IndraLab

Statements

ATP inhibits IFIH1. 6 / 6
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"Biochemical analyses of gain-of-function variants have shown that mutations in the ATP binding site such as R337G increase the affinity of MDA5 for short dsRNAs in the presence of ATP by inhibiting ATP hydrolysis and hence ATP-dependent proofreading ."
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"Therefore, these data suggest that abundant ATP can prevent unwanted basal activation of apo MDA5 against unanchored K63-polyUb chains mainly via its hydrotropic function."
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"Mutations in the ATP binding pocket inhibit ATP hydrolysis without affecting filament formation, whereas those at the RNA interface increase the affinity or avidity of MDA5 for RNA ."
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"First, the CTD of the V protein can bind to the minimal V protein binding region (MVBR) of MDA5 and inhibit its ATP hydrolysis activity, thereby inhibiting the normal folding and aggregation of MDA5 to form a filamentous structure, which makes it unable to activate the downstream VISA/MAVS/IPS-1 complex (Motz et al., 2013; Mandhana et al., 2018)."
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"ΔHel1 MDA5 protein has functional ATPase activity following poly(I:C) stimulation, but compared with WT MDA5 protein, ATP hydrolysis was reduced, which may result in dampened signaling downstream of MDA5."
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"Based on these models of RIG-I and MDA5 described above, one may conclude that ATP hydrolysis negatively regulates the signaling activity of MDA5, while it is required for the RIG-I signaling activity."
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