[HTML][HTML] Deciphering the binding of caveolin-1 to client protein endothelial nitric-oxide synthase (eNOS): scaffolding subdomain identification, interaction modeling …
AE Trane, D Pavlov, A Sharma, U Saqib, K Lau… - Journal of biological …, 2014 - ASBMB
Caveolin-1 (Cav-1) gene inactivation interferes with caveolae formation and causes a range
of cardiovascular and pulmonary complications in vivo. Recent evidence suggests that
blunted Cav-1/endothelial nitric-oxide synthase (eNOS) interaction, which occurs specifically
in vascular endothelial cells, is responsible for the multiple phenotypes observed in Cav-1-
null animals. Under basal conditions, Cav-1 binds eNOS and inhibits nitric oxide (NO)
production via the Cav-1 scaffolding domain (CAV; amino acids 82–101). Although we have …
of cardiovascular and pulmonary complications in vivo. Recent evidence suggests that
blunted Cav-1/endothelial nitric-oxide synthase (eNOS) interaction, which occurs specifically
in vascular endothelial cells, is responsible for the multiple phenotypes observed in Cav-1-
null animals. Under basal conditions, Cav-1 binds eNOS and inhibits nitric oxide (NO)
production via the Cav-1 scaffolding domain (CAV; amino acids 82–101). Although we have …