Dataset Information

Identification of NOS3 interacting proteins

ABSTRACT: The endothelial nitric oxide (NO) synthase (eNOS, or NOS3) can be activated in response to fluid shear stress and numerous agonists via cellular events such as increased intracellular Ca2+, interaction with substrate, co-factors as well as adaptor and regulatory proteins, protein phosphorylation and S-glutathionylation in addition to shuttling between distinct sub-cellular domains. While some protein interactors modulate enzymatic activity, others can be S-nitrosation targets, which are brought in close proximity to the NO source under specific conditions. The identification of proteins interacting with eNOS in human endothelial cells stimulated with serum and growth factors may provide new insight into the regulation of eNOS activity as well as NO signaling via S-nitrosation.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Ilka Wittig

LAB HEAD: Ingrid Fleming

PROVIDER: PXD013755 | Pride | 2021-09-08

REPOSITORIES: Pride

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Publications

Nitric oxide maintains endothelial redox homeostasis through PKM2 inhibition.

Siragusa Mauro M Thöle Janina J Bibli Sofia-Iris SI Luck Bert B Loot Annemarieke E AE de Silva Kevin K Wittig Ilka I Heidler Juliana J Stingl Heike H Randriamboavonjy Voahanginirina V Kohlstedt Karin K Brüne Bernhard B Weigert Andreas A Fisslthaler Beate B Fleming Ingrid I

The EMBO journal 20190722 17

Decreased nitric oxide (NO) bioavailability and oxidative stress are hallmarks of endothelial dysfunction and cardiovascular diseases. Although numerous proteins are S-nitrosated, whether and how changes in protein S-nitrosation influence endothelial function under pathophysiological conditions remains unknown. We report that active endothelial NO synthase (eNOS) interacts with and S-nitrosates pyruvate kinase M2 (PKM2), which reduces PKM2 activity. PKM2 inhibition increases substrate flux throu ...[more]

PMID: 31328803

Dataset Information

Identification of NOS3 interacting proteins

Publications

Nitric oxide maintains endothelial redox homeostasis through PKM2 inhibition.

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