Cargando…
Optimized tight binding between the S1 segment and KCNE3 is required for the constitutively open nature of the KCNQ1-KCNE3 channel complex
Tetrameric voltage-gated K(+) channels have four identical voltage sensor domains, and they regulate channel gating. KCNQ1 (Kv7.1) is a voltage-gated K(+) channel, and its auxiliary subunit KCNE proteins dramatically regulate its gating. For example, KCNE3 makes KCNQ1 a constitutively open channel a...
Autores principales: | Kasuya, Go, Nakajo, Koichi |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9671499/ https://www.ncbi.nlm.nih.gov/pubmed/36331187 http://dx.doi.org/10.7554/eLife.81683 |
Ejemplares similares
-
KCNE1 and KCNE3 Stabilize and/or Slow Voltage Sensing S4 Segment of KCNQ1 Channel
por: Nakajo, Koichi, et al.
Publicado: (2007) -
Allosteric mechanism for KCNE1 modulation of KCNQ1 potassium channel activation
por: Kuenze, Georg, et al.
Publicado: (2020) -
Gating modulation of the KCNQ1 channel by KCNE proteins studied by voltage-clamp fluorometry
por: Nakajo, Koichi
Publicado: (2019) -
KCNQ1 subdomains involved in KCNE modulation revealed by an invertebrate KCNQ1 orthologue
por: Nakajo, Koichi, et al.
Publicado: (2011) -
KCNE1 divides the voltage sensor movement in KCNQ1/KCNE1 channels into two steps
por: Barro-Soria, Rene, et al.
Publicado: (2014)