RT Journal Article
T1 S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities
A1 Martínez Ruiz, Antonio
A1 Villanueva, Laura
A1 González de Orduña, Cecilia
A1 López-Ferrer, Daniel
A1 Higueras, María Ángeles
A1 Tarín, Carlos
A1 Rodríguez Crespo, José Ignacio
A1 Vázquez, Jesús
A1 Lamas, Santiago
A2 Ignarro, Louis J.
AB Nitric oxide is implicated in a variety of signaling pathways in different systems, notably in endothelial cells. Some of its effects can be exerted through covalent modifications of proteins and, among these modifications, increasing attention is being paid to S-nitrosylation as a signaling mechanism. In this work, we show by a variety of methods (ozone chemiluminescence, biotin switch, and mass spectrometry) that the molecular chaperone Hsp90 is a target of S-nitrosylation and identify a susceptible cysteine residue in the region of the C-terminal domain that interacts with endothelial nitric oxide synthase (eNOS). We also show that the modification occurs in endothelial cells when they are treated with S-nitrosoL-cysteine and when they are exposed to eNOS activators. Hsp90 ATPase activity and its positive effect on eNOS activity are both inhibited by S-nitrosylation. Together, these data suggest that S-nitrosylation may functionally regulate the general activities of Hsp90 and provide a feedback mechanism for limiting eNOS activation.
SN 0027-8424
SN 1091-6490
YR 2005
FD 2005-06-03
LK https://hdl.handle.net/20.500.14352/102702
UL https://hdl.handle.net/20.500.14352/102702
LA eng
NO Plan Nacional de I+D+I, Ministerio de Ciencia y Tecnología
NO Comunidad Autónoma de Madrid
NO Ministerio de Sanidad y Consumo
DS Docta Complutense
RD 11 abr 2025