IndraLab

Statements

CAV1 binds KCNMA1. 7 / 10
2 | 1 4
sparser
"Here, we hypothesized that the MaxiK alpha-subunit (Slo1) and caveolin-1 may interact with each other."
18079116
reach
"Therefore, Ca 2+ -dependent activation of a KCa1.1 and Cav complex depends strongly on interchannel distance and is sensitive to even small differences in separation, with the largest effect on Cav3 as compared with Cav2.2 containing complexes (XREF_FIG)."
23928916
biogrid
No evidence text available
15703204
sparser
"Caveolin-1 associates with Slo and may direct the channels to caveolae xref ."
22194818
sparser
"Because the caveolin-1 scaffolding domain is juxtamembrane, it is tempting to suggest that Slo1-caveolin-1 interaction facilitates the tethering of the Slo1 C-terminal end to the membrane."
18079116
biogrid
No evidence text available
15703204
sparser
"Moreover, a physical interaction between Cav-1 and BK channel proteins was confirmed by in vitro binding assay using GST-Cav-1 fusion proteins, showing that BK α-subunits directly interact with the Cav-1 scaffolding domains and producing an inhibitory effect on BK channel functions."
28955251