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

Van Wijk NV, Witte F, Feike AC, Schambony A, Birchmeier W, Mundlos S, Stricker S (2009)

Publication Type: Journal article, Original article

Subtype: other

Publication year: 2009

Journal

Biochemical and Biophysical Research Communications Elsevier

Publisher: Elsevier Inc.

Book Volume: 390

Pages Range: 211-216

Journal Issue: 2

URI: http://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=19785987&retmode=ref&cmd=prlinks

DOI: 10.1016/j.bbrc.2009.09.086

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.

Authors with CRIS profile

Alexandra Schambony Lehrstuhl für Entwicklungsbiologie

Involved external institutions

Max-Planck-Institut für molekulare Genetik / Max Planck Institute for Molecular Genetics DE Germany (DE) Max-Delbrück-Centrum für Molekulare Medizin / Max Delbrück Center for Molecular Medicine (MDC) Berlin-Buch DE Germany (DE)

How to cite

APA:

Van Wijk, N.V., Witte, F., Feike, A.C., Schambony, A., Birchmeier, W., Mundlos, S., & Stricker, S. (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. https://doi.org/10.1016/j.bbrc.2009.09.086

MLA:

Van Wijk, Nicole Verhey, et al. "The LIM domain protein Wtip interacts with the receptor tyrosine kinase Ror2 and inhibits canonical Wnt signalling." Biochemical and Biophysical Research Communications 390.2 (2009): 211-216.

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