ArticleJournal of cell science2022
Molecular determinants of αVβ5 localization in flat clathrin lattices - role of αVβ5 in cell adhesion and proliferation.
Article in Journal of cell science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- Load-dependent RGD-context sensing via αV-class integrins reprograms cell adhesion and mechanics.Nature communications · 2026Article
- Regulation of reticular adhesions by KANK2 and talin2 in two melanoma cell lines.Cell communication and signaling : CCS · 2026Article
- KANK2 at focal adhesions regulates their maintenance and dynamics, while at fibrillar adhesions it influences cell migration via microtubule-dependent mechanism.Cell communication and signaling : CCS · 2026Article
- Dynamics of the formation of flat clathrin lattices in response to growth factor stimulus.PLoS computational biology · 2026Article
- Focal Adhesion and Cancer Cell Cycle-Associated Resistance.ACS omega · 2026Review
- Dynamics of the formation of flat clathrin lattices in response to growth factor stimulus.bioRxiv : the preprint server for biology · 2025Article
- Caskin2 is a novel talin- and Abi1-binding protein that promotes cell motility.Journal of cell science · 2024Article
- Canonical and non-canonical integrin-based adhesions dynamically interconvert.Nature communications · 2024Article
- The ancestral type of the R-RAS protein has oncogenic potential.Cellular & molecular biology letters · 2024Article
- Mechano-regulation by clathrin pit-formation and passive cholesterol-dependent tubules during de-adhesion.Cellular and molecular life sciences : CMLS · 2024Article
- Article
- Reticular adhesions are assembled at flat clathrin lattices and opposed by active integrin α5β1.The Journal of cell biology · 2023Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
The vitronectin receptor integrin αVβ5 can reside in two distinct adhesion structures - focal adhesions (FAs) and flat clathrin lattices (FCLs). Here, we investigate the mechanism that regulates the subcellular distribution of β5 in keratinocytes and show that β5 has approximately 7- and 5-fold higher affinity for the clathrin adaptors ARH (also known as LDLRAP1) and Numb, respectively, than for the talin 1 (TLN1); all proteins that bind to the membrane-proximal NPxY motif of the β5 cytoplasmic domain. Using mass spectrometry, we identified β5 interactors, including the Rho GEFs p115Rho-GEF and GEF-H1 (also known as ARHGEF1 and ARHGEF2, respectively), and the serine protein kinase MARK2, depletion of which diminishes the clustering of β5 in FCLs. Replacement of two serine residues (S759 and S762) in the β5 cytoplasmic domain with phospho-mimetic glutamate residues causes a shift in the localization of β5 from FAs into FCLs without affecting the interactions with MARK2, p115Rho-GEF or GEF-H1. Instead, we demonstrate that changes in the actomyosin-based cellular contractility by ectopic expression of activated Rho or disruption of microtubules regulates β5 localization. Finally, we present evidence that β5 in either FAs or FCLs functions to promote adhesion to vitronectin, cell spreading, and proliferation.
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Registered trials
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