Summary of ssbd-repos-000194

SSBD:database
URL

Name
ssbd-repos-000194 (194-Obashi-SpineDyn)
URL
DOI
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Title
Microscopy images or BDML file for quantiative information about actin polymers mobility in mouse dendritic spines.
Description
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Submited Date
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Release Date
2022-03-31
Updated Date
-
License
Funding information
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File formats
Data size
9.4 MB

Organism
Mus musculus
Strain
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Cell Line
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Genes
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Proteins
ADF, Tiam1QK, cofilin

GO Molecular Function (MF)
NA, signaling molecule
GO Biological Process (BP)
actin polymerization, stimulation of synapse structural plasticity
GO Cellular Component (CC)
dendritic spine
Study Type
Dendritic Spines/ultrastructure, Biological Transport, Actin Cytoskeleton, 1/metabolism, Signal Transduction, Female, Actins/metabolism, Calcium-Calmodulin-Dependent Protein Kinase Type 2, Mice, Inbred ICR, Neuronal Plasticity, Dendritic Spines/metabolism, Male, T-Lymphoma Invasion and Metastasis-inducing Protein, Dendritic Spines, Calcium-Calmodulin-Dependent Protein Kinase Type 2/metabolism, Cultured, Animals, Actin Cytoskeleton/metabolism, Actins, Diffusion, Cells, T-Lymphoma Invasion and Metastasis-inducing Protein 1
Imaging Methods
time lapse microscopy, two-photon laser scanning microscopy, structured illumination microscopy

Method Summary
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Related paper(s)

Kazuki Obashi, Atsushi Matsuda, Yasuhiro Inoue, Shigeo Okabe (2019) Precise Temporal Regulation of Molecular Diffusion within Dendritic Spines by Actin Polymers during Structural Plasticity., Cell reports, Volume 27, Number 5, pp. 1503-1515.e8

Published in 2019 Apr 30

(Abstract) The biochemical transduction of excitatory synaptic signals occurs in the cytoplasm within dendritic spines. The associated reaction kinetics are shaped by the mobility of the signaling molecules; however, accurate monitoring of diffusional events within the femtoliter-sized spine structures has not yet been demonstrated. Here, we applied two-photon fluorescence correlation spectroscopy and raster image correlation spectroscopy to monitor protein dynamics within spines, revealing that F-actin restricts the mobility of proteins with a molecular mass of >100 kDa. This restriction is transiently removed during actin remodeling at the initial phase of spine structural plasticity. Photobleaching experiments combined with super-resolution imaging indicate that this increase in mobility facilitates molecular interactions, which may modulate the functions of key postsynaptic signaling molecules, such as Tiam1 and CaMKII. Thus, actin polymers in dendritic spines act as precise temporal regulators of molecular diffusion and modulate signal transduction during synaptic plasticity.
(MeSH Terms)

Contact(s)
Shigeo Okabe
Organization(s)
the University of Tokyo, Tokyo , Department of Cellular Neurobiology, Graduate School of Medicine
Image Data Contributors
Quantitative Data Contributors

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