ArticleThe Journal of biological chemistry2011
Type I keratin 17 protein is phosphorylated on serine 44 by p90 ribosomal protein S6 kinase 1 (RSK1) in a growth- and stress-dependent fashion.
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 19 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.
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.
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Who cites it
19 citing papers in PubMed, 35 citations in OpenAlex.
- Improving the Culture of Human Skin Explants for Use in Preclinical Testing of Wound Healing Treatments.Pharmaceutics · 2025Article
- SRC and ERK Regulate the Turnover of Cytoskeletal Keratin Filaments.International journal of molecular sciences · 2025Article
- Repeated stress to the skin amplifies neutrophil infiltration in a keratin 17- and PKCα-dependent manner.PLoS biology · 2024Article
- Keratin 17 covalently binds to alpha-enolase and exacerbates proliferation of keratinocytes in psoriasis.International journal of biological sciences · 2023Article
- Keratins as an Inflammation Trigger Point in Epidermolysis Bullosa Simplex.International journal of molecular sciences · 2021Review
- A role for keratin 17 during DNA damage response and tumor initiation.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Identification of stress responsive genes by studying specific relationships between mRNA and protein abundance.Heliyon · 2018Article
- Proteomic Analysis of Primary Human Airway Epithelial Cells Exposed to the Respiratory Toxicant Diacetyl.Journal of proteome research · 2017Article
- Assays for Posttranslational Modifications of Intermediate Filament Proteins.Methods in enzymology · 2016Article
- Phosphorylation and Reorganization of Keratin Networks: Implications for Carcinogenesis and Epithelial Mesenchymal Transition.Biomolecules & therapeutics · 2015Review
- Regulation of C-X-C chemokine gene expression by keratin 17 and hnRNP K in skin tumor keratinocytes.The Journal of cell biology · 2015Article
- Activation of the low molecular weight protein tyrosine phosphatase in keratinocytes exposed to hyperosmotic stress.PloS one · 2015Article
- Comparative proteomics analysis of differential proteins in respond to doxorubicin resistance in myelogenous leukemia cell lines.Proteome science · 2015Article
- A novel role for keratin 17 in coordinating oncogenic transformation and cellular adhesion in Ewing sarcoma.Molecular and cellular biology · 2013Article
- A conserved rod domain phosphotyrosine that is targeted by the phosphatase PTP1B promotes keratin 8 protein insolubility and filament organization.The Journal of biological chemistry · 2013Article
- Networking galore: intermediate filaments and cell migration.Current opinion in cell biology · 2013Review
- The expanding significance of keratin intermediate filaments in normal and diseased epithelia.Current opinion in cell biology · 2013Review
- Identification of novel interaction between annexin A2 and keratin 17: evidence for reciprocal regulation.The Journal of biological chemistry · 2012Article
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Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Keratin 17 (K17) is a type I intermediate filament protein that is constitutively expressed in ectoderm-derived epithelial appendages and robustly induced in epidermis following injury, during inflammation, and in chronic diseases such as psoriasis and cancer. Mutations within K17 are responsible for two rare diseases related to ectodermal dysplasias. Studies in K17-null mice uncovered several roles for K17, including structural support, resistance to TNFα-induced apoptosis, regulation of protein synthesis, and modulation of cytokine expression. Yet, little is known about the regulation of K17 protein via post-translational modification. Here, we report that serine 44 in the N-terminal head domain of K17 (K17-Ser(44)) is phosphorylated in response to extracellular stimuli (serum, EGF, and the phorbol ester 12-O-tetradecanoylphorbol-13-acetate) that alter skin keratinocyte growth, and to cellular stresses (sorbitol-induced hyperosmotic shock, UV irradiation, and hydrogen peroxide-induced oxidative stress). It also occurs in basaloid skin tumors in situ. Upon its stimulation in skin keratinocytes, K17-Ser(44) phosphorylation is induced rapidly but stays on transiently. The majority of the phosphorylated K17-Ser(44) pool is polymer-bound and is not obviously related to a change in filament organization. The amino acid sequence surrounding K17-Ser(44) matches the consensus for the AGC family of basophilic kinases. We show that p90 RSK1, an AGC kinase involved in the regulation of cell survival and proliferation, phosphorylates K17-Ser(44) in skin keratinocytes. These findings confirm and expand the tight link that has emerged between K17 up-regulation and growth and stress responses in the skin epithelium.
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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.