eNOS associates with Caveolin-1

Stable Identifier
Reaction [binding]
Homo sapiens
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Caveolin-1 is the primary negative regulatory protein for eNOS. Caveolin-1 binding to eNOS compromises its ability to bind Calmodulin (CaM), thereby inhibiting enzyme activity. The major binding region of caveolin-1 for eNOS is within amino acids 60-101 and to a lesser extent, amino acids 135-178.
Literature References
PubMed ID Title Journal Year
9325253 Dissecting the interaction between nitric oxide synthase (NOS) and caveolin. Functional significance of the nos caveolin binding domain in vivo.

Sessa, WC, Skidd, PM, Lisanti, MP, Masters, BS, Garcia-Cardena, G, Li, S, Martasek, P, Couet, J

J Biol Chem 1997
8798458 Endothelial nitric oxide synthase targeting to caveolae. Specific interactions with caveolin isoforms in cardiac myocytes and endothelial cells.

Michel, T, Kobzik, L, Belhassen, L, Smith, TW, Feron, O, Kelly, RA

J Biol Chem 1996
9712842 Interaction between caveolin-1 and the reductase domain of endothelial nitric-oxide synthase. Consequences for catalysis.

Crooks, C, Lisanti, MP, Gachhui, R, Ghosh, S, Wu, C, Stuehr, DJ

J Biol Chem 1998
11498544 Loss of caveolae, vascular dysfunction, and pulmonary defects in caveolin-1 gene-disrupted mice

Schedl, A, Kasper, M, Verkade, P, Elger, M, Luft, FC, Menne, J, Kurzchalia, TV, Lindschau, C, Lauterbach, B, Lohn, M, Haller, H, Mende, F, Drab, M

Science 2001
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