ArticleMolecular biology of the cell2008
Rapid turnover rate of phosphoinositides at the front of migrating MDCK cells.
Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 71 citations in OpenAlex.
- Front-biased activation of the Ras-Rab5-Rac1 loop coordinates collective cell migration.Journal of cell science · 2025Article
- Probing spatiotemporally organized GPCR signaling using genetically encoded molecular tools.Experimental & molecular medicine · 2025Review
- Sensitive fluorescent biosensor reveals differential subcellular regulation of PKC.Nature chemical biology · 2025Article
- Molecular Spies in Action: Genetically Encoded Fluorescent Biosensors Light up Cellular Signals.Chemical reviews · 2024Review
- Probing and imaging phospholipid dynamics in live cells.Life metabolism · 2024Review
- ORP9-PH domain-based fluorescent reporters for visualizing phosphatidylinositol 4-phosphate dynamics in living cells.RSC chemical biology · 2024Article
- Sensitive Fluorescent Biosensor Reveals Differential Subcellular Regulation of PKC.bioRxiv : the preprint server for biology · 2024Article
- Regulation of Cell Adhesion and Migration via Microtubule Cytoskeleton Organization, Cell Polarity, and Phosphoinositide Signaling.Biomolecules · 2023Review
- Monitoring Phosphoinositide Fluxes and Effectors During Leukocyte Chemotaxis and Phagocytosis.Frontiers in cell and developmental biology · 2021Review
- Fluorescent Biosensors for Multiplexed Imaging of Phosphoinositide Dynamics.ACS chemical biology · 2020Article
- Automated Fluorescence Lifetime Imaging High-Content Analysis of Förster Resonance Energy Transfer between Endogenously Labeled Kinetochore Proteins in Live Budding Yeast Cells.SLAS technology · 2019Article
- Genetically Encoded Fluorescent Biosensors Illuminate the Spatiotemporal Regulation of Signaling Networks.Chemical reviews · 2018Review
- Active K-RAS induces the coherent rotation of epithelial cells: A model for collective cell invasion in vitro.Cancer science · 2018Article
- Role of green fluorescent proteins and their variants in development of FRET-based sensors.Journal of biosciences · 2018Review
- A Mathematical Model of the Phosphoinositide Pathway.Scientific reports · 2018Article
- Quantifying lipid changes in various membrane compartments using lipid binding protein domains.Cell calcium · 2017Review
- Trifunctional lipid probes for comprehensive studies of single lipid species in living cells.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Open Source High Content Analysis Utilizing Automated Fluorescence Lifetime Imaging Microscopy.Journal of visualized experiments : JoVE · 2017Article
- Comparative lipid analysis in the normal and cancerous organoids of MDCK cells.Journal of biochemistry · 2016Article
- Allosteric substrate switching in a voltage-sensing lipid phosphatase.Nature chemical biology · 2016Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phosphoinositides (PtdInss) play key roles in cell polarization and motility. With a series of biosensors based on Förster resonance energy transfer, we examined the distribution and metabolism of PtdInss and diacylglycerol (DAG) in stochastically migrating Madin-Darby canine kidney (MDCK) cells. The concentrations of phosphatidylinositol (4,5)-bisphosphate, phosphatidylinositol (3,4,5)-trisphosphate (PIP(3)), phosphatidylinositol (3,4)-bisphosphate, and DAG were higher at the plasma membrane in the front of the cell than at the plasma membrane of the rear of the cell. The difference in the concentrations of PtdInss was estimated to be less than twofold between the front and rear of the migrating MDCK cells. To decode the spatial activities of PtdIns metabolic enzymes from the obtained concentration maps of PtdInss, we developed a one-dimensional reaction diffusion model of PtdIns metabolism. In this model, the activities of phosphatidylinositol monophosphate 5-kinase, phosphatidylinositol 3-kinase, phospholipase C, and PIP(3) 5-phosphatases were higher at the plasma membrane of the front than at the plasma membrane of the rear of the cell. This result suggests that, although the difference in the steady-state level of PtdInss is less than twofold, PtdInss were more rapidly turned over at the front than the rear of the migrating MDCK cells.
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