Two redox centers within Yap1 for H2O2 and thiol-reactive chemicals signaling

Azevedo, Dulce; Tacnet, Frédérique; Delaunay, A; Rodrigues-Pousada, Claudina; Toledano, Michel B.

doi:10.1016/s0891-5849(03)00434-9

Cited by 117 publications

(107 citation statements)

References 45 publications

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“…The Yap2 cCRD thus constitutes a bona fide Cd-sensing domain, as the homologous Yap1 domain. We also show that, as anticipated in the case of Yap1 [2], cCRD cysteine residues are crucial for sensing Cd, probably serving as binding site for the metal. The binding of Cd to cCRD cysteine residues probably modify the A wild type strain transformed with GFP-cCRDYap2, GFP-cCRDYap2 C356A GFP-cCRDYap2 C378A GFP-cCRDYap2 C387A GFP-cCRDYap2 C391A and GFPcCRDYap2 C356AC387A were assessed for its GFP staining before and after treatment with 1 mM Cd for 1 h. (B) Expression of FRM2 and GTT2.…”

Section: Discussionsupporting

confidence: 80%

“…Although sharing extensive similarity, especially in the cCRD, Yap1 and Yap2 are physiologically distinct. Yap1 responds to several stress signals such as H 2 O 2 , thiolreactive chemicals and Cd [2,31,32], which Yap2 does not respond to [9,26]. Yet, a role of Yap2 in Cd detoxification has been previously suggested, based on the effect of this agent to stimulate its transcriptional activity [26], and to promote its nuclear accumulation [28].…”

Section: Discussionmentioning

confidence: 99%

“…However, the Yap2 cCRD cannot substitute for the homologous Yap1 domain in H 2 O 2 responsiveness, confirming that two distinct mechanisms operate for Cd and H 2 O 2 sensing by Yap1 [2].…”

Section: Differential Activation Of Yap1 and Yap2 By CD And H 2 Omentioning

confidence: 95%

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The S. cerevisiae Yap1 and Yap2 transcription factors share a common cadmium‐sensing domain

et al. 2006

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Towards elucidating the function of Yap2, which remains unclear, we have taken advantage of the C-terminal homology between Yap1 and Yap2. Swapping domains experiments show that the Yap2 C-terminal domain functionally substitutes for the homologous Yap1 domain in the response to Cd, but not to H 2 O 2 . We conclude that specificity determinants of the Cd response are encoded within both Yap1 and Yap2 Cterminus, whereas those required for H 2 O 2 response are only present in the Yap1 C-terminus. Furthermore, our results identify FRM2 as Cd-responsive Yap2 target and indicate a possible role of this protein in regulating a metal stress response.

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Section: Discussionsupporting

confidence: 80%

Section: Discussionmentioning

confidence: 99%

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The S. cerevisiae Yap1 and Yap2 transcription factors share a common cadmium‐sensing domain

et al. 2006

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“…The yeast transcriptional factor Yap1 senses the intracellular redox state via its carboxy-terminal cysteine-rich domain (c-CRD) (17), and the structure of c-CRD has been reported to reflect the equilibrated and steady-state physiological redox status (1). The Redoxfluor C probe (C probe) contains a tandem repeat of the partial sequence for c-CRD (Yap1 601-650) (Fig.…”

Section: Development and Characterization Of Redoxfluor As A Redox Inmentioning

confidence: 99%

A Novel Fluorescent Sensor Protein for Visualization of Redox States in the Cytoplasm and in Peroxisomes

Yano

Oku

Akeyama

et al. 2010

Molecular and Cellular Biology

102

101

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Reactive oxygen species are generated within peroxisomes during peroxisomal metabolism. However, due to technological difficulties, the intraperoxisomal redox state remain elusive, and the effect of peroxisome deficiency on the intracellular redox state is controversial. A newly developed, genetically encoded fluorescence resonance energy transfer (FRET) probe, Redoxfluor, senses the physiological redox state via its internal disulfide bonds, resulting in a change in the conformation of the protein leading to a FRET response. We made use of Redoxfluor to measure the redox states at the subcellular level in yeast and Chinese hamster ovary (CHO) cells. In wild-type peroxisomes harboring an intact fatty acid ␤-oxidation system, the redox state within the peroxisomes was more reductive than that in the cytosol, despite the fact that reactive oxygen species were generated within the peroxisomes. Interestingly, we observed that the redox state of the cytosol of cell mutants for peroxisome assembly, regarded as models for a neurological metabolic disorder, was more reductive than that of the wild-type cells in yeast and CHO cells. Furthermore, Redoxfluor was utilized to develop an efficient system for the screening of drugs that moderate the abnormal cytosolic redox state in the mutant CHO cell lines for peroxisome assembly without affecting the redox state of normal cells.

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“…Several studies have demonstrated that Yap1p, a b-Zip protein belonging to the yeast Yap family of transcriptional regulators (Rodrigues-Pousada et al, 2004), plays a central role in sensing and modulating gene expression in response to several forms of oxidative stress (Alarco et al, 1997;Delaunay et al, 2000;Gasch et al, 2000;Lee et al, 1999;Dumond et al, 2000;Nguyen et al, 2001;Wemmie et al, 1994;1366 T. Nevitt, J. Pereira and C. Rodrigues-Pousada Azevedo et al, 2003). Yap1p-responsive genes typically contain within their promoter region a Yap-response element (YRE-TTAC/GTAA) encoding for most cellular proteins with antioxidant function and several membrane-associated drug efflux pumps .…”

Section: Introductionmentioning

confidence: 99%

YAP4 gene expression is induced in response to several forms of stress in Saccharomyces cerevisiae

Nevitt

Rodrigues-Pousada

2004

Yeast

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Exposure of Saccharomyces cerevisiae to several environmental insults, including conditions of oxidative, heavy metal, metalloid and heat stress, induces the expression of the YAP4 gene, previously shown to play a role in the response to hyperosmotic stress. Expression analyses in several mutant strains under pro-oxidant conditions have determined that YAP4 is regulated by the transactivators Yap1p and Msn2p. Mutation of either the Yap1p-response element (YRE), located at −517 bp from the ATG, or the most proximal stress response element (STRE) at −430 bp, is shown to strongly compromise YAP4 gene expression under these conditions. Furthermore, these two mutations in combination lead to a severe depletion of detectable mRNA levels, indicating interplay between the transcription factors Yap1p and Msn2p in the regulation of YAP4 transcription. Transcriptional activation of this gene reflects a concomitant increase in Yap4p protein levels that appear phosphorylated upon stress and negatively regulated by protein kinase A. Yap4p amino acid residues Ser89, Ser196 and Thr241 are shown to be required for protein phosphorylation and/or protein stability.

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Two redox centers within Yap1 for H2O2 and thiol-reactive chemicals signaling

Cited by 117 publications

References 45 publications

The S. cerevisiae Yap1 and Yap2 transcription factors share a common cadmium‐sensing domain

The S. cerevisiae Yap1 and Yap2 transcription factors share a common cadmium‐sensing domain

A Novel Fluorescent Sensor Protein for Visualization of Redox States in the Cytoplasm and in Peroxisomes

YAP4 gene expression is induced in response to several forms of stress in Saccharomyces cerevisiae

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