Phosphorylation-dependent binding of 14-3-3 proteins controls TRESK regulation.

ABSTRACT: The two-pore domain K(+) channel, TRESK (TWIK-related spinal cord K(+) channel) is reversibly activated by the calcium/calmodulin-dependent protein phosphatase, calcineurin. In the present study, we report that 14-3-3 proteins directly bind to the intracellular loop of TRESK and control the kinetics of the calcium-dependent regulation of the channel. Coexpression of 14-3-3eta with TRESK blocked, whereas the coexpression of a dominant negative form of 14-3-3eta accelerated the return of the K(+) current to the resting state after the activation mediated by calcineurin in Xenopus oocytes. The direct action of 14-3-3 was spatially restricted to TRESK, since 14-3-3eta was also effective, when it was tethered to the channel by a flexible polyglutamine-containing chain. The effect of both the co

SUBMITTER: Czirjak G 

PROVIDER: S-EPMC3259650 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature