The UV response involving the ras signaling pathway and AP-1 transcription factors is conserved between yeast and mammals

Engelberg, David; Klein, Charles; Martinetto, Horacio; Struhl, Kevin; Karin, Michael

doi:10.1016/0092-8674(94)90153-8

Cited by 214 publications

(158 citation statements)

References 63 publications

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“…This suggests that UV light interferes with IFN␥-induced tyrosine phosphorylation of STAT1, thereby preventing activation of the GAS element in the IRF-1 promoter by IFN␥. UV light is known to activate several transcription factors including NF-B or AP-1 (18)(19)(20)(21), thus the present findings indicate that UV light can affect transcription activators in a negative regulatory way and may do so by interfering with phosphorylation. At present, the sequences of six mammalian STAT family members have been reported (8).…”

Section: Uv Light Inhibits Activation Of the Gas Element By Ifn␥mentioning

confidence: 87%

“…Like other adverse agents (alkylating chemicals, oxidants), UV light induces changes in mammalian gene expression (31)(32)(33). Induction of gene expression depends on the activation of specific transcription factors, including activation of NF-B and AP-1 (18)(19)(20)(21). Among a variety of others, genes encoding for cytokines are induced by UV light, ultimately resulting in the release of the majority of these mediators.…”

Section: Discussionmentioning

confidence: 99%

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Down-regulation of interferon γ-activated STAT1 by UV light

Aragane¹,

Kulms²,

Luger³

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

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STAT1 is a cytoplasmic transcription factor that is phosphorylated by Janus kinases (Jak) in response to interferon-␥ (IFN␥). Phosphorylated STAT1 translocates to the nucleus, where it turns on specific sets of IFN␥-inducible genes. Here, we show that UV light interferes with tyrosine phosphorylation of STAT1, thereby hindering IFN␥ from exerting its biological effects. This effect is not due to a down-regulation of the IFN␥ receptor because phosphorylation of upstream-located Jak1 and Jak2 was not suppressed by UV light. In contrast, UV light had no effect on the phosphorylation of STAT3, which is activated by the proinf lammatory cytokine interleukin 6. The UV light effect on STAT1 phosphorylation could be antagonized by vanadate, indicating at least partial involvement of a protein tyrosine phosphatase. Therefore, this study indicates a mechanism by which UV light can inhibit gene activation and suggests STAT1 as a new extranuclear UV target closely located to the membrane.

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Section: Uv Light Inhibits Activation Of the Gas Element By Ifn␥mentioning

confidence: 87%

Section: Discussionmentioning

confidence: 99%

Down-regulation of interferon γ-activated STAT1 by UV light

Aragane¹,

Kulms²,

Luger³

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

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“…Activation of these transcription factors by UV is mediated through oxidative stress and/or DNA damage and cRas is a component in the signal transduction pathway (Engelberg et al, 1994;Devary et al, 1991Devary et al, , 1993. We have shown earlier that stimulation of activated Ras expression leads also to increased Egr-1 expression (Huang et al, 1994b).…”

Section: Introductionmentioning

confidence: 99%

“…In bacteria, UV activates the SOS response which is characterized by a number of phenotypic changes including enhanced capacity for DNA repair as well as mutagenesis, inhibition of cell division and prophage induction (Holbrook and Fornace, 1991). In mammalian cells, the UV response has been demonstrated to suppress the immune response (Kripke, 1994) in addition to serving a protective function against UV damage (Devary et al, 1992;Engelberg et al, 1994;Holbrook and Fornace, 1991;Lu and Lane, 1993). However, precise mechanisms for any protective function are unknown, although cell cycle arrest (Wang and Ellem, 1994;Orren et al, 1995;DiLeonardo et al, 1994;El-Deiry et al, 1994), DNA repair and the apoptotic process (Caelles et al, 1994;Lowe et al, 1993) are receiving a great deal of attention.…”

Section: Introductionmentioning

confidence: 99%

Egr-1 inhibits apoptosis during the UV response: correlation of cell survival with Egr-1 phosphorylation

et al. 1998

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UV irradiation of normal or immortalized cells induces a rapid increase in the expression of several transcription factors and is thought to serve a protective function. The human fibrosarcoma cell line, HT1080 clone H4, expresses almost undetectable levels of Egr-1 and does not respond to UV-C irradiation by the induction of Egr-1. The H4 cells are hypersensitive to UV which induces apoptosis and reduces clonogenicity. The introduction of exogenous Egr-1 into H4 (H4E9 and H4E4 cell-lines) confers protection from UV damage as measured by a number of assays. In both NIH3T3 (with inducible Egr-1) and H4E9 (constitutive Egr-1) cells, UV irradiation gave enhanced transactivation of Egr-1 reporters that correlated with phosphorylated Egr-1. Studies using inhibitors indicated that protein kinase-C and tyrosine kinases are involved in the anti-apoptotic effects of Egr-1 after UV damage. This is the first description of a biological effect of phosphorylated Egr-1.

