ArticleThe Journal of cell biology1994
Identification of the major physiologic phosphorylation site of human keratin 18: potential kinases and a role in filament reorganization.
Article in The Journal of cell biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 93 citations in OpenAlex.
- In focus in HCB.Histochemistry and cell biology · 2020Article
- Phosphorylation of keratin 18 serine 52 regulates mother-daughter centriole engagement and microtubule nucleation by cell cycle-dependent accumulation at the centriole.Histochemistry and cell biology · 2020Article
- Cytoskeletal and extracellular matrix proteins as markers for metastatic triple negative breast cancer.The Journal of international medical research · 2019Article
- Cytokeratin19 induced by HER2/ERK binds and stabilizes HER2 on cell membranes.Cell death and differentiation · 2015Article
- Chloride channel-3 promotes tumor metastasis by regulating membrane ruffling and is associated with poor survival.Oncotarget · 2015Article
- Functional module search in protein networks based on semantic similarity improves the analysis of proteomics data.Molecular & cellular proteomics : MCP · 2014Article
- A Rising Cancer Prevention Target of RSK2 in Human Skin Cancer.Frontiers in oncology · 2013Article
- Keratins in colorectal epithelial function and disease.International journal of experimental pathology · 2012Review
- Keratin 8 phosphorylation regulates keratin reorganization and migration of epithelial tumor cells.Journal of cell science · 2012Article
- 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.The Journal of biological chemistry · 2011Article
- Redox regulation of cytokeratin 18 protein by NADPH oxidase 1 in preneoplastic human epithelial cells.Journal of cancer research and clinical oncology · 2011Article
- p38 MAP kinase and MAPKAP kinases MK2/3 cooperatively phosphorylate epithelial keratins.The Journal of biological chemistry · 2010Article
- Shear stress induced reorganization of the keratin intermediate filament network requires phosphorylation by protein kinase C zeta.Molecular biology of the cell · 2009Article
- Identifying the role of specific motifs in the lens fiber cell specific intermediate filament phakosin.Investigative ophthalmology & visual science · 2007Article
- Raf-1 activation disrupts its binding to keratins during cell stress.The Journal of cell biology · 2004Article
- Nestin promotes the phosphorylation-dependent disassembly of vimentin intermediate filaments during mitosis.Molecular biology of the cell · 2003Article
- Keratin binding to 14-3-3 proteins modulates keratin filaments and hepatocyte mitotic progression.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Keratins turn over by ubiquitination in a phosphorylation-modulated fashion.The Journal of cell biology · 2000Article
- Active caspases and cleaved cytokeratins are sequestered into cytoplasmic inclusions in TRAIL-induced apoptosis.The Journal of cell biology · 2000Article
- The alpha isoform of protein kinase C is involved in signaling the response of desmosomes to wounding in cultured epithelial cells.Molecular biology of the cell · 2000Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
There is ample in vitro evidence that phosphorylation of intermediate filaments, including keratins, plays an important role in filament reorganization. In order to gain a better understanding of the function of intermediate filament phosphorylation, we sought to identify the major phosphorylation site of human keratin polypeptide 18 (K18) and study its role in filament assembly or reorganization. We generated a series of K18 ser-->ala mutations at potential phosphorylation sites, followed by expression in insect cells and comparison of the tryptic 32PO4-labeled patterns of the generated constructs. Using this approach, coupled with Edman degradation of the 32PO4-labeled tryptic peptides, and comparison with tryptic peptides analyzed after labeling normal human colonic tissues, we identified ser-52 as the major K18 physiologic phosphorylation site. Ser-52 in K18 is not glycosylated and matches consensus sequences for phosphorylation by CAM kinase, S6 kinase and protein kinase C, and all these kinases can phosphorylate K18 in vitro predominantly at that site. Expression of K18 ser-52-->ala mutant in mammalian cells showed minimal phosphorylation but no distinguishable difference in filament assembly when compared with wild-type K18. In contrast, the ser-52 mutation played a clear but nonexclusive role in filament reorganization, based on analysis of filament alterations in cells treated with okadaic acid or arrested at the G2/M stage of the cell cycle. Our results show that ser-52 is the major physiologic phosphorylation site of human K18 in interphase cells, and that its phosphorylation may play an in vivo role in filament reorganization.
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