Reactome | eNOS associates with Caveolin-1

eNOS associates with Caveolin-1

Stable Identifier

R-HSA-203712

Type

Reaction [transition]

Species

Homo sapiens

Compartment

plasma membrane, lipid droplet

ReviewStatus

5/5

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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 (Garcia-Cardena et al. 1997; Ghosh et al. 1998).

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. Garcia-Cardena, G, Martasek, P, Masters, BS, Skidd, PM, Couet, J, Li, S, Lisanti, MP, Sessa, WC	J Biol Chem	1997
8798458	Endothelial nitric oxide synthase targeting to caveolae. Specific interactions with caveolin isoforms in cardiac myocytes and endothelial cells. Feron, O, Belhassen, L, Kobzik, L, Smith, TW, Kelly, RA, Michel, T	J Biol Chem	1996
9712842	Interaction between caveolin-1 and the reductase domain of endothelial nitric-oxide synthase. Consequences for catalysis. Ghosh, S, Gachhui, R, Crooks, C, Wu, C, Lisanti, MP, Stuehr, DJ	J Biol Chem	1998
11498544	Loss of caveolae, vascular dysfunction, and pulmonary defects in caveolin-1 gene-disrupted mice Drab, M, Verkade, P, Elger, M, Kasper, M, Lohn, M, Lauterbach, B, Menne, J, Lindschau, C, Mende, F, Luft, FC, Schedl, A, Haller, H, Kurzchalia, TV	Science	2001