CaMKII‐mediated displacement of AIDA‐1 out of the postsynaptic density core

Ankyrin repeat and sterile alpha motif domain‐containing protein 1B (ANKS1B, also known as AIDA‐1) is a major component of the postsynaptic density (PSD) in excitatory neurons where it concentrates at the electron‐dense core under basal conditions and moves out during activity. This study investigat...

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Bibliographic Details
Published in:FEBS letters 2016-09, Vol.590 (17), p.2934-2939
Main Authors: Dosemeci, Ayse, Toy, Dana, Burch, Amelia, Bayer, K. Ulrich, Tao‐Cheng, Jung‐Hwa
Format: Article
Language:English
Subjects:
AIDA‐1
Animals
Calcium-Calmodulin-Dependent Protein Kinase Type 2 - antagonists & inhibitors
Calcium-Calmodulin-Dependent Protein Kinase Type 2 - genetics
Calcium-Calmodulin-Dependent Protein Kinase Type 2 - metabolism
CaMKII
Carrier Proteins - genetics
Carrier Proteins - metabolism
Hippocampus - metabolism
Hippocampus - ultrastructure
Humans
Microscopy, Immunoelectron
Neurons - metabolism
Neurons - ultrastructure
Peptides - pharmacology
Phosphorylation
Post-Synaptic Density - metabolism
Post-Synaptic Density - ultrastructure
postsynaptic density
Rats
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Summary:Ankyrin repeat and sterile alpha motif domain‐containing protein 1B (ANKS1B, also known as AIDA‐1) is a major component of the postsynaptic density (PSD) in excitatory neurons where it concentrates at the electron‐dense core under basal conditions and moves out during activity. This study investigates the molecular mechanism underlying activity‐induced displacement of AIDA‐1. Experiments with PSD fractions from brain indicate phosphorylation of AIDA‐1 upon activation of endogenous CaMKII. Immuno‐electron microscopy studies show that treatment of hippocampal neurons with NMDA results in an ~ 30 nm shift in the median distance of the AIDA‐1 label from the postsynaptic membrane, an effect that is blocked by the CaMKII inhibitor tatCN21. CaMKII‐mediated redistribution of AIDA‐1 is similar to that observed for SynGAP. CaMKII‐mediated removal of two abundant PSD‐95‐binding proteins from the PSD core during activity is expected to initiate a molecular reorganization at the PSD.
ISSN:0014-5793
1873-3468
DOI:10.1002/1873-3468.12334