"Coimmunoprecipitation experiments confirmed that RhoA associates with Kv1.2."
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"To further define the interaction domain for RhoA binding to Kv1.2, we constructed a deletion mutant of Kv1.2 (Kv1.2-ΔN125) in which the distal 125 amino acids of the amino terminus were removed."
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"To test whether the physical association of RhoA with Kv1.2 is required for the RhoA-induced effect on Kv1.2 ionic current, we used a mutant channel deficient in RhoA binding."
"Our finding that amino-terminal truncated Kv1.2 channels fail to become significantly suppressed by overexpression of RhoA indicates that the physical association of RhoA with Kv1.2 is necessary for its effect on Kv1.2 physiology."
"In human embryonic kidney 293 cells overexpressing Kv1.2, immunoprecipitation using an anti-RhoA antibody revealed an association of RhoA with Kv1.2."
"Does the association of RhoA with Kv1.2 have any physiological effect on ionic current generated by Kv1.2 channels?"
"To confirm this finding, we performed in vitro binding experiments, which demonstrated that the GTP-bound form of RhoA associates with the amino terminus of Kv1.2 preferentially over the GDP-bound form ( Figure 1 C)."
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"Here, we report the interaction between RhoA and the delayed rectifier potassium channel Kv1.2."
"Since Kv1.2 is endogenously expressed in NG108-15 neuroblastoma cells ( Yokoyama et al. 1989 ), we asked whether we could detect interactions between RhoA and Kv1.2 in this native system."
"After verifying that RhoA interacts with Kv1.2, we next asked whether this interaction affects Kv1.2 physiology."
"Physical interaction between RhoA and Kv1.2 channel indicates involvement of Kv1.2 channel in cell motility (Cachero et al., xref )."
"Therefore, the interaction between RhoA and Kv1.2 occurs in a native mammalian system."
"Using whole-cell lysates from NG108-15 cells, immunoprecipitation with anti-RhoA monoclonal antibody revealed that endogenous RhoA associates with the endogenous Kv1.2 protein ( Figure 1 A, bottom panel)."
"To determine whether the interaction between Kv1.2 and RhoA is cytoplasmic or takes place at the membrane level, we performed coimmunoprecipitation experiments in a crude membrane preparation using 293 cells stably expressing Kv1.2."
"RhoA coimmunoprecipitates Kv1.2 in the membrane ( Figure 1 B), suggesting that RhoA associates with Kv1.2 in its membrane-associated, GTP-bound state."
"We show that RhoA physically associates with the amino terminus of Kv1.2, and electrophysiological analyses reveal that, in Xenopus laevis oocytes, overexpression of RhoA markedly reduces the ionic current generated by coexpressed Kv1.2 channels."
"Therefore, RhoA binds to Kv1.2 preferentially in its activated, GTP-bound form."
"Our finding that RhoA associates with the amino terminus of Kv1.2 in a two hybrid assay was confirmed in a series of immunoprecipitation experiments."