[HTML][HTML] Reconstitution of an endothelial nitric-oxide synthase (eNOS), hsp90, and caveolin-1 complex in vitro: evidence that hsp90 facilitates calmodulin stimulated …
JP Gratton, J Fontana, DS O'Connor… - Journal of Biological …, 2000 - ASBMB
The activity of endothelial nitric-oxide synthase (eNOS) is regulated by its subcellular
localization, phosphorylation and through its interaction with different proteins. The
association of eNOS with caveolin-1 (Cav) is believed to maintain eNOS in an inactive state;
however, increased association of eNOS to heat shock protein 90 (hsp90) is observed
following activation. In this study, we investigate the relationship between caveolin and
hsp90 as opposing regulatory proteins on eNOS function. Immunoprecipitation of Cav-1 …
localization, phosphorylation and through its interaction with different proteins. The
association of eNOS with caveolin-1 (Cav) is believed to maintain eNOS in an inactive state;
however, increased association of eNOS to heat shock protein 90 (hsp90) is observed
following activation. In this study, we investigate the relationship between caveolin and
hsp90 as opposing regulatory proteins on eNOS function. Immunoprecipitation of Cav-1 …