KvLQT1 and IsK (minK) proteins associate to form the IKS cardiac potassium current

Nature ◽  
1996 ◽  
Vol 384 (6604) ◽  
pp. 78-80 ◽  
Author(s):  
Jacques Barhanin ◽  
Florian Lesage ◽  
Eric Guillemare ◽  
Michel Fink ◽  
Michel Lazdunski ◽  
...  
Keyword(s):  
Potassium Current ◽  
Cardiac Potassium Current

scholarly journals Feedback Remodeling of Cardiac Potassium Current Expression

Circulation ◽  
2008 ◽  
Vol 118 (10) ◽  
pp. 983-992 ◽  
Author(s):  
Ling Xiao ◽  
Jiening Xiao ◽  
Xiaobin Luo ◽  
Huixian Lin ◽  
Zhiguo Wang ◽  
...  
Keyword(s):  
Potassium Current ◽  
Cardiac Potassium Current

scholarly journals Single-channel basis for the slow activation of the repolarizing cardiac potassium current,IKs

2013 ◽  
Vol 110 (11) ◽  
pp. E996-E1005 ◽  
Author(s):  
Daniel Werry ◽  
Jodene Eldstrom ◽  
Zhuren Wang ◽  
David Fedida
Keyword(s):  
Potassium Current ◽  
Single Channel ◽  
Cardiac Potassium Current

scholarly journals A minK–HERG complex regulates the cardiac potassium current IKr

Nature ◽  
10.1038/40882 ◽  
1997 ◽  
Vol 388 (6639) ◽  
pp. 289-292 ◽  
Author(s):  
Thomas V. McDonald ◽  
Zhihui Yu ◽  
Zhen Ming ◽  
Eugen Palma ◽  
Marian B. Meyers ◽  
...  
Keyword(s):  
Potassium Current ◽  
Cardiac Potassium Current

scholarly journals Doxorubicin induces caspase-mediated proteolysis of KV7.1

2018 ◽  
Author(s):  
Anne Strigli ◽  
Christian Raab ◽  
Sabine Hessler ◽  
Tobias Huth ◽  
Adam J. T. Schuldt ◽  
...  
Keyword(s):  
Posttranslational Modification ◽  
Potassium Current ◽  
Induced Pluripotent Stem Cell ◽  
Neonatal Rat ◽  
Loss Of Function ◽  
Long Qt ◽  
Human Cardiomyocytes ◽  
Induced Pluripotent ◽  
Lqt Syndrome ◽  
Cardiac Potassium Current

AbstractThe voltage-gated potassium channel Kv7.1 (KCNQ1) co-assembles with KCNE1 to generate the cardiac potassium current IKs. Gain- and loss-of-function mutations in KCNQ1 are associated with atrial fibrillation and long-QT (LQT) syndrome, respectively, highlighting the importance of modulating IKS activity for proper cardiac function. On a post-translational level, IKS can be regulated by phosphorylation, ubiquitination and sumoylation. Here, we report proteolysis of Kv7.1 as a novel, irreversible posttranslational modification. The identification of two C-terminal fragments (CTF1 and CTF2) of Kv7.1 led us to identify an aspartate critical for the generation of CTF2 and caspases as responsible for mediating Kv7.1 proteolysis. Activating caspases by apoptotic stimuli significantly reduced Kv7.1/KCNE1 currents, which was abrogated in cells expressing caspase-resistant Kv7.1 D459A/KCNE1 channels. An increase in cleavage of Kv7.1 could be detected in the case of LQT mutation G460S, which is located adjacent to the cleavage site. Application of apoptotic stimuli or doxorubicin-induced cardiotoxicity provoked caspase-mediated cleavage of endogenous Kv7.1 in human cardiomyocytes. In summary, our findings establish caspases as novel regulatory components for modulating Kv7.1 activity which may have important implications for the molecular mechanism of doxorubicin-induced cardiotoxicity.Non-standard Abbreviations and AcronymsCamcalmodulinEBCequilibrium buffer contentLQT syndromelong QT syndromeNRVMNeonatal rat ventricular cardiomyocyteshiPSC-CMshuman induced pluripotent stem cell-derived cardiomyocytes

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