Proteomics

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EIF4E2 regulates GSK3b kinase activity


ABSTRACT: we found eIF4E2 regulates GSK3b kinase activity. And we performed the quantitative iTRAQ-based phosphoproteomic to identify phophosites regulated by eIF4E2-GSK3b pathway

ORGANISM(S): Homo Sapiens

SUBMITTER: Min Zhang  

PROVIDER: PXD024226 | iProX | Wed Feb 17 00:00:00 GMT 2021

REPOSITORIES: iProX

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Publications

Mammalian eIF4E2-GSK3β maintains basal phosphorylation of p53 to resist senescence under hypoxia.

Sun Lei L   Yang He H   He Dong D   Chen Jian J   Dong Zhiqiang Z   Luo Shaoxiang S   Liang Huiting H   Cao Yu Y   Cai Bingcheng B   Zhang Min M  

Cell death & disease 20220514 5


Hypoxia modulates senescence, but their physiological link remains unclear. Here, we found that eIF4E2, a hypoxia-activated translation initiation factor, interacted with GSK3β to maintain phosphorylation of p53, thus resisting senescence under hypoxia. RNA-binding protein RBM38 interacted with eIF4E to inhibit the translation of p53, but GSK3β-mediated Ser195 phosphorylation disrupted the RBM38-eIF4E interaction. Through investigation of RBM38 phosphorylation, we found that the eIF4E2-GSK3β pat  ...[more]

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