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Potassium voltage-gated channel, subfamily G, member 3

Kv6.3, KCNG3, Kv10.1, Kv10.1a, Kv10.1b, Kv6.4
Voltage-gated potassium (Kv) channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. Their diverse functions include regulating neurotransmitter release, heart rate, insulin secretion, neuronal excitability, epithelial electrolyte transport, smooth muscle contraction, and cell volume. This gene encodes a member of the potassium channel, voltage-gated, subfamily G. This member is a gamma subunit functioning as a modulatory molecule. Alternative splicing results in two transcript variants encoding distinct isoforms. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Kv2.1, CAN, Kv1.4, HAD, ACID
Papers on Kv6.3
Kv10.1 K(+) channel: from physiology to cancer.
Pardo et al., Amiens, France. In Pflugers Arch, Feb 2016
Ether-à-go-go-1 (Eag1, Kv10.1, KCNH1) is a member of the voltage-activated potassium channel family and was the first K(+) channel to be associated with oncogenesis and tumor development.
Early onset schizophrenia: Gender analysis of genome-wide potential methylation.
De Luca et al., Toronto, Canada. In Clin Chim Acta, Oct 2015
In the gene-wise analysis, the KCNG3 was significantly associated with higher potential methylation in males (p=0.0004).
Mutations in KCNH1 and ATP6V1B2 cause Zimmermann-Laband syndrome.
Kutsche et al., Hamburg, Germany. In Nat Genet, Jun 2015
KCNH1 encodes the voltage-gated K(+) channel Eag1 (Kv10.1).
Expression and function of a CP339,818-sensitive K⁺ current in a subpopulation of putative nociceptive neurons from adult mouse trigeminal ganglia.
Catacuzzeno et al., Perugia, Italy. In J Neurophysiol, May 2015
It could neither be associated with Kv2.1 channels homomeric or heteromerically associated with the Kv9.2, Kv9.3, or Kv6.4 subunits, whose block by CP, tested using two-electrode voltage-clamp recordings from Xenopus oocytes, resulted in the low micromolar range, nor to the Kv7 subfamily, given the lack of blocking efficacy of 3 μM XE991.
Auxiliary KCNE subunits modulate both homotetrameric Kv2.1 and heterotetrameric Kv2.1/Kv6.4 channels.
Bocksteins et al., Copenhagen, Denmark. In Sci Rep, 2014
Here, we demonstrate that the transmembrane β-subunit KCNE5 modifies the Kv2.1/Kv6.4
Analysis of the expression of Kv10.1 potassium channel in patients with brain metastases and glioblastoma multiforme: impact on survival.
Pardo et al., Göttingen, Germany. In Bmc Cancer, 2014
BACKGROUND: Kv10.1, a voltage-gated potassium channel only detected in the healthy brain, was found to be aberrantly expressed in extracerebral cancers.
Modulation of Closed-State Inactivation in Kv2.1/Kv6.4 Heterotetramers as Mechanism for 4-AP Induced Potentiation.
Snyders et al., Antwerp, Belgium. In Plos One, 2014
In contrast, Kv6.4 currents were potentiated by 4-AP while displaying moderately increased affinities for the channel pore blockers quinidine and flecainide.
KV10.1 K(+)-channel plasma membrane discrete domain partitioning and its functional correlation in neurons.
Ortega et al., Mexico. In Biochim Biophys Acta, 2014
KV10.1 potassium channels are implicated in a variety of cellular processes including cell proliferation and tumour progression.
BKCa and hEag1 channels regulate cell proliferation and differentiation in human bone marrow-derived mesenchymal stem cells.
Li et al., Hong Kong, Hong Kong. In J Cell Physiol, 2014
The present study investigated potential roles of large-conductance Ca(2+) -activated potassium (BKCa ) channels and ether-à-go-go potassium (hEag1 or Kv10.1) channels in regulating cell proliferation and differentiation in human MSCs.
