Phosphatidylinositol 4,5-bisphosphate functions as a second messenger that regulates cytoskeleton-plasma membrane adhesion
Open accessAbstract
Binding interactions between the plasma membrane and the cytoskeleton define cell functions such as cell shape, formation of cell processes, cell movement, and endocytosis. Here we use optical tweezers tether force measurements and show that plasma membrane phosphatidylinositol 4,5-bisphosphate (PIP2) acts as a second messenger that regulates the adhesion energy between the cytoskeleton and the plasma membrane. Receptor stimuli that hydrolyze PIP2 lowered adhesion energy, a process that could be mimicked by expressing PH domains that sequester PIP2 or by targeting a 5'-PIP2-phosphatase to the plasma membrane to selectively lower plasma membrane PIP2 concentration. Our study suggests that plasma membrane PIP2 controls dynamic membrane functions and cell shape by locally increasing and decreasing the adhesion between the actin-based cortical cytoskeleton and the plasma membrane.
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PLCδ-PH-GFP can be used not only to monitor the distribution of 4,5-PIP2, but when expressed at sufficiently high levels, also to competitively inhibit other 4,5-PIP2-dependent processes.
“PLCδ-PH-GFP can be used not only to monitor the distribution of 4,5-PIP2, but when expressed at sufficiently high levels, also to competitively inhibit other 4,5-PIP2–dependent processes.”
From Localized Biphasic Changes in Phosphatidylinositol-4,5-Bisphosphate at Sites of Phagocytosis (2000) · cites this paper as Raucher et al. 2000
The yeast 4,5-PIP2-specific 5′-phosphatase INP54p reduces the content of 4,5-PIP2 in COS cells.
“This yeast phosphatase has been shown to reduce the content of 4,5-PIP2 in COS cells (Raucher et al. 2000).”
From Localized Biphasic Changes in Phosphatidylinositol-4,5-Bisphosphate at Sites of Phagocytosis (2000) · cites this paper as Raucher et al. 2000
PI(4,5)P2 is one of the main drivers of actin cytoskeleton remodelling; it interacts with several actin-binding proteins at the plasma membrane and regulates their activity through its levels.
“One of the main drivers for this process is PI(4,5)P2 [87]; it interacts with several actin-binding proteins at the plasma membrane, serving to regulate their activity through its levels (Figure 5) [14,88].”
From Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane (2020) · cites this paper as [87]
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References 31 · Cited by 675
- Authors
- Raucher, D., Stauffer, T., Chen, W., Shen, K., Guo, S., York, J. D., Sheetz, M. P., & Meyer, T.
- Affiliations
- Duke Medical Center (US)
- Corresponding author
- Meyer, Tobias
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2000-01
- Volume
- 100
- Issue
- 2
- Pages
- 221-228
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2091701502
- Cited by
- 675
- References
- 31
- Citations by year
- 2026: 5 · 2025: 12 · 2024: 7 · 2023: 9 · 2022: 15 · 2021: 21 · 2020: 29 · 2019: 18 · 2018: 22 · 2017: 22 · 2016: 19 · 2015: 21 · 2014: 35 · 2013: 30 · 2012: 27
- FWCI
- 18.02
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Cell (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Heart, Lung, and Blood Institute (R01HL055672, HL55672)
- National Institute of General Medical Sciences (GM 362277, GM-48113)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Keywords
- phosphatidylinositol 4,5-bisphosphate, second messengers, adhesion energy, PIP2 hydrolysis, pleckstrin homology domain, cell shape, optical tweezers
- MeSH terms
- Actins, Animals, Cell Membrane, Cytoskeleton, Energy Metabolism, Membrane Proteins, Multienzyme Complexes, Phosphoric Monoester Hydrolases, Polymers, Protein Binding, Stress, Mechanical, Second Messenger Systems, Signal Transduction, 3T3 Cells, Phosphatidylinositol 4,5-Diphosphate, Mice
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