Summary of 39-Shibata-MolDynPTEN

SSBD:database
SSBD:database URL
Title
-
Description
-
Relase date
2017-10-03
Updated date
2018-11-15
License
CC BY
Kind
Quantitative data, Image data based on Experiment
Number of Datasets
4 ( Image datasets: 2, Quantitative data datasets: 2 )
Size of Datasets
759.1 MB ( Image datasets: 723.2 MB, Quantitative data datasets: 35.8 MB )

Organism(s)
D. discoideum
Gene symbol(s)
Akt
Protein name(s)
PTEN
Protein tag(s)
EGFP, TMR

Datatype
cell dynamics
Molecular Function (MF)
Biological Process (BP)
cellular protein localization
Cellular Component (CC)
-
Biological Imaging Method
-
XYZ Scale
XY: 0.33 micrometer/pixel, Z: 0 micrometer/frame
T scale
5 second for each time interval

Image Acquisition
Experiment type
-
Microscope type
-
Acquisition mode
-
Contrast method
-
Microscope model
-
Detector model
-
Objective model
-
Filter set
-

Related paper(s)

Tatsuo Shibata, Masatoshi Nishikawa, Satomi Matsuoka, Masahiro Ueda (2012) Modeling the self-organized phosphatidylinositol lipid signaling system in chemotactic cells using quantitative image analysis., Journal of cell science, Volume 125, Number Pt 21, pp. 5138-50

Published in 2012 Nov 1 (Electronic publication in Aug. 16, 2012, midnight )

(Abstract) A key signaling event that is responsible for gradient sensing in eukaryotic cell chemotaxis is a phosphatidylinositol (PtdIns) lipid reaction system. The self-organization activity of this PtdIns lipid system induces an inherent polarity, even in the absence of an external chemoattractant gradient, by producing a localized PtdIns (3,4,5)-trisphosphate [PtdIns(3,4,5)P(3)]-enriched domain on the membrane. Experimentally, we found that such a domain could exhibit two types of behavior: (1) it could be persistent and travel on the membrane, or (2) be stochastic and transient. Taking advantage of the simultaneous visualization of PtdIns(3,4,5)P(3) and the enzyme phosphatase and tensin homolog (PTEN), for which PtdIns(3,4,5)P(3) is a substrate, we statistically demonstrated the inter-dependence of their spatiotemporal dynamics. On the basis of this statistical analysis, we developed a theoretical model for the self-organization of PtdIns lipid signaling that can accurately reproduce both persistent and transient domain formation; these types of formations can be explained by the oscillatory and excitability properties of the system, respectively.
(MeSH Terms)

Contact
Tatsuo Shibata , RIKEN , Quantitative Biology Center , Laboratories for Physical Biology
Contributors
Tatsuo Shibata, Masatoshi Nishikawa, Satomi Matsuoka, Masahiro Ueda


Dataset List of 39-Shibata-MolDynPTEN

#
Dataset ID
Kind
Size
4D View
SSBD:OMERO
Download BDML
Download Images
# 1017
Datast ID Fig1B
Dataset Kind Image data
Dataset Size 361.6 MB
4D view
SSBD:OMERO
Download BDML
Download Image data

# 1018
Datast ID Fig1B
Dataset Kind Quantitative data
Dataset Size 18.4 MB
4D view
SSBD:OMERO
Download BDML
Download Image data

# 1019
Datast ID Fig1C
Dataset Kind Image data
Dataset Size 361.6 MB
4D view
SSBD:OMERO
Download BDML
Download Image data

# 1020
Datast ID Fig1C
Dataset Kind Quantitative data
Dataset Size 17.5 MB
4D view
SSBD:OMERO
Download BDML
Download Image data