Nuclear–cytoplasmic shuttling protein PP2AB56 contributes to mTORC1-dependent dephosphorylation of FOXK1

Hirokazu Nakatsumi, Takeru Oka, Tsunaki Higa, Michiko Shirane, Keiichi I. Nakayama

研究成果: ジャーナルへの寄稿記事

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Mammalian target of rapamycin complex 1 (mTORC1) kinase is a master regulator of the cellular response to nutrition-related signals such as insulin and amino acids. mTORC1 is activated on the lysosomal membrane and induces phosphorylation of a variety of downstream molecules. We previously showed that activated mTORC1 induces protein phosphatase 2A (PP2A)-mediated dephosphorylation of the transcription factor forkhead box K1 (FOXK1). The mechanism underlying the signal transduction from the cytoplasmic mTORC1 to the nuclear FOXK1 has remained unclear, however, we now show that a nuclear–cytoplasmic transport system is necessary for the mTORC1-FOXK1 signal transduction. This reaction is mediated by a shuttling protein B56, which is a regulatory subunit of PP2A and plays an essential role in the mTORC1-dependent dephosphorylation of FOXK1. These results suggest that PP2AB56 phosphatase contributes to the signaling for mTORC1-dependent transcriptional regulation.

元の言語英語
ページ(範囲)599-605
ページ数7
ジャーナルGenes to Cells
23
発行部数7
DOI
出版物ステータス出版済み - 7 2018

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All Science Journal Classification (ASJC) codes

  • Genetics
  • Cell Biology

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