N-terminal hydrophobic amino acids of activating transcription factor 5 (ATF5) protein confer interleukin 1β (IL-1β)-induced stabilization

Takanori Abe, Masaki Kojima, Satoshi Akanuma, Hiromi Iwashita, Takashi Yamazaki, Ryuichi Okuyama, Kenji Ichikawa, Mariko Umemura, Haruo Nakano, Shigeru Takahashi, Yuji Takahashi

研究成果: Article

5 引用 (Scopus)

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Background: The N-terminal region of ATF5 is responsible for its CdCl2- and NaAsO2-induced expression. Results: IL-1β stabilizes ATF5 protein and elevates the translation efficiency of ATF5 mRNA. Conclusion: The N-terminal hydrophobic amino acids of ATF5 are important for protein stabilization and responsiveness to IL-1β. Significance: This study provides new insights about the roles of ATF5 in immune response.

元の言語English
ページ(範囲)3888-3900
ページ数13
ジャーナルJournal of Biological Chemistry
289
発行部数7
DOI
出版物ステータスPublished - 2014 2 14
外部発表Yes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Abe, T., Kojima, M., Akanuma, S., Iwashita, H., Yamazaki, T., Okuyama, R., Ichikawa, K., Umemura, M., Nakano, H., Takahashi, S., & Takahashi, Y. (2014). N-terminal hydrophobic amino acids of activating transcription factor 5 (ATF5) protein confer interleukin 1β (IL-1β)-induced stabilization. Journal of Biological Chemistry, 289(7), 3888-3900. https://doi.org/10.1074/jbc.M113.491217