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.
Pubmed ID: 17635915 RIS Download
Mesh terms: Adaptor Proteins, Signal Transducing | Animals | COS Cells | Calcium-Calmodulin-Dependent Protein Kinase Type 2 | Calcium-Calmodulin-Dependent Protein Kinases | Cercopithecus aethiops | Dendrites | Hippocampus | Lentivirus | Membrane Proteins | Neuronal Plasticity | Phosphorylation | Protein Structure, Tertiary | Protein Transport | RNA Interference | Rats | Shal Potassium Channels | Synapses
Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.