IndraLab

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SCN5A binds SNTA1. 11 / 14
2 1 | 4 7
sparser
"The reasons for this are not known, but it could be that there are additional regulatory components in the native myocytes that are regulating the interaction of SNTA1 and SCN5A. Alternatively, the stoichiometry of the transfected/infected components may be different between the two systems."
27028743
reach
"Since SCN5A is widely and definitively linked to DCM genetic architecture, and considering that a loss of interaction between SNTA1 and SCN5A could alter the sodium channel availability or biophysical properties, we can hypothesize that SNTA1 might contribute to the SCN5A-mediated phenotypes in DCM."
36292100
sparser
"Moreover, the functional studies for the complex SCN5A-SNTA1 (lacking both nNOS and PMCA4b) or SCN5A-SNTA1-nNOS complex (lacking PMCA4b) suggest that the three SNTA1 mutations do not cause increased late I Na by a direct interaction between SNTA1 and SCN5A or between SNTA1 and nNOS."
20009079
sparser
"The SNTA1 binds the motif of PDZ domain of Nav1.5."
35773684
sparser
"As a scaffold protein, SNTA1 binds to the C-terminal of Nav1.5 and played a vital regulatory role in Nav1.5 [ xref ]."
35773684
reach
"By using a GST-fusion protein of the C terminus of SCN5A, we showed that WT-SNTA1 interacted with SCN5A, nNOS, and PMCA4b."
18591664
sparser
"In a study by Ueda et al. [ xref ], it has been demonstrated that SNTA1 also interacts with SCN5A, connecting it to the nNOS–PMCA complex in the heart, and a missense mutation in SNTA1 disrupts the association between PMCA4b and SCN5A, leading to an increased late sodium current (I Na) in both a non-cardiomyocyte heterologous expression system and native cardiomyocytes [ xref ]."
36292100
sparser
"Since SCN5A is widely and definitively linked to DCM genetic architecture, and considering that a loss of interaction between SNTA1 and SCN5A could alter the sodium channel availability or biophysical properties, we can hypothesize that SNTA1 might contribute to the SCN5A-mediated phenotypes in DCM."
36292100
sparser
"A257G) which precipitated a marked increase in peak I Na and altered Nav1.5 channel kinetics in both HEK293 cells and cardiomyocytes through direct interaction of mutant SNTA1 with SCN5A. xref All these findings suggest that SNTA1 is a crucial Nav1.5 channel interacting protein (ChIP) involved in maintaining the normal function of the cardiac sodium channel."
24319568
reach
"Moreover, the functional studies for the complex SCN5A and SNTA1 (lacking both nNOS and PMCA4b) or SCN5A, SNTA1, and nNOS complex (lacking PMCA4b) suggest that the three SNTA1 mutations do not cause increased late I Na by a direct interaction between SNTA1 and SCN5A or between SNTA1 and nNOS."
20009079
reach
"The reasons for this are not known, but it could be that there are additional regulatory components in the native myocytes that are regulating the interaction of SNTA1 and SCN5A."
27028743