ArticleJournal of dermatological science2014
Obligatory roles of filamin A in E-cadherin-mediated cell-cell adhesion in epidermal keratinocytes.
Article in Journal of dermatological science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 20 citations in OpenAlex.
- Dysregulation of STS in keratinocytes promotes calcium signaling and differentiation.Scientific reports · 2025Article
- Calcium-Sensing Receptor Regulates Epidermal Intracellular CaThe Journal of investigative dermatology · 2019Article
- Sensitive Skin: Lessons From Transcriptomic Studies.Frontiers in medicine · 2019Review
- Signaling by Small GTPases at Cell-Cell Junctions: Protein Interactions Building Control and Networks.Cold Spring Harbor perspectives in biology · 2018Review
- Rho GTPases and actomyosin: Partners in regulating epithelial cell-cell junction structure and function.Experimental cell research · 2017Review
- FGFR3 silencing by siRNA inhibits invasion of A549 cells.Oncology letters · 2016Article
- Calcium-Sensing Receptor in Breast Physiology and Cancer.Frontiers in physiology · 2016Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
backgroundExtracellular Ca(2+) (Cao(2+))-induced E-cadherin-mediated cell-cell adhesion plays a critical role in promoting differentiation in epidermal keratinocytes. Our previous studies show that the calcium-sensing receptor (CaR) regulates keratinocyte cell-cell adhesion and differentiation via Rho A-mediated signaling. CaR forms a protein complex with Rho A, guanine nucleotide exchange factor Trio, and a cytoskeletal actin-binding protein, filamin A, at the cell-cell junctions in response to elevated Cao(2+) levels. Filamin A has the ability to interact directly with CaR, Trio, and Rho and mediate CaR-dependent signaling events.
objectiveThis study was conducted to investigate the roles of filamin A and Trio in regulating Cao(2+)-induced Rho activation and intercellular adhesion.
methodsExpression of filamin A and Trio in keratinocytes was inhibited by siRNA. Its effects on Cao(2+)-dependent junction formation and adhesion complex formation were evaluated by fluorescence immunostaining and immunoprecipitation. Endogenous Rho activity and expression of keratinocyte differentiation markers were also examined. The significance of the physical interactions of filamin A with Trio and Rho was assessed in dominant-negative inhibition studies.
resultsInhibiting filamin A expression blocked the formation of CaR-Rho A-Trio-E-cadherin protein complex. Knockdown of filamin A or Trio inhibited Cao(2+)-induced membrane localization and activation of Rho A, formation of the E-cadherin-catenin adhesion complex, and keratinocyte terminal differentiation. Expressing dominant-negative peptides disruptive to the endogenous filamin-Trio, filamin-Rho, and CaR-filamin interactions suppressed the formation of adherens junctions.
conclusionThrough physical interactions with CaR, Trio and Rho, filamin A generates a scaffold for organizing a signaling complex that promotes E-cadherin-mediated cell-cell adhesion and keratinocyte differentiation.
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