FAST Is a Survival Protein That Senses Mitochondrial Stress and Modulates TIA-1-Regulated Changes in Protein Expression

Li, Wei; Simarro, Marı́a; Kedersha, Nancy; Anderson, Paul

doi:10.1128/mcb.24.24.10718-10732.2004

Cited by 53 publications

(75 citation statements)

References 39 publications

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“…Consistent with the function of the FAST kinase acting as a survival protein is the finding that RNAi knockdown of FAST leads to apoptosis and that overexpression of FAST protects cells from apoptosis (23). In contrast with that of FAST, knockdown of FASTKD2 protects cells from apoptosis, while increased expression of FASTKD2 leads to apoptosis (Fig.…”

Section: Discussionsupporting

confidence: 69%

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A Novel Transcription Complex That Selectively Modulates Apoptosis of Breast Cancer Cells through Regulation of FASTKD2

Yeung

Das

Zhang

et al. 2011

Molecular and Cellular Biology

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We previously reported that expression of NRIF3 (nuclear receptor interacting factor-3) rapidly and selectively leads to apoptosis of breast cancer cells. DIF-1 (also known as interferon regulatory factor-2 binding protein 2 [IRF-2BP2]), the cellular target of NRIF3, was identified as a transcriptional repressor, and DIF-1 knockdown leads to apoptosis of breast cancer cells but not other cell types. Here, we identify IRF-2BP1 and EAP1 (enhanced at puberty 1) as important components of the DIF-1 complex mediating both complex stability and transcriptional repression. This interaction of DIF-1, IRF-2BP1, and EAP1 occurs through the conserved C4 zinc fingers of these proteins. Microarray studies were carried out in breast cancer cell lines engineered to conditionally and rapidly increase the levels of the death domain (DD1) region of NRIF3. The DIF-1 complex was found to repress FASTKD2, a putative proapoptotic gene, in breast cancer cells and to bind to the FASTKD2 gene by chromatin immunoprecipitation. FASTKD2 knockdown prevents apoptosis of breast cancer cells from NRIF3 expression or DIF-1 knockdown, while expression of FASTKD2 leads to apoptosis of both breast and nonbreast cancer cells. Thus, regulation of FASTKD2 by NRIF3 and the DIF-1 complex acts as a novel death switch that selectively modulates apoptosis in breast cancer.

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Section: Discussionsupporting

confidence: 69%

“…The original FAST kinase is an anti-apoptotic factor that is essential for cell survival (23). Consistent with the function of the FAST kinase acting as a survival protein is the finding that RNAi knockdown of FAST leads to apoptosis and that overexpression of FAST protects cells from apoptosis (23).…”

Section: Discussionmentioning

confidence: 91%

A Novel Transcription Complex That Selectively Modulates Apoptosis of Breast Cancer Cells through Regulation of FASTKD2

Yeung

Das

Zhang

et al. 2011

Molecular and Cellular Biology

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“…In human cells, proteins such as Fas-activated serine/threonine kinase (FAST) and prohibitin-2, both of which are apoptotic regulators normally resident within mitochondrial membranes, relocalize to stress granules during stress (Kedersha et al, 2005;Ohn et al, 2008). Indeed, FAST has been implicated as a possible scaffolding factor for stress granules and P-bodies (Kedersha et al, 2005) and, owing to physical and functional interactions with TIA-1, might serve as a sensor of mitochondrial stress that facilitates an appropriate posttranscriptional response (Li et al, 2004). In future work, it will be of interest to determine whether stress granules are induced in other conditions associated with mitochondrial dysfunction, including disease states such as diabetes mellitus and mitochondrial myopathies.…”

Section: Nan 3 Stress Granules and Mitochondrial Dysfunctionmentioning

confidence: 99%

Stress-specific composition, assembly and kinetics of stress granules in Saccharomyces cerevisiae

Buchan

Yoon

Parker

2011

Journal of Cell Science

227

245

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SummaryEukaryotic cells respond to cellular stresses by the inhibition of translation and the accumulation of mRNAs in cytoplasmic RNAprotein (ribonucleoprotein) granules termed stress granules and P-bodies. An unresolved issue is how different stresses affect formation of messenger RNP (mRNP) granules. In the present study, we examine how sodium azide (NaN 3 ), which inhibits mitochondrial respiration, affects formation of mRNP granules as compared with glucose deprivation in budding yeast. We observed that NaN 3 treatment inhibits translation and triggers formation of P-bodies and stress granules. The composition of stress granules induced by NaN 3 differs from that of glucose-deprived cells by containing eukaryotic initiation factor (eIF)3, eIF4A/B, eIF5B and eIF1A proteins, and by lacking the heterogeneous nuclear RNP (hnRNP) protein Hrp1. Moreover, in contrast with glucose-deprived stress granules, NaN 3 -triggered stress granules show different assembly rules, form faster and independently from P-bodies and dock or merge with P-bodies over time. Strikingly, addition of NaN 3 and glucose deprivation in combination, regardless of the order, always results in stress granules of a glucose deprivation nature, suggesting that both granules share an mRNP remodeling pathway. These results indicate that stress granule assembly, kinetics and composition in yeast can vary in a stress-specific manner, which we suggest reflects different rate-limiting steps in a common mRNP remodeling pathway.

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“…Cytoplasmic poly (A) mRNAs stalled in the translational initiation phase are sequestered in SGs and potentially protected from degradation until stress is released and normal protein synthesis can resume. SGs also can sequester signaling molecules important for apoptosis and contribute in this fashion to the protection of cells from stress (12,13).…”

mentioning

confidence: 99%

Syk Is Recruited to Stress Granules and Promotes Their Clearance through Autophagy

Krisenko¹,

Higgins

Ghosh

et al. 2015

Journal of Biological Chemistry

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Background: Syk associates with proteins that are found in stress granules. Results: Stress granules contain Syk, Grb7, and phosphotyrosine and persist in cells treated with inhibitors of autophagy. Conclusion: Syk is recruited to stress granules and promotes their clearance through autophagy. Significance: The regulation of both stress granule clearance and autophagy is important for the survival of cells exposed to external stress.

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FAST Is a Survival Protein That Senses Mitochondrial Stress and Modulates TIA-1-Regulated Changes in Protein Expression

Cited by 53 publications

References 39 publications

A Novel Transcription Complex That Selectively Modulates Apoptosis of Breast Cancer Cells through Regulation of FASTKD2

A Novel Transcription Complex That Selectively Modulates Apoptosis of Breast Cancer Cells through Regulation of FASTKD2

Stress-specific composition, assembly and kinetics of stress granules in Saccharomyces cerevisiae

Syk Is Recruited to Stress Granules and Promotes Their Clearance through Autophagy

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