It has been suggested that the large conductance Ca2+-activated K+ channel contains one or more domains known as regulators of K+ conductance (RCK) in its cytosolic C terminus. Here, we show that the second RCK domain (RCK2) is functionally important and that it forms a heterodimer with RCK1 via a hydrophobic interface. Mutant channels lacking RCK2 are nonfunctional despite their tetramerization and surface expression. The hydrophobic residues that are expected to form an interface between RCK1 and RCK2, based on the crystal structure of the bacterial MthK channel, are well conserved, and the interactions of these residues were confirmed by mutant cycle analysis. The hydrophobic interaction appears to be critical for the Ca2+-dependent gating of the large conductance Ca2+-activated K+ channel.
Hydrophobic Interface between Two Regulators of K+ Conductance Domains Critical for Calcium-dependent Activation of Large Conductance Ca2+-activated K+ Channels*
Hyun-Ju Kim,Hyun-Ho Lim,S. Rho,S. Eom,Chul-Seung Park
Published 2006 in Journal of Biological Chemistry
ABSTRACT
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- Publication year
2006
- Venue
Journal of Biological Chemistry
- Publication date
2006-12-15
- Fields of study
Biology, Medicine, Chemistry
- Identifiers
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- Source metadata
Semantic Scholar, PubMed
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