Autophosphorylation-dependent targeting of calcium/ calmodulin-dependent protein kinase II by the NR2B subunit of the N-methyl- D-aspartate receptor

Stefan Strack; Roger J Colbran

doi:10.1074/jbc.273.33.20689

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Autophosphorylation-dependent targeting of calcium/ calmodulin-dependent protein kinase II by the NR2B subunit of the N-methyl- D-aspartate receptor

Journal article

Open access

Peer reviewed

Autophosphorylation-dependent targeting of calcium/ calmodulin-dependent protein kinase II by the NR2B subunit of the N-methyl- D-aspartate receptor

Stefan Strack and Roger J Colbran

The Journal of biological chemistry, Vol.273(33), pp.20689-20692

08/14/1998

DOI: 10.1074/jbc.273.33.20689

PMID: 9694809

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Abstract

Activation and Thr286 autophosphorylation of calcium/calmodulindependent kinase II (CaMKII) following Ca2+ influx via N-methyl-D-aspartate (NMDA)-type glutamate receptors is essential for hippocampal long term potentiation (LTP), a widely investigated cellular model of learning and memory. Here, we show that NR2B, but not NR2A or NR1, subunits of NMDA receptors are responsible for autophosphorylation-dependent targeting of CaMKII. CaMKII and NMDA receptors colocalize in neuronal dendritic spines, and a CaMKII.NMDA receptor complex can be isolated from brain extracts. Autophosphorylation induces direct high-affinity binding of CaMKII to a 50 amino acid domain in the NR2B cytoplasmic tail; little or no binding is observed to NR2A and NR1 cytoplasmic tails. Specific colocalization of CaMKII with NR2B-containing NMDA receptors in transfected cells depends on receptor activation, Ca2+ influx, and Thr286 autophosphorylation. Translocation of CaMKII because of interaction with the NMDA receptor Ca2+ channel may potentiate kinase activity and provide exquisite spatial and temporal control of postsynaptic substrate phosphorylation.

Phosphorylation

Recombinant Proteins - metabolism

Amino Acid Sequence

Animals

Receptors, N-Methyl-D-Aspartate - chemistry

Humans

Cells, Cultured

Receptors, N-Methyl-D-Aspartate - metabolism

Protein Binding

Rats

Calcium-Calmodulin-Dependent Protein Kinase Type 2

Calcium-Calmodulin-Dependent Protein Kinases - metabolism

Details

Title: Subtitle: Autophosphorylation-dependent targeting of calcium/ calmodulin-dependent protein kinase II by the NR2B subunit of the N-methyl- D-aspartate receptor
Creators: Stefan Strack - Department of Molecular Physiology and Biophysics and Center for Molecular Neuroscience, Vanderbilt University Medical Center, Nashville, Tennessee 37232-0615, USA
Roger J Colbran
Resource Type: Journal article
Publication Details: The Journal of biological chemistry, Vol.273(33), pp.20689-20692
DOI: 10.1074/jbc.273.33.20689
PMID: 9694809
NLM abbreviation: J Biol Chem
ISSN: 0021-9258
eISSN: 1083-351X
Publisher: United States
Grant note: DK20593 / NIDDK NIH HHS GM47973 / NIGMS NIH HHS CA68485 / NCI NIH HHS
Language: English
Date published: 08/14/1998
Academic Unit: Pathology; Iowa Neuroscience Institute; Fraternal Order of Eagles Diabetes Research Center; Neuroscience and Pharmacology
Record Identifier: 9984040443202771

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