ArticleExperimental cell research2017
VANGL2 interacts with integrin αv to regulate matrix metalloproteinase activity and cell adhesion to the extracellular matrix.
Article in Experimental cell research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 38 citations in OpenAlex.
- Rac1 and Nectin3 are essential for planar cell polarity-directed axon guidance in the peripheral auditory system.Development (Cambridge, England) · 2025Article
- Article
- Vangl as a Master Scaffold for Wnt/Planar Cell Polarity Signaling in Development and Disease.Frontiers in cell and developmental biology · 2022Review
- The Biological Significance and Implications of Planar Cell Polarity for Nephrology.Frontiers in physiology · 2021Review
- Non-canonical Wnt signalling regulates scarring in biliary disease via the planar cell polarity receptors.Nature communications · 2020Article
- Vangl2 acts at the interface between actin and N-cadherin to modulate mammalian neuronal outgrowth.eLife · 2020Article
- Dorsal convergence of gastrula cells requires Vangl2 and an adhesion protein-dependent change in protrusive activity.Development (Cambridge, England) · 2019Article
- VANGL2 protein stability is regulated by integrin αv and the extracellular matrix.Experimental cell research · 2019Article
- Vangl2, a planar cell polarity molecule, is implicated in irreversible and reversible kidney glomerular injury.The Journal of pathology · 2018Article
- Vangl2-dependent regulation of membrane protrusions and directed migration requires a fibronectin extracellular matrix.Development (Cambridge, England) · 2018Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Planar cell polarity (PCP) proteins are implicated in a variety of morphogenetic processes including embryonic cell migration and potentially cancer progression. During zebrafish gastrulation, the transmembrane protein Vang-like 2 (VANGL2) is required for PCP and directed cell migration. These cell behaviors occur in the context of a fibrillar extracellular matrix (ECM). While it is thought that interactions with the ECM regulate cell migration, it is unclear how PCP proteins such as VANGL2 influence these events. Using an in vitro cell culture model system, we previously showed that human VANGL2 negatively regulates membrane type-1 matrix metalloproteinase (MMP14) and activation of secreted matrix metalloproteinase 2 (MMP2). Here, we investigated the functional relationship between VANGL2, integrin αvβ3, and MMP2 activation. We provide evidence that VANGL2 regulates cell surface integrin αvβ3 expression and adhesion to fibronectin, laminin, and vitronectin. Inhibition of MMP14/MMP2 activity suppressed the cell adhesion defect in VANGL2 knockdown cells. Furthermore, our data show that MMP14 and integrin αv are required for increased proteolysis by VANGL2 knockdown cells. Lastly, we have identified integrin αvβ3 as a novel VANGL2 binding partner. Together, these findings begin to dissect the molecular underpinnings of how VANGL2 regulates MMP activity and cell adhesion to the ECM.
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