Proteomics

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Prolyl 4-hydroxylase alpha-2 directly activates mTOR kinase

ABSTRACT: To identify candidate mTOR-interacting molecules, we performed an anti-Flag immunoprecipitation (IP) followed by mass spectrometry (MS)-based proteomic analysis in 293T cells overexpressing Flag-tagged mTOR. We identified P4HA2 binding proteins with anti-HA IP followed by (MS)-based proteomic analysis in 293T cells overexpressing HA-tagged P4HA2. To speculate that mTOR can be hydroxylated by P4HA2. We used 293T cells overexpressing Flag-mTOR, Flag-mTOR/HA-P4HA2, and Flag-mTOR/HA-P4HA2-overexpressing cells treated with EDHB, we conducted an anti-Flag IP to capture and enrich mTOR protein, and the immunoprecipitates were subjected to MS analysis.

ORGANISM(S): Homo Sapiens

SUBMITTER: Hongtao Zhang  

PROVIDER: PXD041531 | iProX | Fri Apr 14 00:00:00 BST 2023

REPOSITORIES: iProX

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Publications

P4HA2 activates mTOR via hydroxylation and targeting P4HA2-mTOR inhibits lung adenocarcinoma cell growth.

Jin Ersuo E   Wang Shengjie S   Chen Donglai D   Wang Jia-Ping JP   Zeng Yuanyuan Y   Sun Runfeng R   Zhang Hong-Tao HT  

Oncogene 20240423 24

Mammalian target of rapamycin (mTOR) kinase functions as a central regulator of cell growth and metabolism, and its complexes mTORC1 and mTORC2 phosphorylate distinct substrates. Dysregulation of mTOR signaling is commonly implicated in human diseases, including cancer. Despite three decades of active research in mTOR, much remains to be determined. Here, we demonstrate that prolyl 4-hydroxylase alpha-2 (P4HA2) binds directly to mTOR and hydroxylates one highly conserved proline 2341 (P2341) wit  ...[more]

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