Activity-driven postsynaptic translocation of CaMKII

Michelle A Merrill; Yucui Chen; Stefan Strack; Johannes W Hell

doi:10.1016/j.tips.2005.10.003

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Activity-driven postsynaptic translocation of CaMKII

Journal article

Peer reviewed

Activity-driven postsynaptic translocation of CaMKII

Michelle A Merrill, Yucui Chen, Stefan Strack and Johannes W Hell

Trends in pharmacological sciences (Regular ed.), Vol.26(12), pp.645-653

12/2005

DOI: 10.1016/j.tips.2005.10.003

PMID: 16253351

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Abstract

Ca2+ influx through the NMDA receptor and subsequent activation of Ca2+/calmodulin-dependent protein kinase II (CaMKII) are crucial for learning and one of its physiological correlates, long-term potentiation (LTP). Ca2+/calmodulin promotes CaMKII binding to several postsynaptic proteins, including the NMDA receptor. These interactions strategically place CaMKII at locations where Ca2+ influx through the NMDA receptor is highest for further activation of CaMKII and for phosphorylation of nearby AMPA receptors and of other proteins that are important for LTP. Ca2+-dependent postsynaptic CaMKII clustering is of specific interest because LTP is synapse specific: only synapses that experience LTP-inducing high-frequency activity exhibit LTP. Ca2+-driven protein binding ensures that CaMKII accumulates only at those synapses undergoing LTP. This selectivity is economical and could contribute to the synapse specificity of LTP because downstream effects of CaMKII will occur mainly at synapses that accumulate CaMKII. In this article, we provide an overview of recent progress in postsynaptic CaMKII anchoring and discuss its implication in synaptic plasticity and the etiology and potential treatments of neurological diseases.

Nervous System Diseases - enzymology

Synaptic Transmission - physiology

Humans

Receptors, N-Methyl-D-Aspartate - metabolism

Protein Transport

Animals

Neuronal Plasticity - physiology

Long-Term Potentiation - physiology

Protein Binding

Nervous System Diseases - metabolism

Nervous System Diseases - physiopathology

Calcium-Calmodulin-Dependent Protein Kinase Type 2

Calcium-Calmodulin-Dependent Protein Kinases - metabolism

Details

Title: Subtitle: Activity-driven postsynaptic translocation of CaMKII
Creators: Michelle A Merrill - Department of Pharmacology, University of Iowa, Iowa City, IA 52242-1109, USA
Yucui Chen
Stefan Strack
Johannes W Hell
Resource Type: Journal article
Publication Details: Trends in pharmacological sciences (Regular ed.), Vol.26(12), pp.645-653
Publisher: England
DOI: 10.1016/j.tips.2005.10.003
PMID: 16253351
ISSN: 0165-6147
eISSN: 1873-3735
Language: English
Date published: 12/2005
Academic Unit: Pathology; Iowa Neuroscience Institute; Neuroscience and Pharmacology
Record Identifier: 9984040575302771

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