Phospholipase C–mediated hydrolysis of PIP2 releases ERM proteins from lymphocyte membrane
Open accessAbstract
Mechanisms controlling the disassembly of ezrin/radixin/moesin (ERM) proteins, which link the cytoskeleton to the plasma membrane, are incompletely understood. In lymphocytes, chemokine (e.g., SDF-1) stimulation inactivates ERM proteins, causing their release from the plasma membrane and dephosphorylation. SDF-1–mediated inactivation of ERM proteins is blocked by phospholipase C (PLC) inhibitors. Conversely, reduction of phosphatidylinositol 4,5-bisphosphate (PIP2) levels by activation of PLC, expression of active PLC mutants, or acute targeting of phosphoinositide 5-phosphatase to the plasma membrane promotes release and dephosphorylation of moesin and ezrin. Although expression of phosphomimetic moesin (T558D) or ezrin (T567D) mutants enhances membrane association, activation of PLC still relocalizes them to the cytosol. Similarly, in vitro binding of ERM proteins to the cytoplasmic tail of CD44 is also dependent on PIP2. These results demonstrate a new role of PLCs in rapid cytoskeletal remodeling and an additional key role of PIP2 in ERM protein biology, namely hydrolysis-mediated ERM inactivation.
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In lymphocytes, SDF-1 inactivates ERM proteins, causing their release from the plasma membrane following PLC activation.
“In lymphocytes, the chemokine, SDF-1 (stromal cell-derived factor 1 (also known as chemokine 12)), inactivates ERM proteins, causing their release from the plasma membrane following PLC activation [92].”
From Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane (2020) · cites this paper as [92]
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- Authors
- Hao, J.-J., Liu, Y., Kruhlak, M., Debell, K. E., Rellahan, B. L., & Shaw, S.
- Affiliations
- National Institutes of Health (US)
- United States Food and Drug Administration (US)
- Corresponding author
- Shaw, Stephen
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2009-02-09
- Volume
- 184
- Issue
- 3
- Pages
- 451-462
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2646552
- OpenAlex
- W2104477681
- Cited by
- 137
- References
- 50
- Citations by year
- 2026: 2 · 2025: 7 · 2024: 4 · 2023: 3 · 2022: 10 · 2021: 6 · 2020: 12 · 2019: 9 · 2018: 7 · 2017: 4 · 2016: 2 · 2015: 10 · 2014: 13 · 2013: 17 · 2012: 8
- FWCI
- 4.16
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- 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 Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- phospholipase C, phosphatidylinositol 4,5-bisphosphate, ERM proteins, ezrin, moesin, lymphocytes, CXCL12, chemokine signaling, membrane association, cytoskeletal remodeling, CD44, phosphoinositide 5-phosphatase, plasma membrane
- MeSH terms
- Ezrin, Phosphoinositide 5-Phosphatases, Animals, Cell Membrane, Cytoskeletal Proteins, Cytoskeleton, Enzyme Activation, Humans, Lymphocytes, Membrane Proteins, Microfilament Proteins, Type C Phospholipases, Phosphoric Monoester Hydrolases, Recombinant Fusion Proteins, Signal Transduction, Hyaluronan Receptors, Jurkat Cells, Phosphatidylinositol 4,5-Diphosphate, Chemokine CXCL12
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