Functional mutagenesis screens reveal the ‘cap structure’ formation in disulfide-bridge free TASK channels

• DOI: 10.1038/srep19492
• Publication Date: 2016-01-22T10:12:06Z
• Authors: Matthias Goldstein; Susanne Rinné; Aytug K. Kiper; David Ramírez; Michael F. Netter; Daniel Bustos; Beatriz Ortiz-Bonnin; Wendy González; Niels Decher
• Keywords: Bridge (graph theory)

Abstract Two-pore-domain potassium (K 2P ) channels have a large extracellular cap structure formed by two M1-P1 linkers, containing cysteine for dimerization. However, this is not present in the TASK-1/3/5 subfamily. The functional role of poorly understood and it remained unclear whether K assemble domain-swapped orientation or not. Functional alanine-mutagenesis screens TASK-1 TRAAK were used to build an silico model cap. According our data disulfide-bridge free TASK similar that other most likely assembled orientation. As conserved essential expression all tested, we propose hydrophobic residues at inner leaflets domains can interact with each way stabilizing among channels.