ArticleThe Journal of cell biology1991
Cytokeratin phosphorylation, cytokeratin filament severing and the solubilization of the maternal mRNA Vg1.
Article in The Journal of cell biology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 92 citations in OpenAlex.
- Regulation of neurofilament length and transport by a dynamic cycle of phospho-dependent polymer severing and annealing.Molecular biology of the cell · 2023Article
- Desmosome dualism - most of the junction is stable, but a plakophilin moiety is persistently dynamic.Journal of cell science · 2021Article
- Leukamenin E Induces K8/18 Phosphorylation and Blocks the Assembly of Keratin Filament Networks Through ERK Activation.International journal of molecular sciences · 2020Article
- Modeling microtubule-based transport and anchoring of mRNA.SIAM journal on applied dynamical systems · 2018Article
- Severing and end-to-end annealing of neurofilaments in neurons.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Organization of cytokeratin cytoskeleton and germ plasm in the vegetal cortex of Xenopus laevis oocytes depends on coding and non-coding RNAs: three-dimensional and ultrastructural analysis.Experimental cell research · 2007Article
- Caspase cleavage of keratin 18 and reorganization of intermediate filaments during epithelial cell apoptosis.The Journal of cell biology · 1997Article
- Intermediate filaments as dynamic structures.Cancer metastasis reviews · 1996Review
- Implications of intermediate filament protein phosphorylation.Cancer metastasis reviews · 1996Review
- A nontetrameric species is the major soluble form of keratin in Xenopus oocytes and rabbit reticulocyte lysates.The Journal of cell biology · 1996Article
- Dynamics of human keratin 18 phosphorylation: polarized distribution of phosphorylated keratins in simple epithelial tissues.The Journal of cell biology · 1995Article
- Identification of the major physiologic phosphorylation site of human keratin 18: potential kinases and a role in filament reorganization.The Journal of cell biology · 1994Article
- Regulated docking of nuclear membrane vesicles to vimentin filaments during mitosis.The Journal of cell biology · 1993Article
- RNA on the move: the mRNA localization pathway.The Journal of cell biology · 1993Review
- Host cell factors controlling vimentin organization in the Xenopus oocyte.The Journal of cell biology · 1992Article
- Evidence that the deep keratin filament systems of the Xenopus embryo act to ensure normal gastrulation.Proceedings of the National Academy of Sciences of the United States of America · 1992Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
During meiotic maturation, the cortical cytokeratin filament system of the Xenopus oocyte disappears (Klymkowsky, M. W., and L. A. Maynell. 1989. Dev. Biol. 134:479). Here we demonstrate that this disappearance results from the severing of cytokeratin filaments into a heterogenous population of oligomers, with S- values ranging from 12S and greater. Cytokeratin filament severing correlates with the hyperphosphorylation of the type II cytokeratin of the oocyte. Both the severing of cytokeratin filaments and cytokeratin hyperphosphorylation are reversed by treatment with cycloheximide. These data suggest that fragmentation of cytokeratin filaments is controlled, at least in part, by the phosphorylation of the type II cytokeratin, and that the cytokeratin kinase activity responsible is biosynthetically labile. Cytokeratin filaments have been suggested to anchor the maternal mRNA Vg1 to the vegetal cortex of the oocyte (Pondel, M., and M. L. King. 1988. Proc. Natl. Acad. Sci. USA. 85:7216). By injecting fractions containing active maturation promoting factor or a purified, mutant cyclin protein, we find that the bulk of the Vg1 mRNA in the oocyte can be solubilized under conditions that block the fragmentation of cytokeratin filaments, and that the fragmentation of cytokeratin filaments itself leads to the solubilization of only a minor fraction of the Vg1 mRNA. Thus, at best, cytokeratin filaments directly anchor only a minor fraction of the Vg1 mRNA in the oocyte. Moreover, factors distinct from maturation promoting factor appear to be required for the complete solubilization of Vg1 mRNA during oocyte maturation.
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