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SAP97 directs the localization of Kv4.2 to spines in hippocampal neurons: regulation by CaMKII.

Authors: Gardoni, F  Mauceri, D  Marcello, E  Sala, C  Di Luca, M  Jeromin, A 
Citation: Gardoni F, etal., J Biol Chem. 2007 Sep 28;282(39):28691-9. Epub 2007 Jul 16.
Pubmed: (View Article at PubMed) PMID:17635915
DOI: Full-text: DOI:10.1074/jbc.M701899200

The pore-forming alpha-subunit Kv4.2 is a key constituent of the A-type channel and critically involved in the regulation of dendritic excitability and plasticity. Here we show that Kv4.2 is enriched in the postsynaptic density (PSD) fraction and specifically interacts with synapse-associated protein 97 (SAP97). This interaction requires an intact C terminus of Kv4.2 and occurs via the PDZ domains of SAP97. Pharmacologically induced translocation of SAP97 to spines also drives Kv4.2 to the PSD, whereas SAP97 lentivirally based RNA interference reduces Kv4.2 in the PSD. In addition, calcium/calmodulin-dependent protein kinase II (CaMKII)-dependent SAP97 phosphorylation regulates the subcellular localization of Kv4.2. These results show that SAP97-CaMKII pathway plays an important role for the trafficking of Kv4.2 to dendrites and spines.


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CRRD Object Information
CRRD ID: 2306826
Created: 2009-05-07
Species: All species
Last Modified: 2009-05-07
Status: ACTIVE


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