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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)3888-3900
Number of pages13
JournalJournal of Biological Chemistry
Volume289
Issue number7
DOIs
Publication statusPublished - 2014 Feb 14
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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