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Canonical Wnt Induces Focal Adhesion and Integrin Beta-1 Endocytosis

ABSTRACT: Canonical Wnt Induces Focal Adhesion and Integrin Beta-1 Endocytosis

PROVIDER: PRJNA795994 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR17532288_1.fastq.gz	Fastqsanger.gz
	SRR17532288_2.fastq.gz	Fastqsanger.gz
	SRR17532289_1.fastq.gz	Fastqsanger.gz
	SRR17532289_2.fastq.gz	Fastqsanger.gz
	SRR17532290_1.fastq.gz	Fastqsanger.gz

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Canonical Wnt Induces Focal Adhesion and Integrin Beta-1 Endocytosis

Project description:Activation of the Wnt pathway is at the core of many human cancers. During canonical Wnt signaling, the Lrp6 and Frizzled receptors bind to the Wnt growth factor, which leads to the complex being endocytosed. Glycogen Synthase Kinase 3 (GSK3), Dishevelled (Dvl), and Axin are sequestered inside the intraluminal vesicles of 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 provide link the cytoskeleton to the extracellular matrix. Wnt-induced macropinocytosis of the plasma membrane caused ITGβ1 depletion 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 focal adhesion-associated proteins. An in vivo model using Xenopus embryos dorsalized by Wnt8 mRNA showed that ITGβ1 depletion decreased Wnt signaling. The cross-talk between Wnt signaling, membrane trafficking, and focal adhesions should be relevant to human cancer and cell biology.

2022-03-18 | GSE193381 | GEO

Canonical Wnt signaling induces focal adhesion and Integrin beta-1 endocytosis.

Project description: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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Focal Adhesion Kinase Dependent Expression

Project description:The goal of this study was to identify transcripts, which are differentially regulatulated in the presence and absence of Focal Adhesion Kinase. As Focal Adhesion Kinase activity can depend upon cell density (Snijder et al. Nature 2009), biological replicates where cells, were seeded very sparsely or confluently, were used. Focal Adhesion Kinase Knockout (ATCC CRL-2644) and Rescue Cells (Sieg et al. 1998, clone DA2) were seeded at two different concentrations. Replicas refer to biological replicates, performed on different days. Only one single technical replicate has been done per biological replicate.

2013-09-17 | E-GEOD-43873 | biostudies-arrayexpress

Focal Adhesion Kinase Dependent Expression

2013-09-17 | GSE43873 | GEO

miR-29a-3p coordinates the ECM-integrin-adaptor protein axis to regulate focal adhesion in allergic rhinitis

Project description:miR-29a-3p coordinates the ECM-integrin-adaptor protein axis to regulate focal adhesion in allergic rhinitis

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sVEGFR-1 signaling through Î±5Î²1 integrin

Project description:Soluble VEGFR-1 (sVEGFR-1) acts both as a decoy receptor for VEGFs and as an extracellular matrix protein for Î±5Î²1 integrin. A sVEGFR-1-derived peptide that interacts with Î±5Î²1 integrin promotes angiogenesis. However, canonical signal downstream integrin activation is not induced, resulting into lack of focal adhesion maturation. We performed a gene expression profile of endothelial cells adhering on sVEGFR-1 compared to that of cells adhering on fibronectin, the principal Î±5Î²1 integrin ligand. Three protein kinase-C substrates, adducin, MARCKS, and radixin were differently modulated. Adducin and MARCKS were less phosphorylated whereas radixin was higher phosphorylated in sVEGFR-1 adhering cells, the latter leading to prolonged small GTPase Rac1 activation and induction of a pathway involving the heterotrimeric G protein Î±13. Altogether, our data indicated endothelial cell acquisition of an highly motile phenotype when adherent on sVEGFR-1. Finally, we indicated radixin as accountable for the angiogenic effect of Î±5Î²1 integrin interaction with sVEGFR-1 that in turn depends on an active VEGF-A/VEGFR-2 signaling. Endothelial cells were let adhere in Petri dishes coated with fibronectin or sVEGFR-1 before RNA extraction and hybridization on Affymetrix microarrays. Endothelial cells plated on BSA-treated Petri dishes were used as non-adhesion control. Each hybridization was performed in triplicate.

2014-01-20 | E-GEOD-32560 | biostudies-arrayexpress

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Project description:Effect of a tumor promoter TPA on collagen IV based focal adhesions from CHO cells expressing human integrin alpha1 with activating mutation E317A

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Project description:To explore the dynamics of integrin adhesion complex disassembly, isolated adhesion complexes from U2OS cells were subjected to mass spectrometry based proteomic analysis. U2OS cells were allowed to spread on FN, treated with nocodazole for 4 hours to disrupt microtubules. To coordinate microtubule-induced integrin adhesion complex disassembly nocodazole was subsequently washed out and adhesion complexes isolated at 5, 10 and 15 minutes during this process.

2016-07-20 | MSV000079967 | MassIVE

miR-29a-3p coordinates the ECM-integrin-adaptor protein axis to regulate focal adhesion in allergic rhinitis [RNA-Seq]

Project description:miR-29a-3p coordinates the ECM-integrin-adaptor protein axis to regulate focal adhesion in allergic rhinitis [RNA-Seq]

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