SSBD:database

Key Organism Strain Cell Line Gene Symbol Protein name Protein tag Reporter Project ID Dataset ID Title Description Data Type Gene Ontology Biological Imaging Methods Method Summary Paper Information Medical Subject Headlines Person

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459-Abe-EGFRdynamics

https://ssbd.riken.jp/database/459-Abe-EGFRdynamics/

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ssbd-repos-000459

https://ssbd.riken.jp/repository/459/

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TIRF imaging of EGFR and PIP2 on Hela cells

Anionic lipid molecules, including phosphatidylinositol-4,5-bisphosphate (PI(4,5)P_{2}), are implicated in the regulation of epidermal growth factor receptor (EGFR). However, the role of the spatiotemporal dynamics of PI(4,5)P_{2} in the regulation of EGFR activity in living cells is not fully understood, as it is difficult to visualize the local lipid domains around EGFR. Here, we visualized both EGFR and PI(4,5)P_{2} nanodomains in the plasma membrane of HeLa cells using super-resolution single-molecule microscopy. The EGFR and PI(4,5)P_{2} nanodomains aggregated before stimulation with epidermal growth factor (EGF) through transient visits of EGFR to the PI(4,5)P_{2} nanodomains. The degree of coaggregation decreased after EGF stimulation and depended on phospholipase Cgamma, the EGFR effector hydrolyzing PI(4,5)P_{2}. Artificial reduction in the PI(4,5)P_{2} content of the plasma membrane reduced both the dimerization and autophosphorylation of EGFR after stimulation with EGF. Inhibition of PI(4,5)P_{2} hydrolysis after EGF stimulation decreased phosphorylation of EGFR-Thr654. Thus, EGFR kinase activity and the density of PI(4,5)P_{2} around EGFR molecules were found to be mutually regulated.

2026-06-09

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CC BY 4.0

Image data based on Experiment

4 ( Image datasets: 4, Quantitative data datasets: 0 )

400.1 MB ( Image datasets: 400.1 MB, Quantitative data datasets: 0 bytes )

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Homo sapiens

HeLa cell

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phosphatidylinositol-4, 5-bisphosphate binding, epidermal growth factor receptor activity

response to epidermal growth factor regulation of epidermal growth factor receptor signaling pathway, regulation of epidermal growth factor receptor signaling pathway

plasma membrane

evanescent wave microscopy

30 milliseconds

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Mitsuhiro Abe, Masataka Yanagawa, Michio Hiroshima, Toshihide Kobayashi, Yasushi Sako (2024) Bilateral regulation of EGFR activity and local PI(4,5)P(2) dynamics in mammalian cells observed with superresolution microscopy., eLife, Volume 13

Published in 2024 Nov 8 (Electronic publication in Nov. 8, 2024, midnight )

• doi: 10.7554/eLife.101652
• pmid: 39513999
  

(Abstract) Anionic lipid molecules, including phosphatidylinositol-4,5-bisphosphate (PI(4,5)P(2)), are implicated in the regulation of epidermal growth factor receptor (EGFR). However, the role of the spatiotemporal dynamics of PI(4,5)P(2) in the regulation of EGFR activity in living cells is not fully understood, as it is difficult to visualize the local lipid domains around EGFR. Here, we visualized both EGFR and PI(4,5)P(2) nanodomains in the plasma membrane of HeLa cells using super-resolution single-molecule microscopy. The EGFR and PI(4,5)P(2) nanodomains aggregated before stimulation with epidermal growth factor (EGF) through transient visits of EGFR to the PI(4,5)P(2) nanodomains. The degree of coaggregation decreased after EGF stimulation and depended on phospholipase Cgamma, the EGFR effector hydrolyzing PI(4,5)P(2). Artificial reduction in the PI(4,5)P(2) content of the plasma membrane reduced both the dimerization and autophosphorylation of EGFR after stimulation with EGF. Inhibition of PI(4,5)P(2) hydrolysis after EGF stimulation decreased phosphorylation of EGFR-Thr654. Thus, EGFR kinase activity and the density of PI(4,5)P(2) around EGFR molecules were found to be mutually regulated.

(MeSH Terms)

• ErbB Receptors/metabolism[major]
• Humans
• Phosphatidylinositol 4,5-Diphosphate/metabolism[major]
• HeLa Cells
• Cell Membrane/metabolism[major]
• Epidermal Growth Factor/metabolism[major]
• Epidermal Growth Factor/pharmacology[major]
• Phosphorylation
• Phospholipase C gamma/metabolism
• Single Molecule Imaging/methods
• Microscopy/methods

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Yasushi Sako , RIKEN , Cluster for Pioneering Research , Cluster for Pioneering Research

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