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Journal Article

The LIM domain protein Wtip interacts with the receptor tyrosine kinase Ror2 and inhibits canonical Wnt signalling

MPS-Authors

van Wijk,  Nicole Verhey
Max Planck Society;

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Witte,  Florian
Dept. of Computational Molecular Biology (Head: Martin Vingron), Max Planck Institute for Molecular Genetics, Max Planck Society;

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Mundlos,  Stefan
Research Group Development & Disease (Head: Stefan Mundlos), Max Planck Institute for Molecular Genetics, Max Planck Society;

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Stricker,  Sigmar
Research Group Development & Disease (Head: Stefan Mundlos), Max Planck Institute for Molecular Genetics, Max Planck Society;

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Citation

van Wijk, N. V., Witte, F., Feike, A. C., Schambony, A., Birchmeier, W., Mundlos, S., et al. (2009). The LIM domain protein Wtip interacts with the receptor tyrosine kinase Ror2 and inhibits canonical Wnt signalling. Biochemical and Biophysical Research Communications, 390(2), 211-216. Retrieved from http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6WBK-4X9TTRS-3-7&_cdi=6713&_user=127795&_pii=S0006291X09018956&_orig=browse&_coverDate=12%2F11%2F2009&_sk=996099997&view=c&wchp=dGLzVzz-zSkWb&md5=c9f5ca81e4f3eb0d7f3d49493d36036c&ie=/sdarticle.pdf.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-7CA0-6
Abstract
Wtip is a LIM domain protein of the Ajuba/Zyxin family involved in kidney and neural crest development; Ror2 is a receptor tyrosine kinase involved in the development of skeleton, heart, lung, genitalia and kidneys. Here we describe Wtip as an intracellular interaction partner of Ror2. Full-length Ror2 recruits Wtip to the cell membrane, a mutant involved in human disease fails to do so. Both genes and proteins show overlapping expression in the mouse embryo. We show that Wtip is able to inhibit canonical Wnt signalling in mammalian cells and in Xenopus embryos linking Wtip to a crucial developmental pathway.