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: Contribution to journalArticle査読

2 被引用数 (Scopus)


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.

ジャーナルGenes to Cells
出版ステータス出版済み - 7 2018

All Science Journal Classification (ASJC) codes

  • 遺伝学
  • 細胞生物学


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