Hippocampal ether-à-go-go1 potassium channels blockade: effects in the startle reflex and prepulse inhibition.
Del Bel et al., Ribeirão Preto, Brazil. In Neurosci Lett, 2014
Recently, our group described the ether-à-go-go1(Eag1) voltage-gated potassium (K(+)) channel (Kv10.1)
Regulation of hERG and hEAG channels by Src and by SHP-1 tyrosine phosphatase via an ITIM region in the cyclic nucleotide binding domain.
Lam et al., Toronto, Canada. In Plos One, 2013
In particular, two prototypes, EAG1/Kv10.1/KCNH1
The subfamily-specific interaction between Kv2.1 and Kv6.4 subunits is determined by interactions between the N- and C-termini.
Snyders et al., Antwerp, Belgium. In Plos One, 2013
The "silent" voltage-gated potassium (KvS) channel subunit Kv6.4 does not form electrically functional homotetramers at the plasma membrane but assembles with Kv2.1 subunits, generating functional Kv2.1/Kv6.4
Behavioural and functional characterization of Kv10.1 (Eag1) knockout mice.
Stuehmer et al., Göttingen, Germany. In Hum Mol Genet, 2013
Kv10.1 (Eag1), member of the Kv10 family of voltage-gated potassium channels, is preferentially expressed in adult brain.
External pH modulates EAG superfamily K+ channels through EAG-specific acidic residues in the voltage sensor.
Jegla et al., United States. In J Gen Physiol, 2013
Previous studies indicate that external acidification inhibits activation of three EAG superfamily K(+) channels, Kv10.1 (Eag1), Kv11.1 (Erg1), and Kv12.1 (Elk1).
Intracellular ion channels and cancer.
Szabò et al., Padova, Italy. In Front Physiol, 2012
The nuclear potassium channel Kv10.1 and the nuclear chloride channel CLIC4 as well as the endoplasmatic reticulum (ER)-located inositol 1,4,5-trisphosphate (IP3) receptor, the ER-located Ca(2+) depletion sensor STIM1 (stromal interaction molecule 1), a component of the store-operated Ca(2+) channel and the ER-resident TRPM8 are also mentioned.
Approaches targeting K(V)10.1 open a novel window for cancer diagnosis and therapy.
Stühmer et al., Göttingen, Germany. In Curr Med Chem, 2011
[review] an overview of the current status of data linking K(V)10.1 to cancer, and techniques that could exploit K(V)10.1's properties for the management of cancer
Mutation of histidine 105 in the T1 domain of the potassium channel Kv2.1 disrupts heteromerization with Kv6.3 and Kv6.4.
Preisig-Müller et al., Marburg an der Lahn, Germany. In J Biol Chem, 2009
Mutation of histidine 105 in the T1 domain of the potassium channel Kv2.1 disrupts heteromerization with Kv6.3 and Kv6.4.
Domain analysis of Kv6.3, an electrically silent channel.
Snyders et al., Antwerp, Belgium. In J Physiol, 2005
This study suggests that the silent behaviour of Kv6.3 is largely caused by the C-terminal part of its sixth transmembrane domain that causes ER retention of the subunit.
Obligatory heterotetramerization of three previously uncharacterized Kv channel alpha-subunits identified in the human genome.
Snyders et al., Antwerp, Belgium. In Proc Natl Acad Sci U S A, 2002
Obligatory heterotetramerization of three previously uncharacterized Kv channel subunits identified in human genome (Kv6.3)(Kv10.1) (Kv11.1)
Molecular cloning and characterization of Kv6.3, a novel modulatory subunit for voltage-gated K(+) channel Kv2.1.
Furuichi et al., Tsukuba, Japan. In Febs Lett, 2002
These results indicate that Kv6.3 is a novel member of the voltage-gated K(+) channel which functions as a modulatory subunit of the Kv2.1 channel.
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