Cadmium interferes with the degradation of ATF5 via a post-ubiquitination step of the proteasome degradation pathway

Uekusa, Hiroyuki; Namimatsu, Mihoko; Hiwatashi, Yusuke; Akimoto, Takuya; Nishida, Tamotsu; Takahashi, Shigeru; Takahashi, Yûji

doi:10.1016/j.bbrc.2009.01.158

Cited by 18 publications

(20 citation statements)

References 17 publications

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“…We showed that CdCl 2 and NaAsO 2 exposure stabilizes ATF5 protein and increases ATF5 protein levels (9). Furthermore, we demonstrated that the N-terminal 21 amino acids of ATF5 protein serve as a destabilization domain in steady-state conditions and function as a stress response stabilization domain after CdCl 2 and NaAsO 2 exposure.…”

mentioning

confidence: 73%

N-terminal Hydrophobic Amino Acids of Activating Transcription Factor 5 (ATF5) Protein Confer Interleukin 1β (IL-1β)-induced Stabilization

Abe

Kojima

Akanuma

et al. 2014

Journal of Biological Chemistry

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Background:The N-terminal region of ATF5 is responsible for its CdCl 2 -and NaAsO 2 -induced expression. Results: IL-1␤ 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-1␤. Significance: This study provides new insights about the roles of ATF5 in immune response.

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confidence: 73%

N-terminal Hydrophobic Amino Acids of Activating Transcription Factor 5 (ATF5) Protein Confer Interleukin 1β (IL-1β)-induced Stabilization

Abe

Kojima

Akanuma

et al. 2014

Journal of Biological Chemistry

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“…Newman and Keating also reported that ATF5 acted as a C/EBPcbinding transcription factor in comprehensive protein array analysis [30]. ATF5 is a stress response transcription factor whose expression is regulated by posttranscriptional regulation [31], translational regulation [32,33] and post-translational regulation [34][35][36][37][38][39][40] in response to cellular stresses including endoplasmic reticulum (ER) stress [33,41], arsenite exposure [32,33,36] and amino acid limitation [31,32]. Limitation of a single amino acid (glutamine, methionine or leucine) in the cell culture medium increased ATF5 mRNA levels in HeLaS3 cells [31].…”

Section: Introductionmentioning

confidence: 99%

“…Cycloheximide, an inhibitor of translation, suppresses the glutamine limitation-induced increase in ATF5 mRNA [31], indicating that up-regulation of ATF5 mRNA depends on de novo protein synthesis. ATF5 is a target of ubiquitin-mediated [34,36,37,39,40] and caspase-mediated proteolysis [37,39], and its protein stability is up-regulated by stresses [36,37,39,40]. Recently, Liu et al found that the chaperone proteins HSP70 and nucleophosmin (NPM1) reciprocally regulate ATF5 protein stability [39].…”

Section: Introductionmentioning

confidence: 99%

The 5′‐untranslated region regulates ATF5 mRNA stability via nonsense‐mediated mRNA decay in response to environmental stress

et al. 2013

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We previously reported that activating transcription factor 5 (ATF5) mRNA increases in response to amino acid limitation, and that this increase is dependent on mRNA stabilization. The ATF5 gene allows transcription of mRNAs with two alternative 5′-UTRs, 5′-UTRa and 5′-UTRb, derived from exon 1a and exon 1b. 5′-UTRa contains the upstream open reading frames uORF1 and uORF2. Phosphorylation of eukaryotic initiation factor 2a during the integrated stress response had been previously shown to lead to bypassing of uORF2 translation and production of ATF5 protein. Translation of uORF2 is expected to result in translational termination at a position 125 nucleotides upstream of the exon junction, and this fits the criterion of a nonsense-mediated decay target mRNA. We investigated the potential role of 5′-UTRa in the control of mRNA stabilization, and found that 5′-UTRa reduced the stability of ATF5 mRNA. 5′-UTRa-regulated destabilization of mRNA was suppressed by knockdown of the nonsense-mediated decay factors Upf1 and Upf2. Mutation of the downstream AUG (uAUG2) rendered mRNA refractory to Upf1 and Upf2 knockdown. Moreover, 5′-UTRa-regulated down-regulation was hindered by amino acid limitation and tunicamycin treatment, and stressinduced phosphorylation of eukaryotic initiation factor 2a was involved in stabilization of ATF5 mRNA. These studies show that ATF5 mRNA is a naturally occurring normal mRNA target of nonsense-mediated decay, and provide evidence for linkage between stress-regulated translational regulation and the mRNA decay pathway. This linkage constitutes a mechanism that regulates expression of stress response genes.

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“…ATF5 was first identified as a partner of C/EBP␥ (26), and a recent study demonstrated that ATF5 associates with C/EBP␤ during 3T3-L1 differentiation (27). Several reports have suggested that ATF5 is inherently very unstable; however, it can be stabilized in response to a variety of stimuli, such as cisplatin (28), cadmium chloride (CdCl 2 ) (29), sodium arsenite (NaAsO 2 ) (30), and IL-1␤ (31).…”

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confidence: 99%

Stabilization of ATF5 by TAK1–Nemo-Like Kinase Critically Regulates the Interleukin-1β-Stimulated C/EBP Signaling Pathway

Zhang

et al. 2015

Molecular and Cellular Biology

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Cadmium interferes with the degradation of ATF5 via a post-ubiquitination step of the proteasome degradation pathway

Cited by 18 publications

References 17 publications

N-terminal Hydrophobic Amino Acids of Activating Transcription Factor 5 (ATF5) Protein Confer Interleukin 1β (IL-1β)-induced Stabilization

N-terminal Hydrophobic Amino Acids of Activating Transcription Factor 5 (ATF5) Protein Confer Interleukin 1β (IL-1β)-induced Stabilization

The 5′‐untranslated region regulates ATF5 mRNA stability via nonsense‐mediated mRNA decay in response to environmental stress

Stabilization of ATF5 by TAK1–Nemo-Like Kinase Critically Regulates the Interleukin-1β-Stimulated C/EBP Signaling Pathway

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