Detail of Fig1C



Project
Title
Microscopy images of a D. discoideum cell expressing PTEN-TMR and PH_Akt/PKB-EGFP
Description
NA
Release, Updated
2017-10-03,
2018-11-15
License
CC BY
Kind
Image data based on Experiment
File Formats
Data size
361.6 MB

Organism
D. discoideum ( NCBI:txid44689 )
Strain(s)
-
Cell Line
-
Gene symbols
Akt
Protein names
PTEN
Protein tags
TMR, EGFP

Datatype
cell dynamics
Molecular Function (MF)
Biological Process (BP)
cellular protein localization ( GO:0034613 )
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
-

Summary of Methods
See details in Shibata et al. (2012) J. Cell Sci., 125: 5138-5150.
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

OMERO Dataset
OMERO Project
Source