IndraLab

Statements

SCN5A binds CAV3. 5 / 5
1 | 2 2
biogrid
No evidence text available
17060380
reach
"The exact residues of association between Cav-3 and SCN5A are not yet known, but many other interaction sites on Cav-3 have been implicated in association with other signaling proteins such as adenylyl cyclase and beta adrenergic receptors reflecting its importance as a structural member of the SCCP Cav-3 appears to be important in mediating adrenergic upregulation of cardiac I Na through G proteins [XREF_BIBR]."
23557754
sparser
"80 Moreover, missense variants in CAV3-encoded caveolin-3, which forms macromolecules with Nav1.5 and serves as a negative regulator for I Na,L , could result in I Na,L increase and thus cause LQTS9, providing new therapeutic strategies to correct I Na,L ."
| PMC
reach
"We also performed immunoprecipitation with FLAG antibody using a FLAG tagged SCN5A co-expressed with nNOS, SNTA1, and Cav3 (WT, F97C, or vector) in HEK cells and found that the complex remained intact with the mutant Cav3 (XREF_SUPPLEMENTARY) Taken together, these results demonstrate that nNOS, SCN5A and SNTA1 form a complex with Cav3 in the heart."
23541953
sparser
"Due to the complexity of signaling network in caveolar cardiac ion channels, we cannot exclude the possibilities that Cav3-F97C may disturb other signaling molecular complexes associated with Cav3 to have additional effects on SCN5A, or alter biophysical properties of other caveolar cardiac ion channels through specific signaling pathways to affect cellular electrophysiology."
23541953