Retinoic acid-inducible G protein-coupled receptors bind to frizzled receptors and may activate non-canonical Wnt signaling

Yuko Harada; Chika Yokota; Raymond Habas; Diane C Slusarski; Xi He

doi:10.1016/j.bbrc.2007.04.208

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Retinoic acid-inducible G protein-coupled receptors bind to frizzled receptors and may activate non-canonical Wnt signaling

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Retinoic acid-inducible G protein-coupled receptors bind to frizzled receptors and may activate non-canonical Wnt signaling

Yuko Harada, Chika Yokota, Raymond Habas, Diane C Slusarski and Xi He

Biochemical and biophysical research communications, Vol.358(4), pp.968-975

2007

DOI: 10.1016/j.bbrc.2007.04.208

PMCID: PMC2854581

PMID: 17521608

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Abstract

Frizzled (Fz) seven-pass transmembrane receptors are Wnt receptors and function in a variety of developmental pathways. Here we identify retinoic acid-inducible gene-1, 2, 3, and 4 (RAIG1, 2, 3, and 4) as potential Fz binding proteins. RAIG proteins are seven-pass transmembrane receptors, and Xenopus RAIG2, 3, and 4 are expressed in early gastrula. XRAIG2 can activate small GTPases, such as RhoA, Rac, and Cdc42, and c-jun N-terminal kinase, thus exhibit activities that overlap with non-canonical Wnt/Fz signaling. Injection of XRAIG2 mRNA into Xenopus embryo causes a severe shortened and bent body axis due to defective gastrulation movements, reminiscent of abnormal non-canonical Wnt signaling. XRAIG2 affects convergent extension in activin-treated animal caps, which can be partially rescued by co-injection of a dominant-negative form of Cdc42. In zebrafish embryo, XRAIG2 also causes Ca 2+ flux, one of the consequences of non-canonical Wnt signaling. These results suggest a possible crosstalk/integration between Wnt/Frizzled and RAIG signal transduction pathways.

G protein-coupled receptor

Convergent extension

Gastrulation

Rac

JNK

Ca 2+ flux

RAIG

Frizzled

RhoA

Cdc42

Details

Title: Subtitle: Retinoic acid-inducible G protein-coupled receptors bind to frizzled receptors and may activate non-canonical Wnt signaling
Creators: Yuko Harada - Neurobiology Program, Children’s Hospital Boston, Department of Neurology, Harvard Medical School, Boston, MA 02115, USA
Chika Yokota - Neurobiology Program, Children’s Hospital Boston, Department of Neurology, Harvard Medical School, Boston, MA 02115, USA
Raymond Habas - Department of Biochemistry, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson School of Medicine, Piscataway, NJ 08854, USA
Diane C Slusarski - Department of Biological Sciences, University of Iowa, Iowa City, IA 52242, USA
Xi He - Neurobiology Program, Children’s Hospital Boston, Department of Neurology, Harvard Medical School, Boston, MA 02115, USA
Resource Type: Journal article
Publication Details: Biochemical and biophysical research communications, Vol.358(4), pp.968-975
DOI: 10.1016/j.bbrc.2007.04.208
PMID: 17521608
PMCID: PMC2854581
NLM abbreviation: Biochem Biophys Res Commun
ISSN: 0006-291X
eISSN: 1090-2104
Publisher: Elsevier Inc
Language: English
Date published: 2007
Academic Unit: Iowa Neuroscience Institute; Biology
Record Identifier: 9983992094102771

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