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 language | English |
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Pages (from-to) | 3888-3900 |
Number of pages | 13 |
Journal | Journal of Biological Chemistry |
Volume | 289 |
Issue number | 7 |
DOIs | |
Publication status | Published - 2014 Feb 14 |
Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology