ArticleJournal of cell science2011
Protein 4.1R regulates cell adhesion, spreading, migration and motility of mouse keratinocytes by modulating surface expression of beta1 integrin.
Article in Journal of cell science, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- AKAP12 Variant 1 Knockout Enhances Vascular Endothelial Cell Motility.Journal of vascular research · 2025Article
- Designs of NKG2D-based immunotherapeutics for cancer.Frontiers in immunology · 2025Review
- Cytoskeletal Protein 4.1R in Health and Diseases.Biomolecules · 2024Review
- The Role of Cytoskeleton Protein 4.1 in Immunotherapy.International journal of molecular sciences · 2023Review
- Suppression of 4.1R enhances the potency of NKG2D-CAR T cells against pancreatic carcinoma via activating ERK signaling pathway.Oncogenesis · 2021Article
- Silencing EPB41 Gene Expression Leads to Cell Cycle Arrest, Migration Inhibition, and Upregulation of Cell Surface Antigen in DC2.4 Cells.Medical science monitor : international medical journal of experimental and clinical research · 2020Article
- Deficiency of αII-spectrin affects endothelial cell-matrix contact and migration leading to impairment of angiogenesis in vitro.Cellular & molecular biology letters · 2020Article
- Cytoskeletal Protein 4.1R Is a Positive Regulator of the FcεRI Signaling and Chemotaxis in Mast Cells.Frontiers in immunology · 2019Article
- [Construction of a stable 4.1R gene knockout cell model in RAW264.7 cells using CRISPR/Cas9 technique].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2017Article
- Kindlin-1 contributes to EGF-induced re-epithelialization in skin wound healing.International journal of molecular medicine · 2017Article
- Alternative polyadenylation in a family of paralogous EPB41 genes generates protein 4.1 diversity.RNA biology · 2017Article
- Protein 4.1G Regulates Cell Adhesion, Spreading, and Migration of Mouse Embryonic Fibroblasts through the β1 Integrin Pathway.The Journal of biological chemistry · 2016Article
- Article
- Integrins in Wound Healing.Advances in wound care · 2014Review
- Comprehensive characterization of protein 4.1 expression in epithelium of large intestine.Histochemistry and cell biology · 2014Article
- A 130-kDa protein 4.1B regulates cell adhesion, spreading, and migration of mouse embryo fibroblasts by influencing actin cytoskeleton organization.The Journal of biological chemistry · 2014Article
- Article
- Mapping the extracellular and membrane proteome associated with the vasculature and the stroma in the embryo.Molecular & cellular proteomics : MCP · 2013Article
- Band 4.1 proteins regulate integrin-dependent cell spreading.Biochemical and biophysical research communications · 2012Article
- Expression of ezrin correlates with malignant phenotype of lung cancer, and in vitro knockdown of ezrin reverses the aggressive biological behavior of lung cancer cells.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2012Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Protein 4.1R is a membrane-cytoskeleton adaptor protein that has diverse roles in controlling the cell surface expression and/or function of transmembrane proteins, and in organizing F-actin. 4.1R is expressed in keratinocytes, but its role in these cells has not been explored. Here, we have investigated the role of 4.1R in skin using 4.1R(-/-) mice. Cell adhesion, spreading, migration and motility were significantly impaired in 4.1R(-/-) keratinocytes, and 4.1R(-/-) mice exhibited defective epidermal wound healing. Cultured 4.1R(-/-) keratinocytes on fibronectin failed to form actin stress fibres and focal adhesions. Furthermore, in the absence of 4.1R, the surface expression, and consequently the activity of β1 integrin were reduced. These data enabled the identification of a functional role for protein 4.1R in keratinocytes by modulating the surface expression of β1 integrin, possibly through a direct association between 4.1R and β1 integrin.
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