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J Biol Chem
2008 Jun 06;28323:15672-80. doi: 10.1074/jbc.M800712200.
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Phosphorylation-dependent binding of 14-3-3 proteins controls TRESK regulation.
Czirják G
,
Vuity D
,
Enyedi P
.
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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 coexpressed and chained 14-3-3 was alleviated by the microinjection of Ser(P)-Raf259 phosphopeptide that competes with TRESK for binding to 14-3-3. The gamma and eta isoforms of 14-3-3 controlled TRESK regulation, whereas the beta, zeta, epsilon, sigma, and tau isoforms failed to influence the mechanism significantly. Phosphorylation of serine 264 in mouse TRESK was required for the binding of 14-3-3eta. Because 14-3-3 proteins are ubiquitous, they are expected to control the duration of calcineurin-mediated TRESK activation in all the cell types that express the channel, depending on the phosphorylation state of serine 264. This kind of direct control of channel regulation by 14-3-3 is unique within the two-pore domain K(+) channel family.
Aitken,
14-3-3 proteins: a historic overview.
2006, Pubmed
Aitken,
14-3-3 proteins: a historic overview.
2006,
Pubmed
Chemin,
Mechanisms underlying excitatory effects of group I metabotropic glutamate receptors via inhibition of 2P domain K+ channels.
2003,
Pubmed
Chen,
Inhibition of a background potassium channel by Gq protein alpha-subunits.
2006,
Pubmed
Czirják,
Formation of functional heterodimers between the TASK-1 and TASK-3 two-pore domain potassium channel subunits.
2002,
Pubmed
,
Xenbase
Czirják,
Targeting of calcineurin to an NFAT-like docking site is required for the calcium-dependent activation of the background K+ channel, TRESK.
2006,
Pubmed
,
Xenbase
Czirják,
The two-pore domain K+ channel, TRESK, is activated by the cytoplasmic calcium signal through calcineurin.
2004,
Pubmed
,
Xenbase
Czirják,
Inhibition of TASK-1 potassium channel by phospholipase C.
2001,
Pubmed
,
Xenbase
Dobler,
TRESK two-pore-domain K+ channels constitute a significant component of background potassium currents in murine dorsal root ganglion neurones.
2007,
Pubmed
,
Xenbase
Dodge,
Calcineurin anchoring and cell signaling.
2003,
Pubmed
Gardino,
Structural determinants of 14-3-3 binding specificities and regulation of subcellular localization of 14-3-3-ligand complexes: a comparison of the X-ray crystal structures of all human 14-3-3 isoforms.
2006,
Pubmed
Heurteaux,
TREK-1, a K+ channel involved in neuroprotection and general anesthesia.
2004,
Pubmed
Hoshi,
Biophysical and molecular mechanisms of Shaker potassium channel inactivation.
1990,
Pubmed
,
Xenbase
Kang,
Functional expression of TRESK-2, a new member of the tandem-pore K+ channel family.
2004,
Pubmed
Kang,
TREK-2 (K2P10.1) and TRESK (K2P18.1) are major background K+ channels in dorsal root ganglion neurons.
2006,
Pubmed
Kang,
Mechanism of inhibition of TREK-2 (K2P10.1) by the Gq-coupled M3 muscarinic receptor.
2006,
Pubmed
Kang,
Lamotrigine inhibits TRESK regulated by G-protein coupled receptor agonists.
2008,
Pubmed
Keshavaprasad,
Species-specific differences in response to anesthetics and other modulators by the K2P channel TRESK.
2005,
Pubmed
Li,
Structural delineation of the calcineurin-NFAT interaction and its parallels to PP1 targeting interactions.
2004,
Pubmed
Li,
Structure of calcineurin in complex with PVIVIT peptide: portrait of a low-affinity signalling interaction.
2007,
Pubmed
Liu,
Potent activation of the human tandem pore domain K channel TRESK with clinical concentrations of volatile anesthetics.
2004,
Pubmed
,
Xenbase
Lotshaw,
Biophysical, pharmacological, and functional characteristics of cloned and native mammalian two-pore domain K+ channels.
2007,
Pubmed
Masino,
Solution structure of polyglutamine tracts in GST-polyglutamine fusion proteins.
2002,
Pubmed
Mathie,
Neuronal two-pore-domain potassium channels and their regulation by G protein-coupled receptors.
2007,
Pubmed
Muslin,
Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine.
1996,
Pubmed
,
Xenbase
O'Kelly,
Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals.
2002,
Pubmed
Patel,
Inhalational anesthetics activate two-pore-domain background K+ channels.
1999,
Pubmed
Rajan,
Interaction with 14-3-3 proteins promotes functional expression of the potassium channels TASK-1 and TASK-3.
2002,
Pubmed
,
Xenbase
Renigunta,
The retention factor p11 confers an endoplasmic reticulum-localization signal to the potassium channel TASK-1.
2006,
Pubmed
,
Xenbase
Roy,
A conserved docking site modulates substrate affinity for calcineurin, signaling output, and in vivo function.
2007,
Pubmed
Sano,
A novel two-pore domain K+ channel, TRESK, is localized in the spinal cord.
2003,
Pubmed
Sen,
Role of histidine interruption in mitigating the pathological effects of long polyglutamine stretches in SCA1: A molecular approach.
2003,
Pubmed
Thorson,
14-3-3 proteins are required for maintenance of Raf-1 phosphorylation and kinase activity.
1998,
Pubmed
Veale,
G(alpha)q-mediated regulation of TASK3 two-pore domain potassium channels: the role of protein kinase C.
2007,
Pubmed
Xiao,
Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways.
1995,
Pubmed
Yaffe,
The structural basis for 14-3-3:phosphopeptide binding specificity.
1997,
Pubmed
Zhang,
Raf-1 kinase and exoenzyme S interact with 14-3-3zeta through a common site involving lysine 49.
1997,
Pubmed
