Canonical Wnt signaling induces focal adhesion and Integrin beta-1 endocytosis
Summary: During canonical Wnt signaling, the Wnt receptor complex is sequestered together with glycogen synthase kinase 3 (GSK3) and Axin inside late endosomes, known as multivesicular bodies (MVBs). Here, we present experiments showing that Wnt causes the endocytosis of focal adhesion (FA) proteins...
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Format: | Article |
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Elsevier
2022-04-01
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Series: | iScience |
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Online Access: | http://www.sciencedirect.com/science/article/pii/S2589004222003935 |
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author | Nydia Tejeda-Muñoz Marco Morselli Yuki Moriyama Pooja Sheladiya Matteo Pellegrini Edward M. De Robertis |
author_facet | Nydia Tejeda-Muñoz Marco Morselli Yuki Moriyama Pooja Sheladiya Matteo Pellegrini Edward M. De Robertis |
author_sort | Nydia Tejeda-Muñoz |
collection | DOAJ |
description | Summary: During canonical Wnt signaling, the Wnt receptor complex is sequestered together with glycogen synthase kinase 3 (GSK3) and Axin inside late endosomes, known as multivesicular bodies (MVBs). Here, we present experiments showing that Wnt causes the endocytosis of focal adhesion (FA) proteins and depletion of Integrin β 1 (ITGβ1) from the cell surface. FAs and integrins link the cytoskeleton to the extracellular matrix. Wnt-induced endocytosis caused ITGβ1 depletion from the plasma membrane and was accompanied by striking changes in the actin cytoskeleton. In situ protease protection assays in cultured cells showed that ITGβ1 was sequestered within membrane-bounded organelles that corresponded to Wnt-induced MVBs containing GSK3 and FA-associated proteins. An in vivo model using Xenopus embryos dorsalized by Wnt8 mRNA showed that ITGβ1 depletion decreased Wnt signaling. The finding of a crosstalk between two major signaling pathways, canonical Wnt and focal adhesions, should be relevant to human cancer and cell biology |
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format | Article |
id | doaj.art-cbfd10f4bdd549a2aabbfdfecb58b5b7 |
institution | Directory Open Access Journal |
issn | 2589-0042 |
language | English |
last_indexed | 2024-04-13T02:33:13Z |
publishDate | 2022-04-01 |
publisher | Elsevier |
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series | iScience |
spelling | doaj.art-cbfd10f4bdd549a2aabbfdfecb58b5b72022-12-22T03:06:29ZengElsevieriScience2589-00422022-04-01254104123Canonical Wnt signaling induces focal adhesion and Integrin beta-1 endocytosisNydia Tejeda-Muñoz0Marco Morselli1Yuki Moriyama2Pooja Sheladiya3Matteo Pellegrini4Edward M. De Robertis5Department of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles 90095-1662, USA; Corresponding authorDipartimento di Scienze Chimiche, della Vita e della Sostenibilità Ambientale, University of Parma, Parm, ItalyDepartment of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles 90095-1662, USA; JT Biohistory Research Hall, Osaka, Japan and Chuo University, Faculty of Science and Engineering, Tokyo, JapanDepartment of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles 90095-1662, USADepartment of Molecular, Cellular and Developmental Biology, University of California, Los Angeles, CA 90095-1662, USADepartment of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles 90095-1662, USA; Corresponding authorSummary: During canonical Wnt signaling, the Wnt receptor complex is sequestered together with glycogen synthase kinase 3 (GSK3) and Axin inside late endosomes, known as multivesicular bodies (MVBs). Here, we present experiments showing that Wnt causes the endocytosis of focal adhesion (FA) proteins and depletion of Integrin β 1 (ITGβ1) from the cell surface. FAs and integrins link the cytoskeleton to the extracellular matrix. Wnt-induced endocytosis caused ITGβ1 depletion from the plasma membrane and was accompanied by striking changes in the actin cytoskeleton. In situ protease protection assays in cultured cells showed that ITGβ1 was sequestered within membrane-bounded organelles that corresponded to Wnt-induced MVBs containing GSK3 and FA-associated proteins. An in vivo model using Xenopus embryos dorsalized by Wnt8 mRNA showed that ITGβ1 depletion decreased Wnt signaling. The finding of a crosstalk between two major signaling pathways, canonical Wnt and focal adhesions, should be relevant to human cancer and cell biologyhttp://www.sciencedirect.com/science/article/pii/S2589004222003935Cell biologyDevelopmental biologyOmics |
spellingShingle | Nydia Tejeda-Muñoz Marco Morselli Yuki Moriyama Pooja Sheladiya Matteo Pellegrini Edward M. De Robertis Canonical Wnt signaling induces focal adhesion and Integrin beta-1 endocytosis iScience Cell biology Developmental biology Omics |
title | Canonical Wnt signaling induces focal adhesion and Integrin beta-1 endocytosis |
title_full | Canonical Wnt signaling induces focal adhesion and Integrin beta-1 endocytosis |
title_fullStr | Canonical Wnt signaling induces focal adhesion and Integrin beta-1 endocytosis |
title_full_unstemmed | Canonical Wnt signaling induces focal adhesion and Integrin beta-1 endocytosis |
title_short | Canonical Wnt signaling induces focal adhesion and Integrin beta-1 endocytosis |
title_sort | canonical wnt signaling induces focal adhesion and integrin beta 1 endocytosis |
topic | Cell biology Developmental biology Omics |
url | http://www.sciencedirect.com/science/article/pii/S2589004222003935 |
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