NPGPx modulates CPEB2-controlled HIF-1α RNA translation in response to oxidative stress.

Abstract:

:Non-selenocysteine-containing phospholipid hydroperoxide glutathione peroxidase (NPGPx or GPx7) is an oxidative stress sensor that modulates the antioxidative activity of its target proteins through intermolecular disulfide bond formation. Given NPGPx's role in protecting cells from oxidative damage, identification of the oxidative stress-induced protein complexes, which forms with key stress factors, may offer novel insight into intracellular reactive oxygen species homeostasis. Here, we show that NPGPx forms a disulfide bond with the translational regulator cytoplasmic polyadenylation element-binding protein 2 (CPEB2) that results in negative regulation of hypoxia-inducible factor 1-alpha (HIF-1α) RNA translation. In NPGPx-proficient cells, high oxidative stress that disrupts this bonding compromises the association of CPEB2 with HIF-1α RNA, leading to elevated HIF-1α RNA translation. NPGPx-deficient cells, in contrast, demonstrate increased HIF-1α RNA translation under normoxia with both impaired induction of HIF-1α synthesis and blunted HIF-1α-programmed transcription following oxidative stress. Together, these results reveal a molecular mechanism for how NPGPx mediates CPEB2-controlled HIF-1α RNA translation in a redox-sensitive manner.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Chen PJ,Weng JY,Hsu PH,Shew JY,Huang YS,Lee WH

doi

10.1093/nar/gkv1010

subject

Has Abstract

pub_date

2015-10-30 00:00:00

pages

9393-404

issue

19

eissn

0305-1048

issn

1362-4962

pii

gkv1010

journal_volume

43

pub_type

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