ArticleProceedings of the National Academy of Sciences of the United States of America2016
Mimicking transient activation of protein kinases in living cells.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
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- Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation.Journal of visualized experiments : JoVE · 2024Article
- Förster resonance energy transfer biosensors for fluorescence and time-gated luminescence analysis of rac1 activity.Scientific reports · 2022Article
- NK1 antagonists attenuate tau phosphorylation after blast and repeated concussive injury.Scientific reports · 2021Article
- Light-regulated allosteric switch enables temporal and subcellular control of enzyme activity.eLife · 2020Article
- Septin2 mediates podosome maturation and endothelial cell invasion associated with angiogenesis.The Journal of cell biology · 2020Article
- Engineering Optogenetic Protein Analogs.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Time-Variant SRC Kinase Activation Determines Endothelial Permeability Response.Cell chemical biology · 2019Article
- Sphingolipids Signaling in Lamellipodia Formation and Enhancement of Endothelial Barrier Function.Current topics in membranes · 2018Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Physiological stimuli activate protein kinases for finite periods of time, which is critical for specific biological outcomes. Mimicking this transient biological activity of kinases is challenging due to the limitations of existing methods. Here, we report a strategy enabling transient kinase activation in living cells. Using two protein-engineering approaches, we achieve independent control of kinase activation and inactivation. We show successful regulation of tyrosine kinase c-Src (Src) and Ser/Thr kinase p38α (p38), demonstrating broad applicability of the method. By activating Src for finite periods of time, we reveal how the duration of kinase activation affects secondary morphological changes that follow transient Src activation. This approach highlights distinct roles for sequential Src-Rac1- and Src-PI3K-signaling pathways at different stages during transient Src activation. Finally, we demonstrate that this method enables transient activation of Src and p38 in a specific signaling complex, providing a tool for targeted regulation of individual signaling pathways.
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