo to negatively regulate the Wnt/β-catenin pathway. However, whether NRX affects another branch of the Wnt pathway, the Wnt/planar cell polarity (PCP) pathway, remains unclear. Here we show that NRX regulates the Wnt/PCP pathway. In Xenopus laevis, over-expression or depletion of NRX by injection of NRX mRNA or antisense morpholino oligonucleotide, respectively, yields the bent-axis phenotype that is typically observed in embryos with abnormal PCP pathway activity. In co-injection experiments of Dvl and NRX mRNA, NRX suppresses the Dvl-induced bent-axis phenotype. Over-expression or depletion of NRX also suppresses the convergent extension movements that are believed to underlie normal gastrulation. We also found that NRX can inhibit Dvl-induced up-regulation of c-Jun phosphorylation. These results indicate that NRX plays crucial roles in the Wnt/PCP pathway through Dvl and regulates Xenopus gastrulation movements.

^* Correspondence: hmiki{at}protein.osaka-u.ac.jp