Title : Dimerization of
TWIK-1 K+
channel subunits via a disulfide bridge
Abstract :
- TWIK-1 is a new type of K+ channel with two P domains and is abundantly expressed in human heart and brain
- Here we show that TWIK-1 subunits can self-associate to give dimers containing an inter chain disulfide bridge
- This assembly involves a 34 amino acid domain that is localized to the extracellular M1P1 linker loop
- Cysteine 69 which is part of this interacting domain is implicated in the formation of the disulfide bond
- Replacing this cysteine with a serine residue results in the loss of functional K+ channel expression
- This is the first example of a covalent association of functional subunits in voltage-sensitive channels via a disulfide bridge
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