IndraLab

Statements


| 3 10

sparser
"A recent study has shown that, MOG1 also interacts with the cardiac sodium channel Nav1.5, regulating its Nav1.5 transport on the cell surface ( Zhou et al., 2016 )."

sparser
"The aim of this study is to perform systematic mutational and electrophysiological studies to identify the key structural elements involved in the interaction between MOG1 and Nav1.5 Loop II and determine the significance of this interaction to the pathogenesis of BrS."
| PMC

sparser
"Point mutation analysis defined the MOG1-Nav1.5 Loop II interaction domain to an 8-amino-acid domain of R1193-Y1200 of Nav1.5 Loop II."
| PMC

sparser
"Mutations R1193W, L1194M and Y1199S associated with BrS reduced the interaction between MOG1 and Nav1.5."
| PMC

sparser
"Mutations R1193W, L1194M and Y1199S weaken the interaction between Nav1.5 and MOG1, and reduce MOG1-enhanced cardiac sodium current densities."
| PMC

sparser
"Ankyrins, fibroblast growth factor homologous factor 1B, calmodulin, caveolin-3, Nedd4-like ubiquitin-protein ligases, dystrophin, syntrophin, glycerol 3-phosphate dehydrogenase 1-like protein (GPD1L), and RAN guanine nucleotide release factor (MOG1) can directly bind to Nav1.5 and regulate Na + channel transport, expression, and gating [ xref , xref , xref ]."

sparser
"Co-IP in lysates prepared from mouse neonatal cardiomyocytes also confirmed the association of MOG1 and SCN5A [ xref ]."

sparser
"Yu et al. used the heterologous systems HEK293 and tsA201 to mechanistically understand the interactions between MOG1 and Nav1.5 proteins."
| PMC

reach
"Point mutation analysis defined the MOG1-Nav1.5 Loop II interaction domain to an 8-amino-acid domain of R1193-Y1200 of Nav1.5 Loop II. Mutations R1193W, L1194M and Y1199S associated with BrS reduced the interaction between MOG1 and Nav1.5."
| PMC

reach
"Mutations R1193W, L1194M and Y1199S weaken the interaction between Nav1.5 and MOG1, and reduce MOG1-enhanced cardiac sodium current densities."
| PMC

sparser
"Mechanistic insights into the interaction of cardiac sodium channel Nav1.5 with MOG1 and a new molecular mechanism for Brugada syndrome."

sparser
"This suggests a functional impact of Q1000K on the Nav1.5-MOG1 interaction."

reach
"Ankyrins, fibroblast growth factor homologous factor 1B, calmodulin, caveolin-3, Nedd4-like ubiquitin-protein ligases, dystrophin, syntrophin, glycerol 3-phosphate dehydrogenase 1-like protein (GPD1L), and RAN guanine nucleotide release factor (MOG1) can directly bind to Nav1.5 and regulate Na channel transport, expression, and gating [75,76,77]."