ArticleThe Journal of biological chemistry2011
Keratin hypersumoylation alters filament dynamics and is a marker for human liver disease and keratin mutation.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 70 citations in OpenAlex.
- The Tilapia Cyst Tissue Enclosing the ProliferatingInternational journal of molecular sciences · 2024Article
- Article
- Deacetylation via SIRT2 prevents keratin-mutation-associated injury and keratin aggregation.JCI insight · 2023Article
- Keratins as an Inflammation Trigger Point in Epidermolysis Bullosa Simplex.International journal of molecular sciences · 2021Review
- SUMO paralogue-specific functions revealed through systematic analysis of human knockout cell lines and gene expression data.Molecular biology of the cell · 2021Article
- SUMOylation of α-tubulin is a novel modification regulating microtubule dynamics.Journal of molecular cell biology · 2021Article
- Posttranslational modifications of the cytoskeleton.Cytoskeleton (Hoboken, N.J.) · 2021Review
- Quantitative SUMO proteomics identifies PIAS1 substrates involved in cell migration and motility.Nature communications · 2020Article
- Multifaceted role of keratins in epithelial cell differentiation and transformation.Journal of biosciences · 2019Review
- SUMOylation of periplakin is critical for efficient reorganization of keratin filament network.Molecular biology of the cell · 2019Article
- Intermediate filaments and IF-associated proteins: from cell architecture to cell proliferation.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2019Review
- Spatiotemporal distribution of small ubiquitin-like modifiers during human placental development and in response to oxidative and inflammatory stress.The Journal of physiology · 2018Article
- Construction of developmental lineage relationships in the mouse mammary gland by single-cell RNA profiling.Nature communications · 2017Article
- Intracellular Motility of Intermediate Filaments.Cold Spring Harbor perspectives in biology · 2017Review
- Isolation of Intermediate Filament Proteins from Multiple Mouse Tissues to Study Aging-associated Post-translational Modifications.Journal of visualized experiments : JoVE · 2017Article
- Intermediate Filaments at the Junction of Mechanotransduction, Migration, and Development.Frontiers in cell and developmental biology · 2017Review
- Expression, Localization of SUMO-1, and Analyses of Potential SUMOylated Proteins inFrontiers in physiology · 2017Article
- Anaplasma phagocytophilum-Occupied Vacuole Interactions with the Host Cell Cytoskeleton.Veterinary sciences · 2016Article
- Functional Implications of O-GlcNAcylation-dependent Phosphorylation at a Proximal Site on Keratin 18.The Journal of biological chemistry · 2016Article
- Intermediate filament dynamics: What we can see now and why it matters.BioEssays : news and reviews in molecular, cellular and developmental biology · 2016Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
Abstract
Keratin polypeptide 8 (K8) associates noncovalently with its partners K18 and/or K19 to form the intermediate filament cytoskeleton of hepatocytes and other simple-type epithelial cells. Human K8, K18, and K19 variants predispose to liver disease, whereas site-specific keratin phosphorylation confers hepatoprotection. Because stress-induced protein phosphorylation regulates sumoylation, we hypothesized that keratins are sumoylated in an injury-dependent manner and that keratin sumoylation is an important regulatory modification. We demonstrate that K8/K18/K19, epidermal keratins, and vimentin are sumoylated in vitro. Upon transfection, K8, K18, and K19 are modified by poly-SUMO-2/3 chains on Lys-285/Lys-364 (K8), Lys-207/Lys-372 (K18), and Lys-208 (K19). Sumoylation affects filament organization and stimulus-induced keratin solubility and is partially inhibited upon mutation of one of three known K8 phosphorylation sites. Extensive sumoylation occurs in cells transfected with individual K8, K18, or K19 but is limited upon heterodimerization (K8/K18 or K8/K19) in the absence of stress. In contrast, keratin sumoylation is significantly augmented in cells and tissues during apoptosis, oxidative stress, and phosphatase inhibition. Poly-SUMO-2/3 conjugates are present in chronically injured but not normal, human, and mouse livers along with polyubiquitinated and large insoluble keratin-containing complexes. Notably, common human K8 liver disease-associated variants trigger keratin hypersumoylation with consequent diminished solubility. In contrast, modest sumoylation of wild type K8 promotes solubility. Hence, conformational changes induced by keratin natural mutations and extensive tissue injury result in K8/K18/K19 hypersumoylation, which retains keratins in an insoluble compartment, thereby limiting their cytoprotective function.
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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.