Regular ArticleCloning and Tissue Distribution of Two New Potassium Channel α-Subunits from Rat Brain☆
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2017, NeuropharmacologyFormation of heteromeric Kv2 channels in mammalian brain neurons
2010, Journal of Biological ChemistryCitation Excerpt :The cDNA sequences of Kv2.1 (8) and Kv2.2 (9) predict proteins that are similar in N-terminal and membrane-spanning domains (∼90% homology), but they differ substantially across the large cytoplasmic C-terminal region (∼50%). Although they can assemble with modulatory α-subunits, Kv5, Kv6, Kv8, and Kv9 (10–13), it has been shown that mammalian Kv2.1 and Kv2.2 do not form heteromeric channels. This has been well supported by two major findings.
Conserved negative charges in the N-terminal tetramerization domain mediate efficient assembly of Kv2.1 and Kv2.1/Kv6.4 channels
2009, Journal of Biological ChemistryCitation Excerpt :Members of the Kv2 subfamily increase their diversity further by forming heterotetramers with α-subunits of the Kv5, Kv6, Kv8, and Kv9 subfamilies. These latter Kv subfamilies are designated silent α-subunits because they fail to express functional channels in a homotetrameric configuration (13–17) and are retained in the endoplasmic reticulum (ER). This retention is rescued by the selective co-assembly with members of the Kv2 subfamily in which the silent Kv subunits modulate the Kv2 currents by reducing the current amplitude, altering the inactivation and deactivation kinetics and shifting the voltage dependence of inactivation toward more hyperpolarized potentials (13, 15–27).
Potassium channel gene expression in the rat cochlear nucleus
2007, Hearing ResearchFunctional preservation of duplicated pair for RSVS III gene in the REST locus of rat 3q42
2005, Biochemical and Biophysical Research CommunicationsCitation Excerpt :The RNA message was abundant only in seminal vesicle and was not detectable in the other tissues, indicating an exclusive expression of both of these genes in seminal vesicle (Fig. 5B). Except RSVS I, we found that the genes encoding the major rat SVS proteins are clustered at a 270 kb region between a potassium voltage-gated channel, KCNS1[20,21], and a secretory leukocyte protease inhibitor, SLPI[22], on the rat 3q42 by the downstream order of RSVS II, RSVS IIIβ, RSVS IV, RSVS IIIα, RSVS VI, and RSVS V with the first two having the same gene orientation and the final four having an opposed orientation (Fig. 6A). Despite the fact that RSVS IV and RSVS V are not involved in the transglutaminase-catalyzed protein cross-links in the rat SVS (Fig. 1A), their genomic sequences still show the characteristic three exon–two intron structure of a REST gene [11].
Modification of Kv2.1 K<sup>+</sup> currents by the silent Kv10 subunits
2004, Molecular Brain Research
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North, R. A.
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To whom all correspondence should be addressed at Max-Planck Institut f. exp. Medizin, Hermann-Rein-Str. 3, D-37075 Göttingen, Germany. Fax: (+49)-551-3899-644. E-mail:[email protected].