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XB-ART-46999
Chem Biol 2013 Apr 18;204:583-93. doi: 10.1016/j.chembiol.2013.03.015.
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A semisynthetic fusicoccane stabilizes a protein-protein interaction and enhances the expression of K+ channels at the cell surface.

Anders C , Higuchi Y , Koschinsky K , Bartel M , Schumacher B , Thiel P , Nitta H , Preisig-Müller R , Schlichthörl G , Renigunta V , Ohkanda J , Daut J , Kato N , Ottmann C .


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Small-molecule stabilization of protein-protein interactions is an emerging field in chemical biology. We show how fusicoccanes, originally identified as fungal toxins acting on plants, promote the interaction of 14-3-3 proteins with the human potassium channel TASK-3 and present a semisynthetic fusicoccane derivative (FC-THF) that targets the 14-3-3 recognition motif (mode 3) in TASK-3. In the presence of FC-THF, the binding of 14-3-3 proteins to TASK-3 was increased 19-fold and protein crystallography provided the atomic details of the effects of FC-THF on this interaction. We also tested the functional effects of FC-THF on TASK channels heterologously expressed in Xenopus oocytes. Incubation with 10 μM FC-THF was found to promote the transport of TASK channels to the cell membrane, leading to a significantly higher density of channels at the surface membrane and increased potassium current.

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Species referenced: Xenopus laevis