Kir5.1 underlies long-lived subconductance levels in heteromeric Kir4.1/Kir5.1 channels from Xenopus tropicalis
| Autor: | Stephen J. Tucker, Sarah V. Ranson, Lijun Shang |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2009 |
| Předmět: |
Subfamily
Kir4.2 Kir5.1 Kir4.1 Protein subunit Xenopus Biophysics Model system Biology Biochemistry Article 03 medical and health sciences 0302 clinical medicine Animals Potassium channel Potassium Channels Inwardly Rectifying Molecular Biology Subconductance level 030304 developmental biology 0303 health sciences Electrophysiological Processes Anatomy Cell Biology biology.organism_classification Protein multimerization Electrophysiological Phenomena Rats Channel analysis Protein Multimerization 030217 neurology & neurosurgery Heteromeric channel |
| Zdroj: | Biochemical and Biophysical Research Communications |
| ISSN: | 1090-2104 0006-291X |
| Popis: | The inwardly-rectifying potassium channel subunit Kir5.1 selectively co-assembles with members of the Kir4.0 subfamily to form novel pH-sensitive heteromeric channels with unique single channel properties. In this study, we have cloned orthologs of Kir4.1 and Kir5.1 from the genome of the amphibian, Xenopus tropicalis (Xt). Heteromeric XtKir4.1/XtKir5.1 channels exhibit similar macroscopic current properties to rat Kir4.1/Kir5.1 with a faster time-dependent rate of activation. However, single channel analysis of heteromeric XtKir4.1/XtKir5.1 channels reveals that they have markedly different long-lived, multi-level subconductance states. Furthermore, we demonstrate that the XtKir5.1 subunit is responsible for these prominent subconductance levels. These results are consistent with a model in which the slow transitions between sublevel states represent the movement of individual subunits. These novel channels now provide an excellent model system to determine the structural basis of subconductance levels and contribution of heteromeric pore architecture to this process. |
| Databáze: | OpenAIRE |
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