| http://purl.uniprot.org/citations/19901547 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19901547 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19901547 | http://www.w3.org/2000/01/rdf-schema#comment | "The somatodendritic subthreshold A-type K(+) current in neurons (I(SA)) depends on its kinetic and voltage-dependent properties to regulate membrane excitability, action potential repetitive firing, and signal integration. Key functional properties of the K(V)4 channel complex underlying I(SA) are determined by dipeptidyl peptidase-like proteins known as dipeptidyl peptidase 6 (DPP6) and dipeptidyl peptidase 10 (DPP10). Among the multiple known DPP10 isoforms with alternative N-terminal sequences, DPP10a confers exceptionally fast inactivation to K(V)4.2 channels. To elucidate the molecular basis of this fast inactivation, we investigated the structure-function relationship of the DPP10a N-terminal region and its interaction with the K(V)4.2 channel. Here, we show that DPP10a shares a conserved N-terminal sequence (MNQTA) with DPP6a (aka DPP6-E), which also induces fast inactivation. Deletion of the NQTA sequence in DPP10a eliminates this dramatic fast inactivation, and perfusion of MNQTA peptide to the cytoplasmic face of inside-out patches inhibits the K(V)4.2 current. DPP10a-induced fast inactivation exhibits competitive interactions with internally applied tetraethylammonium (TEA), and elevating the external K(+) concentration accelerates recovery from DPP10a-mediated fast inactivation. These results suggest that fast inactivation induced by DPP10a or DPP6a is mediated by a common N-terminal inactivation motif via a pore-blocking mechanism. This mechanism may offer an attractive target for novel pharmacological interventions directed at impairing I(SA) inactivation and reducing neuronal excitability."xsd:string |
| http://purl.uniprot.org/citations/19901547 | http://purl.org/dc/terms/identifier | "doi:10.4161/chan.3.6.10216"xsd:string |
| http://purl.uniprot.org/citations/19901547 | http://purl.org/dc/terms/identifier | "doi:10.4161/chan.3.6.10216"xsd:string |
| http://purl.uniprot.org/citations/19901547 | http://purl.uniprot.org/core/author | "Jerng H.H."xsd:string |
| http://purl.uniprot.org/citations/19901547 | http://purl.uniprot.org/core/author | "Jerng H.H."xsd:string |
| http://purl.uniprot.org/citations/19901547 | http://purl.uniprot.org/core/author | "Pfaffinger P.J."xsd:string |
| http://purl.uniprot.org/citations/19901547 | http://purl.uniprot.org/core/author | "Pfaffinger P.J."xsd:string |
| http://purl.uniprot.org/citations/19901547 | http://purl.uniprot.org/core/author | "Covarrubias M."xsd:string |
| http://purl.uniprot.org/citations/19901547 | http://purl.uniprot.org/core/author | "Covarrubias M."xsd:string |
| http://purl.uniprot.org/citations/19901547 | http://purl.uniprot.org/core/author | "Dougherty K."xsd:string |
| http://purl.uniprot.org/citations/19901547 | http://purl.uniprot.org/core/author | "Dougherty K."xsd:string |
| http://purl.uniprot.org/citations/19901547 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19901547 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19901547 | http://purl.uniprot.org/core/name | "Channels"xsd:string |
| http://purl.uniprot.org/citations/19901547 | http://purl.uniprot.org/core/name | "Channels"xsd:string |
| http://purl.uniprot.org/citations/19901547 | http://purl.uniprot.org/core/pages | "448-461"xsd:string |
| http://purl.uniprot.org/citations/19901547 | http://purl.uniprot.org/core/pages | "448-461"xsd:string |
| http://purl.uniprot.org/citations/19901547 | http://purl.uniprot.org/core/title | "A novel N-terminal motif of dipeptidyl peptidase-like proteins produces rapid inactivation of KV4.2 channels by a pore-blocking mechanism."xsd:string |
| http://purl.uniprot.org/citations/19901547 | http://purl.uniprot.org/core/title | "A novel N-terminal motif of dipeptidyl peptidase-like proteins produces rapid inactivation of KV4.2 channels by a pore-blocking mechanism."xsd:string |
| http://purl.uniprot.org/citations/19901547 | http://purl.uniprot.org/core/volume | "3"xsd:string |
| http://purl.uniprot.org/citations/19901547 | http://purl.uniprot.org/core/volume | "3"xsd:string |
| http://purl.uniprot.org/citations/19901547 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/19901547 |
| http://purl.uniprot.org/citations/19901547 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/19901547 |