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KCNA2 binds RHOA. 22 / 23
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biogrid
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sparser
"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."
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"Here, we report the interaction between RhoA and the delayed rectifier potassium channel Kv1.2."
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"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 pan[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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sparser
"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."
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"Does the association of RhoA with Kv1.2 have any physiological effect on ionic current generated by Kv1.2 channels?"
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"Physical interaction between RhoA and Kv1.2 channel indicates involvement of Kv1.2 channel in cell motility (Cachero et al., xref )."
26580832
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"RhoA coimmunoprecipitates Kv1.2 in the membrane ( Figure 1 B), suggesting that RhoA associates with Kv1.2 in its membrane-associated, GTP-bound state."
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"Therefore, RhoA binds to Kv1.2 preferentially in its activated, GTP-bound form."
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hprd
No evidence text available
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"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."
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"After verifying that RhoA interacts with Kv1.2, we next asked whether this interaction affects Kv1.2 physiology."
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"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 29[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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sparser
"Coimmunoprecipitation experiments confirmed that RhoA associates with Kv1.2."
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biogrid
No evidence text available
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sparser
"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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"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 i[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"In human embryonic kidney 293 cells overexpressing Kv1.2, immunoprecipitation using an anti-RhoA antibody revealed an association of RhoA with Kv1.2."
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"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 for[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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biogrid
No evidence text available
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sparser
"Therefore, the interaction between RhoA and Kv1.2 occurs in a native mammalian system."
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sparser
"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 [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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