Detail of fig5a_control_3
Project
Title
Time-lapse FRET image of Rap1 activity in dissociated hippocampal neurons treated with the CaMKII inhibitor inactive analogue.
Description
NA
Release, Updated
2018-11-14
License
CC BY
Kind
Image data
based on Experiment
File Formats
Data size
6.8 MB
Protein names
Rap1
Datatype
spine dynamics
Molecular Function (MF)
Biological Process (BP)
spine apparatus formation
(
GO:1905355
)
Cellular Component (CC)
spine synapse
(
GO:0106033
)
neuron spine
(
GO:0044309
)
Biological Imaging Method
XYZ Scale
XY: 0.0932 micrometer/pixel, Z: 0.400 micrometer/slice
T scale
1800 second for each time interval
Image Acquisition
Experiment type
TimeLapse
Microscope type
ConfocalMicroscope
Acquisition mode
LaserScanningConfocalMicroscopy
Contrast method
Fluorescence
Microscope model
Olympus FluoView FV300
Detector model
-
Objective model
PlanApo X60 1.10 Oil LSM (Olympus)
Filter set
-
Summary of Methods
See details in Koeberle et al. (2017) Sci Rep, 7(1): 13409.
Related paper(s)
Solveigh Cornelia Koeberle, Shinji Tanaka, Toshihiko Kuriu, Hirohide Iwasaki, Andreas Koeberle, Alexander Schulz, Dario-Lucas Helbing, Yoko Yamagata, Helen Morrison, Shigeo Okabe (2017) Developmental stage-dependent regulation of spine formation by calcium-calmodulin-dependent protein kinase IIalpha and Rap1., Scientific reports, Volume 7, Number 1, pp. 13409
Published in 2017 Oct 17 (Electronic publication in Oct. 17, 2017, midnight )
- doi: 10.1038/s41598-017-13728-y
-
pmid: 29042611
(Abstract) The roles of calcium-calmodulin-dependent protein kinase II-alpha (CaMKIIalpha) in the expression of long-term synaptic plasticity in the adult brain have been extensively studied. However, how increased CaMKIIalpha activity controls the maturation of neuronal circuits remains incompletely understood. Herein, we show that pyramidal neurons without CaMKIIalpha activity upregulate the rate of spine addition, resulting in elevated spine density. Genetic elimination of CaMKIIalpha activity specifically eliminated the observed maturation-dependent suppression of spine formation. Enhanced spine formation was associated with the stabilization of actin in the spine and could be reversed by increasing the activity of the small GTPase Rap1. CaMKIIalpha activity was critical in the phosphorylation of synaptic Ras GTPase-activating protein (synGAP), the dispersion of synGAP from postsynaptic sites, and the activation of postsynaptic Rap1. CaMKIIalpha is already known to be essential in learning and memory, but our findings suggest that CaMKIIalpha plays an important activity-dependent role in restricting spine density during postnatal development.(MeSH Terms)
- Animals
- Biomarkers
- Calcium/metabolism
- Calcium-Calmodulin-Dependent Protein Kinase Type 2/genetics[major]
- Calcium-Calmodulin-Dependent Protein Kinase Type 2/metabolism
- Cell Differentiation/genetics[major]
- Dendritic Spines/metabolism[major]
- Fluorescent Antibody Technique
- Hippocampus
- Mice
- Models, Biological
- Neuronal Plasticity
- Neurons/cytology[major]
- Neurons/metabolism[major]
- Phosphorylation
- Protein Binding
- Pyramidal Cells/cytology
- Pyramidal Cells/metabolism
- rap1 GTP-Binding Proteins/genetics[major]
- rap1 GTP-Binding Proteins/metabolism
Contact
Shigeo Okabe
, University of Tokyo
, Department of Cellular Neurobiology, Graduate School of Medicine
Contributors
Solveigh Cornelia Koeberle, Shinji Tanaka, Toshihiko Kuriu, Hirohide Iwasaki, Andreas Koeberle, Alexander Schulz, Dario-Lucas Helbing, Yoko Yamagata, Helen Morrison, Shigeo Okabe
OMERO Dataset
OMERO Project
Source