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Measuring the dependence of the yeast heat shock response on intracellular pH during stress

ABSTRACT: Measuring the dependence of the yeast heat shock response on intracellular pH during stress

PROVIDER: PRJNA599929 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR10850801.fastq.gz	Fastqsanger.gz
	SRR10850802.fastq.gz	Fastqsanger.gz
	SRR10850803.fastq.gz	Fastqsanger.gz
	SRR10850804.fastq.gz	Fastqsanger.gz
	SRR10850805.fastq.gz	Fastqsanger.gz

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Measuring the dependence of the yeast heat shock response on intracellular pH during stress

Project description:S. cerevisiae cells acidify when they experience stressful temperatures. To determine whether this heat-shock associated acidification is important for the cellular response, we manipulated intracellular pH, heat shocked cells, and sequenced the transcriptome.

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Measuring the dependence of the yeast heat shock response on intracellular pH and translation during stress

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Measuring the dependence of the yeast heat shock response on intracellular pH and translation during stress

Project description:S. cerevisiae cells acidify when they experience stressful temperatures. In addition, newly-translated proteins are thought to misfold, triggering the heat shock response. To determine whether heat-shock associated acidification and translation state are important for the cellular response, we manipulated intracellular pH, blocked translation, heat shocked cells, and sequenced the transcriptome.

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Project description:Differences in global levels of histone acetylation occur in normal and cancer cells, although the reason cells regulate these levels has remained unclear. Here we demonstrate a role for histone acetylation in regulating intracellular pH (pHi). As pHi decreases, histones are globally deacetylated by histone deacetylases (HDACs) and the released acetate anions are co-exported with protons out of the cell by monocarboxylate transporters (MCTs), preventing further reductions in pHi. Conversely, global histone acetylation increases at more alkaline pHi, such as when resting cells are induced to proliferate. Inhibition of HDACs or MCTs decreases acetate export and lowers pHi, particularly compromising pHi maintenance in acidic environments. Global deacetylation at low pH is reflected at a genomic level by decreased abundance and extensive redistribution of acetylation at promoters and intergenic regions. Thus acetylation of chromatin functions as a rheostat to regulate pHi with important implications for therapeutic use of HDAC inhibitors. To investigate the redistribution of H4K16ac throughout the genome upon treatment at pH 6.5

2012-11-04 | E-GEOD-40114 | biostudies-arrayexpress

Histone acetylation regulates intracellular pH

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Regulation of intracellular pH by SLC4A7 tunes mTORC1 function to promote plasma cell differentiation

Project description:B cells differentiate into antibody-producing plasma cells, which are critical for humoral immunity, autoimmunity, and vaccine responses. Despite the importance of environmental stressors on regulating humoral immune responses, the influence of pH on PC differentiation has not been described. Here, we identified SLC4A7, a sodium/bicarbonate cotransporter, as a selective regulator of PC differentiation. SLC4A7 deletion impaired the formation of PCs and humoral immunity to influenza A virus infection in mice. Mechanistically, we find that SLC4A7 prevents acidification of intracellular pH and thus maintains lysosomal function and mTORC1 activity. Loss of SLC4A7 suppresses PC differentiation under conditions of extracellular acidosis in vitro and in a mouse model of metabolic acidosis. Here we reveal a novel relationship between the regulation of intracellular pH by SLC4A7 and mTORC1-dependent PC differentiation and humoral immunity.

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microarray analysis in SREBP2-knockdown cells under low pH (pH 6,8) culture conditions

Project description:The conditions of the tumor microenvironment, such as hypoxia and nutrient starvation, play critical roles in cancer progression. However, the role of acidic extracellular pH in cancer progression is not studied as extensively as that of hypoxia. Here, we show that extracellular acidic pH (pH 6.8) triggered activation of sterol regulatory element-binding protein 2 (SREBP2) by stimulating nuclear translocation and promoter binding to its targets along with intracellular acidification. Interestingly, inhibition of SREBP2, but not SREBP1, suppressed the upregulation of low pH-induced cholesterol biosynthesis-related genes. Moreover, acyl-CoA synthetase short-chain family member 2 (ACSS2), a direct SREBP2 target, provided a growth advantage to cancer cells under acidic pH. Furthermore, acidic pH-responsive SREBP2 target genes were associated with reduced overall survival of cancer patients. Thus, our findings show that SREBP2 is a key transcriptional regulator of metabolic genes and progression of cancer cells, partly in response to extracellular acidification.

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