IndraLab

Statements

Tungstate activates KCNMA1. 5 / 5
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reach
"BK channel activation by tungstate requires the beta1 subunit extracellular loop residues essential to modulate voltage sensor function and channel gating."
24158430
reach
"Given that the large-conductance voltage- and Ca (2+)-dependent K (+) (BK) channel is a key element in the control of arterial tone, our aim was to evaluate whether BK channel modulation by tungstate can contribute to its antihypertensive effect."
22473360
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"These results, together with previously published reports, support the idea that the putative binding site for tungstate mediated BK channel activation is located in the pore forming alpha channel subunit, around the Mg (2+) binding site."
24158430
reach
"This observation is in agreement with previous electrophysiological data and comparative structural analysis suggesting that tungstate modulates BK channel activity by direct binding to a site located at the BK alpha subunit (around residues of the voltage sensor and the RCK1 domains that coordinate the binding of Mg 2+) [XREF_BIBR], with the required participation of beta 1 subunit extracellular loop residues that stabilize the active configuration of BK channel voltage sensor [XREF_BIBR]."
25659150
reach
"On the contrary, at micromolar levels (100 muM) tungstate still promotes voltage dependent activation of the vascular (beta 1 subunit containing) BK channel without reducing K + current amplitude."
25659150