ArticleDevelopment (Cambridge, England)2016
IKKε inhibits PKC to promote Fascin-dependent actin bundling.
Article in Development (Cambridge, England), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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.
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- Synergistic assembly, disassembly, and protection of complex forms of bundled F-actin.The Journal of cell biology · 2026Article
- Article
- Dynamic phosphorylation of Fascin-1 orchestrates microglial phagocytosis and neurological recovery after spinal cord injury.Journal of neuroinflammation · 2025Article
- Scale-type-specific requirement for the mosquito Aedes aegypti Spindle-F homologue by regulating microtubule organization.Insect molecular biology · 2022Article
- Cytoskeletal Remodeling in Cancer.Biology · 2020Review
- The stable actin core of mechanosensory stereocilia features continuous turnover of actin cross-linkers.Molecular biology of the cell · 2018Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Signaling molecules have pleiotropic functions and are activated by various extracellular stimuli. Protein kinase C (PKC) is activated by diverse receptors, and its dysregulation is associated with diseases including cancer. However, how the undesired activation of PKC is prevented during development remains poorly understood. We have previously shown that a protein kinase, IKKε, is active at the growing bristle tip and regulates actin bundle organization during Drosophila bristle morphogenesis. Here, we demonstrate that IKKε regulates the actin bundle localization of a dynamic actin cross-linker, Fascin. IKKε inhibits PKC, thereby protecting Fascin from inhibitory phosphorylation. Excess PKC activation is responsible for the actin bundle defects in IKKε-deficient bristles, whereas PKC is dispensable for bristle morphogenesis in wild-type bristles, indicating that PKC is repressed by IKKε in wild-type bristle cells. These results suggest that IKKε prevents excess activation of PKC during bristle morphogenesis.
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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.