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“…It was reported that UV irradiation stimulates MAP kinases in higher plant 26) , budding yeast cells 7) and mammalian cells 5) . It has been well documented that UV irradiation causes genotoxic stress from DNA damage and the production of free radicals by exciting electrons of various biomolecules leading to oxidative stress.…”

Section: Resultsmentioning

confidence: 99%

Identification of a 40 kDa Protein Kinase Activated by Stress in a Halotolerant Green Alga Dunaliella tertiolecta.

Yuasa

2002

Microb. Environ.

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Activation of a 40 kDa protein kinase in Dunaliella tertiolecta was detected by in-gel kinase assay when the cells were subjected to various forms of stress, such as heat shock, acidic stress and H 2 O 2 . The substrate specificity of the 40 kDa kinase resembles that of HAP kinase (high osmotic pressure-activated protein kinase). An anti-phosphotyrosine monoclonal antibody did not co-precipitate with the 40 kDa kinase in the cell extracts of Dunaliella subjected to stress. Treatment of Dunaliella cells with mastoparan or AlF 4 -, trimeric G-protein activators, stimulated another protein kinase with a relative molecular mass of 46 kDa. This protein kinase has a different substrate specificity from that of HAP kinase and the stress-activated 40 kDa kinase. These results suggest that the stress-activated 40 kDa kinase is closely related to HAP kinase and that the 46 kDa kinase is associated with a putative trimeric G-protein.Key words: Dunaliella, green alga, protein kinase, environmental stress, heat shockThe halotolerant green alga Dunaliella tertiolecta can grow in a medium containing 0.1 to 5 M NaCl. These cells do not have a rigid cell wall and, when subjected to hypo-or hyperosmotic shock, temporarily change shape and volume by regulating the intracellular glycerol content. Recent study implies that enzyme activation via regulatory cofactors or chemical modifications such as phosphorylation/ dephosphorylation may participate in the osmotic stress signaling of Dunaliella 36) .It has been reported that various forms of environmental stress including high osmolarity, heat shock, acidic stress and oxidative stress, induce the activation of corresponding protein kinases, HOG1 in budding yeast cells 21) and MAPKAPkinase-2 20) and SAP kinase/c-Jun kinase 13) in mammalian cells. Recently, evidence has been accumulating that particular protein kinases in plant cells are also activated in response to various environmental stress and phytohormones 10,25) .It was demonstrated that protein phosphorylation is involved in the signal transduction of the halotolerant green alga Dunaliella tertiolecta in response to hypo-and hyperosmotic stress 33,35) . In vivo 32 P-phosphate-labeling experiments using D. tertiolecta cells indicated that hypoosmotic shock causes the transient phosphorylation of the microsomal proteins at 28-33 kDa 36) . A previous study with aequorin, a calcium luminescense protein, and a neutralizing antibody against Dunaliella CDPK (Calcium-Dependent Protein Kinase) indicated that intracellular calcium and CDPK have pivotal roles in the osmoregulation of green algal cells 32) . Hyperosmotic shock rapidly stimulates HAP kinase (High osmotic pressure-Activated Protein kinase) with a relative molecular mass of 40 kDa in Dunaliella cells, while hypoosmotic shock activates LAP kinase (Low osmotic pressure-Activated Protein kinase) of 40 kDa 33) . HAP kinase is regulated by phosphorylation status on its polypeptide and composed of protein kinase cascades involved in the osmosensing system of Dunaliella cells. It has

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The UV response involving the ras signaling pathway and AP-1 transcription factors is conserved between yeast and mammals

Cited by 214 publications

References 63 publications

Down-regulation of interferon γ-activated STAT1 by UV light

Down-regulation of interferon γ-activated STAT1 by UV light

Egr-1 inhibits apoptosis during the UV response: correlation of cell survival with Egr-1 phosphorylation

Identification of a 40 kDa Protein Kinase Activated by Stress in a Halotolerant Green Alga Dunaliella tertiolecta.

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