IndraLab

Statements

ANK3 binds SCN5A. 19 / 19
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"Thus, an additional role for Nav-beta subunits to regulate the AnkG/Nav1.5/K ATP complex is a real but unexplored possibility."
31934859
sparser
"This site is highly conserved in ankyrin-binding motifs of sodium channels, and the E1053K mutation blocks binding activity of Nav1.5 to 190 kDa ankyrin-G. Interestingly, the E1053K mutation prevented[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
18083066
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"Co-immunoprecipitation experiments were used to test the Nav1.5-ankyrin-G interaction and Nav1.5-dystrophin interaction."
30233406
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"In vitro binding assays show that the p. E1053K variant disrupts the interaction between Nav1.5 and ankyrin-G resulting in abnormal targeting in myocytes.18 Interestingly, Ankyrin variants have also been found in two young, unrelated individuals with VF storm due to possible ERS, one of them with a family history of SCD."
33324992
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"E1053K variant disrupts the interaction between Nav1.5 and ankyrin-G resulting in abnormal targeting in myocytes. xref Interestingly, Ankyrin variants have also been found in two young, unrelated individuals with VF storm due to possible ERS, one of them with a family history of SCD. xref In summary, as Ankyrins are a critical part of the sodium channel complex, the novel ANK3 variant could impair conduction via loss-of-sodium channel function xref which may contribute to disturbed depolarization in ERS."
33324992
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"Mutations in NaV1.5 that block binding to ankG are associated with the human condition Brugada syndrome [31] ."
19272819
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"An in vivo model with disrupted AnkG/Nav1.5/K ATP interaction would be ideal to address effects in cardiomyopathies or in clinically relevant arrhythmias."
31934859
sparser
"The underlying mechanisms involved the impairment of Nav1.5 trafficking, which could be regulated by the Nav1.5-ankyrin-G interaction and Nav1.5-dystrophin interaction."
30233406
sparser
"Furthermore, we observed less co-localization and weaker binding between Nav1.5 and ankyrin-G or dystrophin after the long-term treatments with amitriptyline, indicating the disrupted Nav1.5-ankyrin-G interaction and Nav1.5-dystrophin interaction induced by amitriptyline."
30233406
sparser
"Although there is a long distance between these two binding sites on the primary sequence, the spatial proximity may exist to provide the necessary conditions for amitriptyline to impair the interaction between Nav1.5 and ankyrin-G. On the other hand, we discovered that the long-term effect of amitriptyline could destroy the Nav1.5-dystrophin interaction."
30233406
sparser
"Such an in vivo model would also be able to address the question of whether disrupted AnkG/Nav1.5/K ATP interaction affects the ICD structure."
31934859
sparser
"Impaired Nav1.5 trafficking, regulated by Nav1.5-ankyrin-G and Nav1.5-dystrophin interaction, was suggested to be the mechanism related to such a long-term effect."
30233406
sparser
"A mutation in SCN5A (E1053K) discovered in a patient with BrS disrupts association of SCN5A with ankyrin-G, resulting in decreased I Na [ xref ]."
23557754
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"Co-immunoprecipitation experiments further testified that the combination of Nav1.5 and ankyrin-G or dystrophin was severely weakened after long-term treatments to amitriptyline, implying the failed interaction between Nav1.5 and ankyrin-G or dystrophin."
30233406
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"The mechanisms of BrS induced by amitriptyline were related to Nav1.5 trafficking and could be explained by the disrupted interaction of ankyrin-G, dystrophin and Nav1.5."
30233406
reach
"These results suggested that the interaction between Nav1.5 and ankyrin-G or dystrophin could be weakened by the long-term effect of amitriptyline."
30233406
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"As deduced from these findings, the novel mechanism responsible for the long-term blockade effect of amitriptyline on Nav1.5 was the impairment of Nav1.5 trafficking.Furthermore, we observed less co-localization and weaker binding between Nav1.5 and ankyrin-G or dystrophin after the long-term treatments with amitriptyline, indicating the disrupted Nav1.5-ankyrin-G interaction and Nav1.5-dystrophin interaction induced by amitriptyline."
30233406
reach
"Although there is a long distance between these two binding sites on the primary sequence, the spatial proximity may exist to provide the necessary conditions for amitriptyline to impair the interaction between Nav1.5 and ankyrin-G."
30233406
sparser
"For example, mutation of the ankyrin-binding motif of Nav1.5 results in a loss of binding of Nav1.5 with its intracellular target chaperon ankyrin G, leading to Brugada syndrome [137] ."
18992999