14-3-3 Proteins regulate K2P5.1 surface expression on T lymphocytes
Juncal Fernández-Orth, Petra Ehling, Tobias Ruck, Susann Pankratz, Majella-Sophie Hofmann, Peter Landgraf, Daniela C. Dieterich, Karl-Heinz Smalla, Thilo Kähne, Guiscard Seebohm, Thomas Budde, Heinz Wiendl, Stefan Bittner and Sven G. Meuth
Version of Record online: 27 NOV 2016 | DOI: 10.1111/tra.12455
K2P5.1 channels possess a putative non-classical consensus motif for 14-3-3 proteins that mediates the interaction and promotes K2P5.1 channels to the plasma membrane. An amino acid mutation reduces the binding of 14-3-3 proteins to K2P5.1 resulting in a reduced number of channels at the plasma membrane and a decreased potassium efflux. Pharmacological inhibition of 14-3-3 protein binding to K2P5.1 functionally impacts T-cell proliferation and cytokine production. 14-3-3 proteins may represent a pharmacological target for the treatment of multiple sclerosis and other autoimmune diseases.