One SUMO is sufficient to silence the dimeric potassium channel K2P1
about
Crystal structure of the human two-pore domain potassium channel K2P1Hyper-SUMOylation of the Kv7 potassium channel diminishes the M-current leading to seizures and sudden death.SUMOylation regulates the homologous to E6-AP carboxyl terminus (HECT) ubiquitin ligase Rsp5p.Individual IKs channels at the surface of mammalian cells contain two KCNE1 accessory subunits.SUMOylation silences heterodimeric TASK potassium channels containing K2P1 subunits in cerebellar granule neurons.A hydrophobic barrier deep within the inner pore of the TWIK-1 K2P potassium channel.Targeting potassium channels in cancerNeuronal SUMOylation: mechanisms, physiology, and roles in neuronal dysfunction.TWIK-1 contributes to the intrinsic excitability of dentate granule cells in mouse hippocampus.Molecular aspects of structure, gating, and physiology of pH-sensitive background K2P and Kir K+-transport channels.SUMO modification of cell surface Kv2.1 potassium channels regulates the activity of rat hippocampal neuronsSUMOylation regulates ciliary localization of olfactory signaling proteins.SUMO downregulates GLP-1-stimulated cAMP generation and insulin secretionTWIK1, a unique background channel with variable ion selectivity.The gap junction channel protein connexin 43 is covalently modified and regulated by SUMOylationWeighing up the possibilities: Controlling translation by ubiquitylation and sumoylation.Heterodimerization within the TREK channel subfamily produces a diverse family of highly regulated potassium channels.SUMOylation alters CRMP2 regulation of calcium influx in sensory neurons.CRMP2 protein SUMOylation modulates NaV1.7 channel trafficking.SUMOylation of NaV1.2 channels mediates the early response to acute hypoxia in central neurons.A Role for K2P Channels in the Operation of Somatosensory NociceptorsSumoylation in neurodegenerative diseases.Molecular targets underlying SUMO-mediated neuroprotection in brain ischemia.Receptor trafficking and the regulation of synaptic plasticity by SUMO.Deciphering the subunit composition of multimeric proteins by counting photobleaching steps.Silent but not dumb: how cellular trafficking and pore gating modulate expression of TWIK1 and THIK2.Much more than a leak: structure and function of K₂p-channels.Sub-cellular localization specific SUMOylation in the heart.Coordination of Cellular Localization-Dependent Effects of Sumoylation in Regulating Cardiovascular and Neurological Diseases.Loss of SUMOylation on ATF3 inhibits proliferation of prostate cancer cells by modulating CCND1/2 activity.SUMOylation determines the voltage required to activate cardiac IKs channels.SUMOylation regulates insulin exocytosis downstream of secretory granule docking in rodents and humans.Silent TWIK-1 potassium channels conduct monovalent cation currents.K2P potassium channels, mysterious and paradoxically exciting.Purification and Characterization of RhoPDE, a Retinylidene/Phosphodiesterase Fusion Protein and Potential Optogenetic Tool from the Choanoflagellate Salpingoeca rosetta.Emerging Roles of TWIK-1 Heterodimerization in the Brain.Expression, purification, and spectral tuning of RhoGC, a retinylidene/guanylyl cyclase fusion protein and optogenetics tool from the aquatic fungus Blastocladiella emersonii.TWIK-1/TASK-3 heterodimeric channels contribute to the neurotensin-mediated excitation of hippocampal dentate gyrus granule cells
P2860
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P2860
One SUMO is sufficient to silence the dimeric potassium channel K2P1
description
2010 nî lūn-bûn
@nan
2010 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
One SUMO is sufficient to silence the dimeric potassium channel K2P1
@ast
One SUMO is sufficient to silence the dimeric potassium channel K2P1
@en
type
label
One SUMO is sufficient to silence the dimeric potassium channel K2P1
@ast
One SUMO is sufficient to silence the dimeric potassium channel K2P1
@en
prefLabel
One SUMO is sufficient to silence the dimeric potassium channel K2P1
@ast
One SUMO is sufficient to silence the dimeric potassium channel K2P1
@en
P2093
P2860
P356
P1476
One SUMO is sufficient to silence the dimeric potassium channel K2P1
@en
P2093
Astrid Kollewe
Irina S Dementieva
Jeremy D Marks
Leigh D Plant
Sonia Olikara
P2860
P304
10743-10748
P356
10.1073/PNAS.1004712107
P407
P577
2010-05-24T00:00:00Z