β-Arrestin Interacts with the Beta/Gamma Subunits of Trimeric G-Proteins and Dishevelled in the Wnt/Ca2+ Pathway in Xenopus Gastrulation
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/...
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| description | 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/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, 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/Ca2+ signaling cascade upstream of Protein Kinase C (PKC) and Ca2+/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/Ca2+ 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. |
| doi_str_mv | 10.1371/journal.pone.0087132 |
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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/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, 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/Ca2+ signaling cascade upstream of Protein Kinase C (PKC) and Ca2+/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/Ca2+ 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.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0087132</identifier><identifier>PMID: 24489854</identifier><language>eng</language><publisher>San Francisco: Public Library of Science</publisher><subject>Arrestin ; Biology ; Ca2+/calmodulin-dependent protein kinase II ; Calcium signalling ; Calcium-binding protein ; Calmodulin ; Cascades ; Cell adhesion & migration ; Cell culture ; Developmental biology ; Dishevelled protein ; Embryos ; Explants ; Frizzled protein ; Gastrulation ; Kinases ; Plasmids ; Polarity ; Protein interaction ; Protein kinase C ; Proteins ; Receptors ; Signal transduction ; Translocation ; Vertebrates ; Wnt protein ; Xenopus ; Xenopus laevis ; β-Catenin</subject><ispartof>PloS one, 2014-01, Vol.9 (1), p.e87132</ispartof><rights>2014 Seitz et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2014 Seitz et al 2014 Seitz et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c334t-10686890a0d92f72efef2b76186db783c34e4d5b10ec5a971bd5a602f13b82d93</citedby><cites>FETCH-LOGICAL-c334t-10686890a0d92f72efef2b76186db783c34e4d5b10ec5a971bd5a602f13b82d93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3906129/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3906129/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2915,23845,27901,27902,53766,53768,79343,79344</link.rule.ids></links><search><creatorcontrib>Seitz, Katharina</creatorcontrib><creatorcontrib>Dürsch, Verena</creatorcontrib><creatorcontrib>Harnoš, Jakub</creatorcontrib><creatorcontrib>Bryja, Vitezslav</creatorcontrib><creatorcontrib>Gentzel, Marc</creatorcontrib><creatorcontrib>Schambony, Alexandra</creatorcontrib><title>β-Arrestin Interacts with the Beta/Gamma Subunits of Trimeric G-Proteins and Dishevelled in the Wnt/Ca2+ Pathway in Xenopus Gastrulation</title><title>PloS one</title><description>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/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, 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/Ca2+ signaling cascade upstream of Protein Kinase C (PKC) and Ca2+/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/Ca2+ 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.</description><subject>Arrestin</subject><subject>Biology</subject><subject>Ca2+/calmodulin-dependent protein kinase II</subject><subject>Calcium signalling</subject><subject>Calcium-binding protein</subject><subject>Calmodulin</subject><subject>Cascades</subject><subject>Cell adhesion & migration</subject><subject>Cell culture</subject><subject>Developmental biology</subject><subject>Dishevelled protein</subject><subject>Embryos</subject><subject>Explants</subject><subject>Frizzled protein</subject><subject>Gastrulation</subject><subject>Kinases</subject><subject>Plasmids</subject><subject>Polarity</subject><subject>Protein interaction</subject><subject>Protein kinase 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one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Seitz, Katharina</au><au>Dürsch, Verena</au><au>Harnoš, Jakub</au><au>Bryja, Vitezslav</au><au>Gentzel, Marc</au><au>Schambony, Alexandra</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>β-Arrestin Interacts with the Beta/Gamma Subunits of Trimeric G-Proteins and Dishevelled in the Wnt/Ca2+ Pathway in Xenopus Gastrulation</atitle><jtitle>PloS one</jtitle><date>2014-01-29</date><risdate>2014</risdate><volume>9</volume><issue>1</issue><spage>e87132</spage><pages>e87132-</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><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/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, 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/Ca2+ signaling cascade upstream of Protein Kinase C (PKC) and Ca2+/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/Ca2+ 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.</abstract><cop>San Francisco</cop><pub>Public Library of Science</pub><pmid>24489854</pmid><doi>10.1371/journal.pone.0087132</doi><oa>free_for_read</oa></addata></record> |
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| subjects | Arrestin Biology Ca2+/calmodulin-dependent protein kinase II Calcium signalling Calcium-binding protein Calmodulin Cascades Cell adhesion & migration Cell culture Developmental biology Dishevelled protein Embryos Explants Frizzled protein Gastrulation Kinases Plasmids Polarity Protein interaction Protein kinase C Proteins Receptors Signal transduction Translocation Vertebrates Wnt protein Xenopus Xenopus laevis β-Catenin |
| title | β-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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