ArticleNature cell biology2010
Cytoskeletal keratin glycosylation protects epithelial tissue from injury.
Article in Nature cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 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
71 citing papers in PubMed, 121 citations in OpenAlex.
- Regulation of Keratin Chemical Modifications: Potential Molecular Mechanisms in Proliferative Diseases.International journal of molecular sciences · 2026Review
- Keratin 20 Suppresses Exosomal Secretion of Peroxiredoxin 2 and Ferroptosis in Acute Kidney Injury.Journal of the American Society of Nephrology : JASN · 2026Article
- Phosphoinositide signalling in cell motility and adhesion.Nature cell biology · 2025Review
- Phosphoinositide signaling at the cytoskeleton in the regulation of cell dynamics.Cell death & disease · 2025Review
- Repeated stress to the skin amplifies neutrophil infiltration in a keratin 17- and PKCα-dependent manner.PLoS biology · 2024Article
- The relationship between keratin 18 and epithelial-derived tumors: as a diagnostic marker, prognostic marker, and its role in tumorigenesis.Frontiers in oncology · 2024Review
- O-GlcNAcylation regulates neurofilament-light assembly and function and is perturbed by Charcot-Marie-Tooth disease mutations.Nature communications · 2023Article
- Plasma Cytokeratin-18 Fragment Level Reflects the Metabolic Phenotype in Obesity.Biomolecules · 2023Article
- The apoptotic effects of soybean agglutinin were induced through three different signal pathways by down-regulating cytoskeleton proteins in IPEC-J2 cells.Scientific reports · 2023Article
- Immunocytochemical characterization ofFrontiers in medicine · 2023Article
- Keratins as an Inflammation Trigger Point in Epidermolysis Bullosa Simplex.International journal of molecular sciences · 2021Review
- Keratin 8/18 Regulate the Akt Signaling Pathway.International journal of molecular sciences · 2021Article
- Revealing the Roles of Keratin 8/18-Associated Signaling Proteins Involved in the Development of Hepatocellular Carcinoma.International journal of molecular sciences · 2021Review
- Role ofPhysiological reviews · 2021Review
- Posttranslational modifications of the cytoskeleton.Cytoskeleton (Hoboken, N.J.) · 2021Review
- Combination of multiple computational methods revealing specific sub-sectional recognition and hydrogen-bond dependent transportation of CKII peptide fragment in O-GlcNAc transferase.Computational and structural biotechnology journal · 2021Article
- Pathophysiology of NAFLD and NASH in Experimental Models: The Role of Food Intake Regulating Peptides.Frontiers in endocrinology · 2020Review
- Keratin 18 is an integral part of the intermediate filament network in murine skeletal muscle.American journal of physiology. Cell physiology · 2020Article
- Biological Assessment of Zn-Based Absorbable Metals for Ureteral Stent Applications.Materials (Basel, Switzerland) · 2019Article
- Liver disease-associated keratin 8 and 18 mutations modulate keratin acetylation and methylation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
11 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 3 institutions in 3 countries.
Funding
Abstract
Keratins 8 and 18 (K8 and K18) are heteropolymeric intermediate filament phosphoglycoproteins of simple-type epithelia. Mutations in K8 and K18 predispose the affected individual to liver disease as they protect hepatocytes from apoptosis. K18 undergoes dynamic O-linked N-acetylglucosamine glycosylation at Ser 30, 31 and 49. We investigated the function of K18 glycosylation by generating mice that overexpress human K18 S30/31/49A substitution mutants that cannot be glycosylated (K18-Gly(-)), and compared the susceptibility of these mice to injury with wild-type and other keratin-mutant mice. K18-Gly(-) mice are more susceptible to liver and pancreatic injury and apoptosis induced by streptozotocin or to liver injury by combined N-acetyl-D-glucosaminidase inhibition and Fas administration. The enhanced apoptosis in the livers of mice that express K18-Gly(-) involves the inactivation of Akt1 and protein kinase Ctheta as a result of their site-specific hypophosphorylation. Akt1 binds to K8, which probably contributes to the reciprocal hyperglycosylation and hypophosphorylation of Akt1 that occurs on K18 hypoglycosylation, and leads to decreased Akt1 kinase activity. Therefore, K18 glycosylation provides a unique protective role in epithelial injury by promoting the phosphorylation and activation of cell-survival kinases.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.