beta-Arrestin Interacts with the Beta/Gamma Subunits of Trimeric G-Proteins and Dishevelled in the Wnt/Ca2+ Pathway in Xenopus Gastrulation

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Authors

SEITZ Katharina DUERSCH Verena HARNOŠ Jakub BRYJA Vítězslav GENTZEL Marc SCHAMBONY Alexandra

Year of publication 2014
Type Article in Periodical
Magazine / Source PLOS ONE
MU Faculty or unit

Faculty of Science

Citation
Web http://apps.webofknowledge.com/full_record.do?product=UA&search_mode=GeneralSearch&qid=17&SID=R2g9W8Fv71CDiX3zjH6&page=1&doc=1#
Doi http://dx.doi.org/10.1371/journal.pone.0087132
Field Genetics and molecular biology
Keywords CONVERGENT EXTENSION MOVEMENTS; WNT SIGNALING PATHWAYS; WNT/BETA-CATENIN; VERTEBRATE GASTRULATION; PARAXIAL PROTOCADHERIN; TISSUE SEPARATION; ACTIVATION; FRIZZLED-7; LAEVIS; KINASE
Description beta-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 beta-Catenin independent signaling cascades including the Wnt/Planar Cell Polarity and the Wnt/Ca2+ cascades. Wnt/Planar Cell Polarity and Wnt/Ca2+ 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, beta-Arrestin has been identified as an essential effector protein in the Wnt/beta-Catenin and the Wnt/Planar Cell Polarity pathway. Our results demonstrate that beta-Arrestin is required in the Wnt/Ca2+ signaling cascade upstream of Protein Kinase C (PKC) and Ca2+/Calmodulin-dependent Protein Kinase II (CamKII). We have further characterized the role of beta-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 beta-Arrestin, the beta subunit of trimeric G-proteins and Dishevelled is required to induce PKC activation and membrane translocation. In Xenopus gastrulation, beta-Arrestin function in Wnt/Ca2+ signaling is essential for convergent extension movements. We further show that beta-Arrestin physically interacts with the beta subunit of trimeric G-proteins and Dishevelled, and that the interaction between beta-Arrestin and Dishevelled is promoted by the beta/gamma subunits of trimeric G-proteins, indicating the formation of a multiprotein signaling complex.
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