Phosphorylation-dependent binding of 14-3-3 proteins controls TRESK regulation
about
Functional analysis of missense variants in the TRESK (KCNK18) K channel14-3-3ζ interacts with stat3 and regulates its constitutive activation in multiple myeloma cellsTwo-pore Domain Potassium Channels in AstrocytesC-Raf deficiency leads to hearing loss and increased noise susceptibility.TRESK background K(+) channel is inhibited by phosphorylation via two distinct pathways.Depletion of 14-3-3γ reduces the surface expression of Transient Receptor Potential Melastatin 4b (TRPM4b) channels and attenuates TRPM4b-mediated glutamate-induced neuronal cell death.TRESK background K(+) channel is inhibited by PAR-1/MARK microtubule affinity-regulating kinases in Xenopus oocytesThe LQLP calcineurin docking site is a major determinant of the calcium-dependent activation of human TRESK background K+ channel.L-type calcium channels play a critical role in maintaining lens transparency by regulating phosphorylation of aquaporin-0 and myosin light chain and expression of connexins14-3-3τ promotes surface expression of Cav2.2 (α1B) Ca2+ channels.Tubulin binds to the cytoplasmic loop of TRESK background K⁺ channel in vitro.PKC-dependent activation of human K(2P) 18.1 K(+) channels.Growth factor-dependent trafficking of cerebellar NMDA receptors via protein kinase B/Akt phosphorylation of NR2C.Trafficking of neuronal two pore domain potassium channels.Membrane proteins as 14-3-3 clients in functional regulation and intracellular transport.A Role for K2P Channels in the Operation of Somatosensory NociceptorsProperties, regulation, pharmacology, and functions of the K₂p channel, TRESK.Two-pore domain potassium channels: potential therapeutic targets for the treatment of pain.The family of K2P channels: salient structural and functional properties.Functional characterization of zebrafish K2P18.1 (TRESK) two-pore-domain K+ channels.Protein kinase A is central for forward transport of two-pore domain potassium channels K2P3.1 and K2P9.1.14-3-3 Proteins regulate K2P 5.1 surface expression on T lymphocytes.Intracellular traffic of the K+ channels TASK-1 and TASK-3: role of N- and C-terminal sorting signals and interaction with 14-3-3 proteins.
P2860
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P2860
Phosphorylation-dependent binding of 14-3-3 proteins controls TRESK regulation
description
2008 nî lūn-bûn
@nan
2008 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Phosphorylation-dependent binding of 14-3-3 proteins controls TRESK regulation
@ast
Phosphorylation-dependent binding of 14-3-3 proteins controls TRESK regulation
@en
Phosphorylation-dependent binding of 14-3-3 proteins controls TRESK regulation
@en-gb
Phosphorylation-dependent binding of 14-3-3 proteins controls TRESK regulation
@nl
type
label
Phosphorylation-dependent binding of 14-3-3 proteins controls TRESK regulation
@ast
Phosphorylation-dependent binding of 14-3-3 proteins controls TRESK regulation
@en
Phosphorylation-dependent binding of 14-3-3 proteins controls TRESK regulation
@en-gb
Phosphorylation-dependent binding of 14-3-3 proteins controls TRESK regulation
@nl
prefLabel
Phosphorylation-dependent binding of 14-3-3 proteins controls TRESK regulation
@ast
Phosphorylation-dependent binding of 14-3-3 proteins controls TRESK regulation
@en
Phosphorylation-dependent binding of 14-3-3 proteins controls TRESK regulation
@en-gb
Phosphorylation-dependent binding of 14-3-3 proteins controls TRESK regulation
@nl
P2860
P921
P3181
P356
P1476
Phosphorylation-dependent binding of 14-3-3 proteins controls TRESK regulation
@en
P2093
Drazsen Vuity
Péter Enyedi
P2860
P304
15672-15680
P3181
P356
10.1074/JBC.M800712200
P407
P577
2008-04-08T00:00:00Z