Summary of 21-Yasui-MolDynPTEN

SSBD:database
SSBD:database URL
Title
-
Description
-
Relase date
2017-10-03
Updated date
2018-11-15
License
CC BY
Kind
Image data based on Experiment
Number of Datasets
13 ( Image datasets: 13, Quantitative data datasets: 0 )
Size of Datasets
1.2 GB ( Image datasets: 1.2 GB, Quantitative data datasets: 0 bytes )

Organism(s)
D. discoideum
Gene symbol(s)
NA
Protein name(s)
PTEN, PTEN4

Datatype
single molecule dynamics
Molecular Function (MF)
Biological Process (BP)
chemotaxis
Cellular Component (CC)
-
Biological Imaging Method
-
XYZ Scale
XY: 0.033 micrometer/pixel, Z: NA
T scale
33 millisecond for each time interval

Image Acquisition
Experiment type
TimeLapse
Microscope type
TotalInternalReflectionFluorescenceMicroscope
Acquisition mode
TIRF
Contrast method
Fluorescence
Microscope model
OLYMPUS IX-70
Detector model
Andor iXon3
Objective model
OLYMPUS PlanApo 60x 1.45NA Oil TIRFM
Filter set
Dichroic: Omega Optical XF2032, Emission: Semrock FF01-575/25

Related paper(s)

Masato Yasui, Satomi Matsuoka, Masahiro Ueda (2014) PTEN hopping on the cell membrane is regulated via a positively-charged C2 domain., PLoS computational biology, Volume 10, Number 9, pp. e1003817

Published in 2014 Sep (Electronic publication in Sept. 11, 2014, midnight )

(Abstract) PTEN, a tumor suppressor that is frequently mutated in a wide spectrum of cancers, exerts PI(3,4,5)P3 phosphatase activities that are regulated by its dynamic shuttling between the membrane and cytoplasm. Direct observation of PTEN in the interfacial environment can offer quantitative information about the shuttling dynamics, but remains elusive. Here we show that positively charged residues located in the calpha2 helix of the C2 domain are necessary for the membrane localization of PTEN via stable electrostatic interactions in Dictyostelium discoideum. Single-molecule imaging analyses revealed that PTEN molecules moved distances much larger than expected had they been caused by lateral diffusion, a phenomenon we call "hopping." Our novel single-particle tracking analysis method found that the calpha2 helix aids in regulating the hopping and stable-binding states. The dynamically established membrane localization of PTEN was revealed to be essential for developmental processes and clarified a fundamental regulation mechanism of the protein quantity and activity on the plasma membrane.
(MeSH Terms)

Contact
Satomi Matsuoka , Osaka University , Graduate School of Frontier Biosciences , Laboratories for Nanobiology
Contributors
Masato Yasui, Satomi Matsuoka, Masahiro Ueda


Dataset List of 21-Yasui-MolDynPTEN

#
Dataset ID
Kind
Size
4D View
SSBD:OMERO
Download BDML
Download Images
# 798
Datast ID Fig2A_pten
Dataset Kind Image data
Dataset Size 150.0 MB
4D view
SSBD:OMERO
Download BDML
Download Image data

# 799
Datast ID Fig2A_pten1
Dataset Kind Image data
Dataset Size 150.0 MB
4D view
SSBD:OMERO
Download BDML
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# 800
Datast ID Fig2A_pten2
Dataset Kind Image data
Dataset Size 150.0 MB
4D view
SSBD:OMERO
Download BDML
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# 801
Datast ID Fig2A_pten3
Dataset Kind Image data
Dataset Size 150.0 MB
4D view
SSBD:OMERO
Download BDML
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# 802
Datast ID Fig2A_pten4
Dataset Kind Image data
Dataset Size 150.0 MB
4D view
SSBD:OMERO
Download BDML
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# 803
Datast ID Fig2A_pten5
Dataset Kind Image data
Dataset Size 150.0 MB
4D view
SSBD:OMERO
Download BDML
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# 804
Datast ID Fig2A_pten6
Dataset Kind Image data
Dataset Size 150.0 MB
4D view
SSBD:OMERO
Download BDML
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# 805
Datast ID Fig2A_pten7
Dataset Kind Image data
Dataset Size 150.0 MB
4D view
SSBD:OMERO
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# 806
Datast ID Fig3A_pten
Dataset Kind Image data
Dataset Size 9.4 KB
4D view
SSBD:OMERO
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# 807
Datast ID Fig3C_pten
Dataset Kind Image data
Dataset Size 9.4 KB
4D view
SSBD:OMERO
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# 808
Datast ID Fig3E_pten
Dataset Kind Image data
Dataset Size 9.4 KB
4D view
SSBD:OMERO
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# 809
Datast ID Fig3G_pten
Dataset Kind Image data
Dataset Size 58.8 KB
4D view
SSBD:OMERO
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# 810
Datast ID Fig5D_pten
Dataset Kind Image data
Dataset Size 150.0 KB
4D view
SSBD:OMERO
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