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FEBS Lett. 2016 Sep;590(17):2934-9. doi: 10.1002/1873-3468.12334. Epub 2016 Aug 20.

CaMKII-mediated displacement of AIDA-1 out of the postsynaptic density core.

Author information

1
Laboratory of Neurobiology, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD, USA.
2
Department of Pharmacology, School of Medicine, University of Colorado Denver, Aurora, CO, USA.
3
EM Facility, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD, USA.

Abstract

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.

KEYWORDS:

AIDA-1; CaMKII; postsynaptic density

PMID:
27477489
PMCID:
PMC5014603
DOI:
10.1002/1873-3468.12334
[Indexed for MEDLINE]
Free PMC Article

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