IndraLab

Statements

BK binds KCNMA1. 6 / 6
| 6
sparser
"In vascular smooth muscle, association of BK β1 with slo1 increases the channel’s apparent Ca 2+ -sensitivity, which allows activation of BK channels at physiological negative voltages."
28012000
sparser
"To directly assess which subunit of BK Ca channels plays a critical role in the activation of BK Ca currents by daidzein, the human α-subunit of BK Ca channels was expressed in HEK293 cells to observe[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
20044987
sparser
"Hence, the data gave rise to the hypothesis that cholesterol’s control over BK Ca channel function involved direct interaction(s) between the sterol and the slo1 proteins, with the sensing of sterol presence by specific amino acids in the slo1 sequence."
36988883
sparser
"Since slo1 proteins often associate with various β subunits to form BK channels in vivo ( xref ; xref ; xref ; xref ; xref ; xref ; xref ; xref ; xref ) and it is known that β1 and β2 subunits affect apparent Ca 2+ sensitivity of the channel ( xref ; xref , xref ; xref ; xref ; xref ; xref ; xref , xref ; xref ; xref ; xref ), it will be interesting to examine if Mg 2+ -dependent activation is also affected by β subunits."
16344323
sparser
"To determine whether BK β1 TM1, TM2 or both are critical to provide the characteristic ion current phenotype of BK β1-containing BK channels, we combined surface protein biotinylation assays with patch-clamp studies under wide voltage and Ca 2+ i ranges (which included the values found in the SM myocyte under physiological conditions) on heteromeric BK complexes resulting from the association of rat cerebral artery SM slo1 (“cbv1”) with engineered BK β1."
25275635
sparser
"Ethanol binds to the slo1 cytosolic Ca 2+ -sensing tail domain of BK channels only in the presence of Ca 2+ [ xref ]."
36431016