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Cited by 761Protein Kinase Regulation and GTPase SignalingCellular transport and secretionPI3K/AKT/mTOR signaling in cancer

Receptor-induced transient reduction in plasma membrane PtdIns(4,5)P2 concentration monitored in living cells

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Stauffer, Thomas P., Ahn, Seungkril, Meyer, Tobias·1998·Current Biology
DOI 10.1016/s0960-9822(98)70135-6
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Abstract

Although phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) is a well-characterized precursor for the second messengers inositol 1,4,5-trisphosphate, diacylglycerol [1] and phosphatidylinositol 3,4,5-trisphosphate [2], it also interacts with the actin-binding proteins profilin and gelsolin [3], as well as with many signaling molecules that contain pleckstrin homology (PH) domains [4]. It is conceivable that stimuli received by receptors in the plasma membrane could be sufficiently strong to decrease the PtdIns(4,5)P2 concentration; this decrease could alter the structure of the cortical cytoskeleton and modulate the activity of signaling molecules that have PH domains. Here, we tested this hypothesis by using an in vivo fluorescent indicator for PtdIns(4,5)P2, by tagging the PH domain of phospholipase C delta 1 (PLC-delta 1) with the green fluorescent protein (GFP-PH). When expressed in cells, GFP-PH was found to be enriched at the plasma membrane. Binding studies in vitro and mutant analysis suggested that GFP-PH bound PtdIns(4,5)P2 selectively over other phosphatidylinositol lipids. Strikingly, receptor stimulation induced a transient dissociation of GFP-PH from the plasma membrane, suggesting that the concentration of PtdIns(4,5)P2 in the plasma membrane was effectively lowered. This transient dissociation was blocked by the PLC inhibitor U73122 but was not affected by the phosphoinositide (PI) 3-kinase inhibitor wortmannin, suggesting that it is mostly mediated by PLC…

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  • PLCδ-PH-GFP associated predominantly with the plasmalemma of RAW cells, with little binding to organellar membranes.

    “As reported for other cell types (Stauffer et al. 1998; Varnai and Balla 1998), PLCδ-PH-GFP associated predominantly with the plasmalemma of RAW cells, with little binding to organellar membranes (Fig. 1 A).”

    From Localized Biphasic Changes in Phosphatidylinositol-4,5-Bisphosphate at Sites of Phagocytosis (2000) · cites this paper as Stauffer et al. 1998

  • Chimeric constructs of GFP with defined lipid-binding domains of proteins can monitor the distribution of phospholipids and their metabolites in transfected cells.

    “Recent and elegant reports have introduced the use of chimeric constructs of GFP with defined lipid-binding domains of proteins to monitor the distribution of phospholipids and their metabolites in transfected cells (Oancea and Meyer 1998; Oancea et al. 1998; Stauffer et al. 1998; Varnai et al. 1999; Czech 2000).”

    From Localized Biphasic Changes in Phosphatidylinositol-4,5-Bisphosphate at Sites of Phagocytosis (2000) · cites this paper as Stauffer et al. 1998

  • PLCδ-PH-GFP and C1δ-GFP probes had been validated in other systems and their suitability was confirmed in RAW macrophages.

    “These probes had been validated in other systems (Oancea et al. 1998; Stauffer et al. 1998; Varnai and Balla 1998) and their suitability was confirmed in RAW macrophages.”

    From Localized Biphasic Changes in Phosphatidylinositol-4,5-Bisphosphate at Sites of Phagocytosis (2000) · cites this paper as Stauffer et al. 1998

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Authors
Stauffer, T. P., Ahn, S., & Meyer, T.
Affiliations
  • Duke Medical Center (US)
  • Duke University (US)
ORCID
Venue
Current Biology
Publisher
Elsevier BV
Published
1998-03
Volume
8
Issue
6
Pages
343-346
ISSN
0960-9822 (ISSN-L)
DOI
10.1016/s0960-9822(98)70135-6
OpenAlex
W1983769291
Cited by
761
References
0
Citations by year
2026: 14 · 2025: 30 · 2024: 25 · 2023: 23 · 2022: 24 · 2021: 31 · 2020: 22 · 2019: 24 · 2018: 36 · 2017: 18 · 2016: 16 · 2015: 25 · 2014: 29 · 2013: 24 · 2012: 40
FWCI
10.12
Type
journal article
Language
en
Open access
Licence
Locations
  • Current Biology (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Procter and Gamble (SRA 1617)
  • Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (823A-050457)
  • National Institutes of Health (GM-51457)
  • David and Lucile Packard Foundation
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
Keywords
phosphatidylinositol 4,5-bisphosphate, phospholipase C delta 1, pleckstrin homology domain, plasma membrane, receptor signaling, second messengers, U73122, wortmannin, phosphatidylinositol 3-kinase, phospholipid binding
MeSH terms
Androstadienes, Animals, Cells, Cultured, Electrophoresis, Polyacrylamide Gel, Enzyme Inhibitors, Fluoroscopy, Membrane Proteins, Phosphodiesterase Inhibitors, Pyrrolidinones, Transfection, Microscopy, Video, Phosphatidylinositol 4,5-Diphosphate, Rats

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