β-Arrestin interacts with the beta/gamma subunits of trimeric G-proteins and dishevelled in the Wnt/Ca(2+) pathway in xenopus gastrulation.

Seitz K, Duersch V, Harnos J, Bryja V, Gentzel M, Schambony A (2014)

Publication Status: Published

Publication Type: Journal article, Original article

Publication year: 2014

Journal

PLoS ONE Public Library of Science

Publisher: Public Library of Science

Book Volume: 9

Article Number: e87132

Journal Issue: 1

URI: http://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=24489854&retmode=ref&cmd=prlinks

DOI: 10.1371/journal.pone.0087132

Abstract

β-Catenin independent, non-canonical Wnt signaling pathways play a major role in the regulation of morphogenetic movements in vertebrates. The term non-canonical Wnt signaling comprises multiple, intracellularly divergent, Wnt-activated and β-Catenin independent signaling cascades including the Wnt/Planar Cell Polarity and the Wnt/Ca cascades. Wnt/Planar Cell Polarity and Wnt/Ca pathways share common effector proteins, including the Wnt ligand, Frizzled receptors and Dishevelled, with each other and with additional branches of Wnt signaling. Along with the aforementioned proteins, β-Arrestin has been identified as an essential effector protein in the Wnt/β-Catenin and the Wnt/Planar Cell Polarity pathway. Our results demonstrate that β-Arrestin is required in the Wnt/Ca signaling cascade upstream of Protein Kinase C (PKC) and Ca/ Calmodulin-dependent Protein Kinase II (CamKII). We have further characterized the role of β-Arrestin in this branch of non-canonical Wnt signaling by knock-down and rescue experiments in Xenopus embryo explants and analyzed protein-protein interactions in 293T cells. Functional interaction of β-Arrestin, the β subunit of trimeric G-proteins and Dishevelled is required to induce PKC activation and membrane translocation. In Xenopus gastrulation, β-Arrestin function in Wnt/Ca signaling is essential for convergent extension movements. We further show that β-Arrestin physically interacts with the β subunit of trimeric G-proteins and Dishevelled, and that the interaction between β-Arrestin and Dishevelled is promoted by the beta/gamma subunits of trimeric G-proteins, indicating the formation of a multiprotein signaling complex. © 2014 Seitz et al.

Authors with CRIS profile

Alexandra Schambony Lehrstuhl für Entwicklungsbiologie

Involved external institutions

Masaryk University CZ Czech Republic (CZ) Max-Planck-Institut für molekulare Zellbiologie und Genetik / Max Planck Institute of Molecular Cell Biology and Genetics (MPI-CBG) DE Germany (DE)

How to cite

APA:

Seitz, K., Duersch, V., Harnos, J., Bryja, V., Gentzel, M., & Schambony, A. (2014). β-Arrestin interacts with the beta/gamma subunits of trimeric G-proteins and dishevelled in the Wnt/Ca(2+) pathway in xenopus gastrulation. PLoS ONE, 9(1). https://dx.doi.org/10.1371/journal.pone.0087132

MLA:

Seitz, Katharina, et al. "β-Arrestin interacts with the beta/gamma subunits of trimeric G-proteins and dishevelled in the Wnt/Ca(2+) pathway in xenopus gastrulation." PLoS ONE 9.1 (2014).

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