Phosphorylation of Nox1 regulates association with NoxA1 activation domain.

ABSTRACT:

Rationale

Activation of Nox1 initiates redox-dependent signaling events crucial in the pathogenesis of vascular disease. Selective targeting of Nox1 is an attractive potential therapy, but requires a better understanding of the molecular modifications controlling its activation.

Objective

To determine whether posttranslational modifications of Nox1 regulate its activity in vascular cells.

Methods and results

We first found evidence that Nox1 is phosphorylated in multiple models of vascular disease. Next, studies using mass spectroscopy and a pharmacological inhibitor demonstrated that protein kinase C-beta1 mediates phosphorylation of Nox1 in response to tumor necrosis factor-α. siRNA-mediated silencing of protein kinase C-beta1 abolished tumor necrosis factor-α-media

SUBMITTER: Streeter J 

PROVIDER: S-EPMC5025877 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature