Reactome | AKT1 binds eNOS complex via HSP90

AKT1 binds eNOS complex via HSP90

Stable Identifier

R-HSA-202137

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol, plasma membrane

ReviewStatus

5/5

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AKT1 is recruited to the M domain of HSP90 (Fontana et al. 2002; Takahashi & Mendelsohn 2003).

Literature References

PubMed ID	Title	Journal	Year
11988487	Domain mapping studies reveal that the M domain of hsp90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release Fontana, J, Fulton, D, Chen, Y, Fairchild, TA, McCabe, TJ, Fujita, N, Tsuruo, T, Sessa, WC	Circ Res	2002
12799359	Synergistic activation of endothelial nitric-oxide synthase (eNOS) by HSP90 and Akt: calcium-independent eNOS activation involves formation of an HSP90-Akt-CaM-bound eNOS complex Takahashi, S, Mendelsohn, ME	J Biol Chem	2003