Identification of a novel tetramerization domain in large conductance K(ca) channels.

Article Details

Citation

Quirk JC, Reinhart PH

Identification of a novel tetramerization domain in large conductance K(ca) channels.

Neuron. 2001 Oct 11;32(1):13-23.

PubMed ID
11604135 [ View in PubMed
]
Abstract

More than 50 genes are known to encode K(+) channel monomers and can coassemble to form hetero-tetrameric K(+) channels. However, only a subset of possible monomer combinations come together to form functional ion channels. The assembly and tetramerization of appropriate channel monomers is mediated by association domains (ADs). To identify such domains in human large-conductance Ca(2+)-activated K(+) channels (hSlo1), we screened hSlo1 domains for self-association using yeast two-hybrid assays. Putative ADs were subjected to functional assays in Xenopus oocytes and further characterized by coprecipitation, native gel electrophoresis, and sucrose density gradient centrifugation assays. This led to the identification of a single intracellular association domain localized near the channel pore and required for channel function. We conclude that this novel tetramerization domain, referred to as BK-T1, promotes the assembly of hSlo1 monomers into functional K(Ca) channels.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Calcium-activated potassium channel subunit alpha-1Q12791Details