ReviewProceedings of the American Thoracic Society2010
The role of the ubiquitin proteasome pathway in keratin intermediate filament protein degradation.
Review in Proceedings of the American Thoracic Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
24 citing papers in PubMed, 44 citations in OpenAlex.
- Skin Organoids in Proteostasis Research: Early Insights into Aging.Biomolecules & therapeutics · 2026Review
- Proteomic profile of epidermal mucus fromFish and shellfish immunology reports · 2023Article
- Post-translational modifications to hemidesmosomes in human airway epithelial cells following diacetyl exposure.Scientific reports · 2022Article
- Airway basal cell injury after acute diacetyl (2,3-butanedione) vapor exposure.Toxicology letters · 2020Article
- Multifaceted role of keratins in epithelial cell differentiation and transformation.Journal of biosciences · 2019Review
- The Cytoskeleton-A Complex Interacting Meshwork.Cells · 2019Review
- Article
- Autophagy and Alzheimer's Disease: From Molecular Mechanisms to Therapeutic Implications.Frontiers in aging neuroscience · 2018Review
- Endocytosis and membrane receptor internalization: implication of F-BAR protein Carom.Frontiers in bioscience (Landmark edition) · 2017Review
- Monoallelic Mutations in the Translation Initiation Codon of KLHL24 Cause Skin Fragility.American journal of human genetics · 2016Article
- Article
- Functional Implications of O-GlcNAcylation-dependent Phosphorylation at a Proximal Site on Keratin 18.The Journal of biological chemistry · 2016Article
- Assays for Posttranslational Modifications of Intermediate Filament Proteins.Methods in enzymology · 2016Article
- Glypican-3 and KRT19 are markers associating with metastasis and poor prognosis of pancreatic ductal adenocarcinoma.Cancer biomarkers : section A of Disease markers · 2016Article
- Keratin 13 mutations associated with oral white sponge nevus in two Chinese families.Meta gene · 2014Article
- Group B streptococcal infection of the choriodecidua induces dysfunction of the cytokeratin network in amniotic epithelium: a pathway to membrane weakening.PLoS pathogens · 2014Article
- Post-translational modifications of intermediate filament proteins: mechanisms and functions.Nature reviews. Molecular cell biology · 2014Review
- Networking galore: intermediate filaments and cell migration.Current opinion in cell biology · 2013Review
- Aldosterone and angiotensin II induce protein aggregation in renal proximal tubules.Physiological reports · 2013Article
- Differentially expressed proteins in the skin mucus of Atlantic cod (Gadus morhua) upon natural infection with Vibrio anguillarum.BMC veterinary research · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Lung injury, whether caused by hypoxic or mechanical stresses, elicits a variety of responses at the cellular level. Alveolar epithelial cells respond and adapt to such injurious stimuli by reorganizing the cellular cytoskeleton, mainly accomplished through modification of the intermediate filament (IF) network. The structural and mechanical integrity in epithelial cells is maintained through this adaptive reorganization response. Keratin, the predominant IF expressed in epithelial cells, displays highly dynamic properties in response to injury, sometimes in the form of degradation of the keratin IF network. Post-translational modification, such as phosphorylation, targets keratin proteins for degradation in these circumstances. As with other structural and regulatory proteins, turnover of keratin is regulated by the ubiquitin (Ub)-proteasome pathway. The degradation process begins with activation of Ub by the Ub-activating enzyme (E1), followed by the exchange of Ub to the Ub-conjugating enzyme (E2). E2 shuttles the Ub molecule to the substrate-specific Ub ligase (E3), which then delivers the Ub to the substrate protein, thereby targeting it for degradation. In some cases of injury and IF-related disease, aggresomes form in epithelial cells. The mechanisms that regulate aggresome formation are currently unknown, although proteasome overload may play a role. Therefore, a more complete understanding of keratin degradation--causes, mechanisms, and consequences--will allow for a greater understanding of epithelial cell biology and lung pathology alike.
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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.