Summary of ssbd-repos-000211

SSBD:database
URL

Name
ssbd-repos-000211 (211-Hiroshima-EGFRTracking)
URL
DOI
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Title
Single-molecule imaging and BDML file for quantitative information about trajectories of EGFR dynamics and activities in living CHO-K1 cells.
Description
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Submited Date
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Release Date
2022-03-31
Updated Date
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License
Funding information
-
File formats
Data size
31.3 GB

Organism
Cricetulus griseus
Strain
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Cell Line
CHO-K1
Genes
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Proteins
EGFR, GRB2

GO Molecular Function (MF)
epidermal growth factor receptor binding, epidermal growth factor-activated receptor activity
GO Biological Process (BP)
epidermal growth factor receptor signaling pathway
GO Cellular Component (CC)
NA, Grb2-EGFR complex
Study Type
Epidermal Growth Factor/metabolism, Fluorescent Antibody Technique, ErbB Receptors/metabolism, Cytoplasm/metabolism, Cricetulus, Cluster Analysis, GRB2 Adaptor Protein/metabolism, Animals, Epidermal Growth Factor, GRB2 Adaptor Protein, Signal Transduction, Single Molecule Imaging/methods, Cytoplasm, CHO Cells, ErbB Receptors, ErbB Receptors/chemistry, Single Molecule Imaging, Spatio-Temporal Analysis
Imaging Methods
time lapse microscopy, evanescent wave microscopy

Method Summary
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Related paper(s)

Michio Hiroshima, Chan-Gi Pack, Kazunari Kaizu, Koichi Takahashi, Masahiro Ueda, Yasushi Sako (2018) Transient Acceleration of Epidermal Growth Factor Receptor Dynamics Produces Higher-Order Signaling Clusters., Journal of molecular biology, Volume 430, Number 9, pp. 1386-1401

Published in 2018 Apr 27 (Electronic publication in March 2, 2018, midnight )

(Abstract) Cell signaling depends on spatiotemporally regulated molecular interactions. Although the movements of signaling proteins have been analyzed with various technologies, how spatial dynamics influence the molecular interactions that transduce signals is unclear. Here, we developed a single-molecule method to analyze the spatiotemporal coupling between motility, clustering, and signaling. The analysis was performed with the epidermal growth factor receptor (EGFR), which triggers signaling through its dimerization and phosphorylation after association with EGF. Our results show that the few EGFRs isolated in membrane subdomains were released by an EGF-dependent increase in their diffusion area, facilitating molecular associations and producing immobile clusters. Using a two-color single-molecule analysis, we found that the EGF-induced state transition alters the properties of the immobile clusters, allowing them to interact for extended periods with the cytoplasmic protein, GRB2. Our study reveals a novel correlation between this molecular interaction and its mesoscale dynamics, providing the initial signaling node.
(MeSH Terms)

Contact(s)
Yasushi Sako
Organization(s)
RIKEN , Cellular Informatics Laboratory
Image Data Contributors
Quantitative Data Contributors

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