Detail of movieS3



Project
Title
Time-lapse images of chemotaxis of gip1 knockout dictyostelium cells expressing Gip1(full)-GFPF toward 100uM cAMP
Description
NA
Release, Updated
2018-11-14
License
CC BY
Kind
Image data based on Experiment
File Formats
Data size
218.9 MB

Organism
D. discoideum AX2 ( NCBI:txid366501 )
Strain(s)
AX2
Cell Line
-
Gene symbols
gip1
Protein names
Gip1
Protein tags
GFP

Datatype
dynamic of eukaryotic chemotaxis
Molecular Function (MF)
Biological Process (BP)
chemotaxis ( GO:0006935 )
Cellular Component (CC)
cAMP dependent protein kinase regulator activity ( GO:0008603 )
Biological Imaging Method
XYZ Scale
XY: 2.5 micrometer/pixel, Z: NA
T scale
10 second for each time interval

Image Acquisition
Experiment type
TimeLapse
Microscope type
ConfocalMicroscope
Acquisition mode
Other
Contrast method
Brightfield
Microscope model
Olympus FV2000
Detector model
-
Objective model
-
Filter set
-

Summary of Methods
See details in Kamimura et al. (2016) Proc Natl Acad Sci U S A, 113(16): 4356-4361.
Related paper(s)

Yoichiro Kamimura, Yukihiro Miyanaga, Masahiro Ueda (2016) Heterotrimeric G-protein shuttling via Gip1 extends the dynamic range of eukaryotic chemotaxis., Proceedings of the National Academy of Sciences of the United States of America, Volume 113, Number 16, pp. 4356-61

Published in 2016 Apr 19 (Electronic publication in April 4, 2016, midnight )

(Abstract) Chemotactic eukaryote cells can sense chemical gradients over a wide range of concentrations via heterotrimeric G-protein signaling; however, the underlying wide-range sensing mechanisms are only partially understood. Here we report that a novel regulator of G proteins, G protein-interacting protein 1 (Gip1), is essential for extending the chemotactic range ofDictyosteliumcells. Genetic disruption of Gip1 caused severe defects in gradient sensing and directed cell migration at high but not low concentrations of chemoattractant. Also, Gip1 was found to bind and sequester G proteins in cytosolic pools. Receptor activation induced G-protein translocation to the plasma membrane from the cytosol in a Gip1-dependent manner, causing a biased redistribution of G protein on the membrane along a chemoattractant gradient. These findings suggest that Gip1 regulates G-protein shuttling between the cytosol and the membrane to ensure the availability and biased redistribution of G protein on the membrane for receptor-mediated chemotactic signaling. This mechanism offers an explanation for the wide-range sensing seen in eukaryotic chemotaxis.
(MeSH Terms)

Contact
Masahiro Ueda , RIKEN , Center for Biosystems Dynamics Research , Laboratory for Cell Signaling Dynamics
Contributors
Yoichiro Kamimura, Yukihiro Miyanagaa, Masahiro Ueda

OMERO Dataset
OMERO Project
Source