Synergistic modulation of KCNQ1/KCNE1 K+ channels (IKs) by phosphatidylinositol 4,5-bisphosphate (PIP2) and [ATP]i

Kienitz, Marie-Cécile; Vladimirova, Dilyana

doi:10.1016/j.cellsig.2015.04.002

Cited by 7 publications

(2 citation statements)

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“…The biophysical and pharmacology properties of KCNQ1 complexes vary quite considerably depending on the type ( Barhanin et al, 1996 ; Jespersen et al, 2005 ) of associated KCNE protein and likely on their quantity as recent studies on KCNE1 subunit indicate ( Wang et al, 2020 ). Intracellular second messengers such as free Ca 2+ ions ( Tohse, 1990 ; Shamgar et al, 2006 ) and adenosine nucleotides ( Li et al, 2013 ; Kienitz and Vladimirova, 2015 ), as well as membranes lipids ( Loussouarn et al, 2003 ; Zaydman et al, 2013 ; Liin et al, 2015b ) and protein kinase A ( Yazawa and Kameyama, 1990 ) exert a pronounced modulatory action on these channels.…”

Section: Introductionmentioning

confidence: 99%

Mechanism of external K+ sensitivity of KCNQ1 channels

Abrahamyan

Eldstrom

Sahakyan

et al. 2023

Journal of General Physiology

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KCNQ1 voltage-gated K+ channels are involved in a wide variety of fundamental physiological processes and exhibit the unique feature of being markedly inhibited by external K+. Despite the potential role of this regulatory mechanism in distinct physiological and pathological processes, its exact underpinnings are not well understood. In this study, using extensive mutagenesis, molecular dynamics simulations, and single-channel recordings, we delineate the molecular mechanism of KCNQ1 modulation by external K+. First, we demonstrate the involvement of the selectivity filter in the external K+ sensitivity of the channel. Then, we show that external K+ binds to the vacant outermost ion coordination site of the selectivity filter inducing a diminution in the unitary conductance of the channel. The larger reduction in the unitary conductance compared to whole-cell currents suggests an additional modulatory effect of external K+ on the channel. Further, we show that the external K+ sensitivity of the heteromeric KCNQ1/KCNE complexes depends on the type of associated KCNE subunits.

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Section: Introductionmentioning

confidence: 99%

Mechanism of external K+ sensitivity of KCNQ1 channels

Abrahamyan

Eldstrom

Sahakyan

et al. 2023

Journal of General Physiology

View full text Add to dashboard Cite

show abstract

“…All experiments were performed using either CHO cells stably expressing the subunits KCNQ1/KCNE1 underlying I Ks (45) or native HEK 293 cells. CHO cells were grown in Iscove's modified Dulbecco's medium containing fetal bovine serum (10%), HT supplement, non-essential amino acids, and 400 g/ml G-418.…”

Section: Methodsmentioning

confidence: 99%