ArticleThe Journal of cell biology2000
Keratins turn over by ubiquitination in a phosphorylation-modulated fashion.
Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed, 157 citations in OpenAlex.
- SRC and ERK Regulate the Turnover of Cytoskeletal Keratin Filaments.International journal of molecular sciences · 2025Article
- Ubiquitination is involved in PKC-mediated degradation of cell surface Kv1.5 channels.The Journal of biological chemistry · 2024Article
- Human APOE4 Protects High-Fat and High-Sucrose Diet Fed Targeted Replacement Mice against Fatty Liver Disease Compared to APOE3.Aging and disease · 2024Article
- Intermediate, but not average: The unusual lives of the nuclear lamin proteins.Current opinion in cell biology · 2023Review
- Deacetylation via SIRT2 prevents keratin-mutation-associated injury and keratin aggregation.JCI insight · 2023Article
- Revisiting the significance of keratin expression in complex epithelia.Journal of cell science · 2022Article
- Keratins as an Inflammation Trigger Point in Epidermolysis Bullosa Simplex.International journal of molecular sciences · 2021Review
- Keratin 7 Is a Constituent of the Keratin Network in Mouse Pancreatic Islets and Is Upregulated in Experimental Diabetes.International journal of molecular sciences · 2021Article
- Differential proteome profile of gill and spleen in three pathogen-infected Paralichthys olivaceus.Genes & genomics · 2021Article
- On the origin of germ cell neoplasia in situ: Dedifferentiation of human adult Sertoli cells in cross talk with seminoma cells in vitro.Neoplasia (New York, N.Y.) · 2021Article
- 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
- Cornification of nail keratinocytes requires autophagy for bulk degradation of intracellular proteins while sparing components of the cytoskeleton.Apoptosis : an international journal on programmed cell death · 2019Article
- Article
- The proteasome helps epithelial cells set up KAMPs.The Journal of cell biology · 2018Article
- Keratin 6a reorganization for ubiquitin-proteasomal processing is a direct antimicrobial response.The Journal of cell biology · 2018Article
- Autophagy and KRT8/keratin 8 protect degeneration of retinal pigment epithelium under oxidative stress.Autophagy · 2017Article
- Intermediate Filaments at the Junction of Mechanotransduction, Migration, and Development.Frontiers in cell and developmental biology · 2017Review
- Keratin impact on PKCδ- and ASMase-mediated regulation of hepatocyte lipid raft size - implication for FasR-associated apoptosis.Journal of cell science · 2016Article
- 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
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
Keratin polypeptides 8 and 18 (K8/18) are intermediate filament (IF) proteins that are expressed in glandular epithelia. Although the mechanism of keratin turnover is poorly understood, caspase-mediated degradation of type I keratins occurs during apoptosis and the proteasome pathway has been indirectly implicated in keratin turnover based on colocalization of keratin-ubiquitin antibody staining. Here we show that K8 and K18 are ubiquitinated based on cotransfection of His-tagged ubiquitin and human K8 and/or K18 cDNAs, followed by purification of ubiquitinated proteins and immunoblotting with keratin antibodies. Transfection of K8 or K18 alone yields higher levels of keratin ubiquitination as compared with cotransfection of K8/18, likely due to stabilization of the keratin heteropolymer. Most of the ubiquitinated species partition with the noncytosolic keratin fraction. Proteasome inhibition stabilizes K8 and K18 turnover, and is associated with accumulation of phosphorylated keratins, which indicates that although keratins are stable they still turnover. Analysis of K8 and K18 ubiquitination and degradation showed that K8 phosphorylation contributes to its stabilization. Our results provide direct evidence for K8 and K18 ubiquitination, in a phosphorylation modulated fashion, as a mechanism for regulating their turnover and suggest that other IF proteins could undergo similar regulation. These and other data offer a model that links keratin ubiquitination and hyperphosphorylation that, in turn, are associated with Mallory body deposits in a variety of liver diseases.
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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.