Genetic Regulation of Phospholipid Metabolism: Yeast as a Model Eukaryote

Henry, Susan A.; Patton‐Vogt, Jana

doi:10.1016/s0079-6603(08)60826-0

Cited by 158 publications

(294 citation statements)

References 246 publications

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“…It is unclear how Opi1p represses phospholipid biosynthesis, but it has been shown to repress INO1 transcription in the presence of inositol (Lai and McGraw, 1994;Lopes, 1995a, 1995b;Henry and Patton-Vogt, 1998). This result is consistent with the downregulation of OPI1 mRNA in p180-expressing cells.…”

Section: P180-induced Membrane Proliferation Appears Enhanced In Opi1mentioning

confidence: 99%

“…The transcription of INO1 and other phospholipid biosynthetic enzymes have been well characterized in yeast. Many of these genes are regulated by the intracellular concentration of free inositol and choline (see Greenberg and Lopes, 1996;Henry and Patton-Vogt, 1998 for review). When inositol and choline levels are low, a transcription factor complex composed of the basic helix-loop-helix (bHLH) proteins, Ino2p and Ino4p, activates the expression of many genes encoding phospholipid, fatty acid, and sterol biosynthetic enzymes.…”

Section: Introductionmentioning

confidence: 99%

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IN02, A Positive Regulator of Lipid Biosynthesis, Is Essential for the Formation of Inducible Membranes in Yeast

Block-Alper

Webster

Zhou

et al. 2002

MBoC

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Expression of the 180-kDa canine ribosome receptor inSaccharomyces cerevisiae leads to the accumulation of ER-like membranes. Gene expression patterns in strains expressing various forms of p180, each of which gives rise to unique membrane morphologies, were surveyed by microarray analysis. Several genes whose products regulate phospholipid biosynthesis were determined by Northern blotting to be differentially expressed in all strains that undergo membrane proliferation. Of these, the INO2 gene product was found to be essential for formation of p180-inducible membranes. Expression of p180 in ino2Δ cells failed to give rise to the p180-induced membrane proliferation seen in wild-type cells, whereas p180 expression in ino4Δ cells gave rise to membranes indistinguishable from wild type. Thus, Ino2p is required for the formation of p180-induced membranes and, in this case, appears to be functional in the absence of its putative binding partner, Ino4p.

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Section: P180-induced Membrane Proliferation Appears Enhanced In Opi1mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

IN02, A Positive Regulator of Lipid Biosynthesis, Is Essential for the Formation of Inducible Membranes in Yeast

Block-Alper

Webster

Zhou

et al. 2002

MBoC

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“…The most highly regulated of these is INO1, the gene encoding inositol-1-phosphate synthase, the rate-limiting enzyme in inositol biosynthesis (7). Cells starved for exogenous inositol, therefore, synthesize inositol de novo.…”

mentioning

confidence: 99%

Glycerophosphoinositol, a Novel Phosphate Source Whose Transport Is Regulated by Multiple Factors in Saccharomyces cerevisiae

Almaguer

Cheng

Nolder

et al. 2004

Journal of Biological Chemistry

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Git1p mediates the transport of the phospholipid metabolite, glycerophosphoinositol, into Saccharomyces cerevisiae. We report that phosphate limitation and inositol limitation affect GIT1 expression and Git1p transport activity via distinct mechanisms that involve multiple transcription factors. GIT1 transcript levels and Git1p activity are greater in cells starved for phosphate, with or without inositol limitation, than in cells only limited for inositol. Furthermore, the kinetics of GIT1 transcript accumulation and Git1p activity upon transfer of cells to phosphate starvation media are different from those obtained upon transfer of cells to inositolfree media. Pho2p and Pho4p are required for GIT1 expression and for Git1p transport activity under all growth conditions tested. In contrast, Ino2p and Ino4p are required for full GIT1 expression when inositol is limiting, with or without phosphate limitation, but not when only phosphate is limiting. Greatly reduced transport activity was detected in ino2⌬ and ino4⌬ cells under all growth conditions. A 300-base pair region of the GIT1 promoter containing potential Pho4p binding sites was shown to be required for full GIT1 expression. Git1p appears to act as a H ؉ -symporter, and neither inositol nor phosphate effectively compete with glycerophosphoinositol for transport by Git1p. Glycerophosphoinositol was shown previously to support the growth of an inositol auxotroph. Remarkably, we now report that glycerophosphoinositol can act as the sole source of phosphate for the cell, providing functional relevance for the regulation of Git1p transport activity by phosphate.

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“…The inositol response in yeast is known to be mediated by the Ino2p-Ino4p bHLH dimer, which regulates the phospholipid biosynthetic genes (Carman and Henry, 1999;Greenberg and Lopes, 1996;Henry and Patton-Vogt, 1998;Jesch et al, 2005;Robinson and Lopes, 2000a;Santiago and Mamoun, 2003). Therefore, the current study suggests that CIT2 expression is coordinated with phospholipid biosynthesis.…”

Section: Discussionmentioning

confidence: 65%

Multiple bHLH proteins regulate CIT2 expression in Saccharomyces cerevisiae

Chen¹,

Lopes²

2010

Yeast

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The basic helix-loop-helix (bHLH) proteins comprise a eukaryotic transcription factor family involved in multiple biological processes. They have the ability to form multiple dimer combinations and most of them also bind a 6 bp site (E-box) with limited specificity. These properties make them ideal for combinatorial regulation of gene expression. The Saccharomyces cerevisiae CIT2 gene, which encodes citrate synthase, was previously known to be induced by the bHLH proteins Rtg1p and Rtg3p in response to mitochondrial damage. Rtg1p-Rtg3p dimers bind two R-boxes (modified E-boxes) in the CIT2 promoter. The current study tested the ability of all nine S. cerevisiae bHLH proteins to regulate the CIT2 gene. The results showed that expression of CIT2-lacZ reporter was induced in a ρ 0 strain by the presence of inositol via the Ino2p and Ino4p bHLH proteins, which are known regulators of phospholipid synthesis. Promoter mutations revealed that inositol induction required a distal E-box in the CIT2 promoter. Interestingly, deleting the INO2, INO4 genes or the cognate E-box revealed phosphate induction of CIT2 expression. This layer of expression required the two R-boxes and the Pho4p bHLH protein, which is known to be required for phosphate-specific regulation. Lastly, the data show that the Hms1p and Sgc1p bHLH proteins also play important roles in repression of CIT2-lacZ expression. Collectively, these results support the model that yeast bHLH proteins coordinate different biological pathways.

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Genetic Regulation of Phospholipid Metabolism: Yeast as a Model Eukaryote

Cited by 158 publications

References 246 publications

IN02, A Positive Regulator of Lipid Biosynthesis, Is Essential for the Formation of Inducible Membranes in Yeast

IN02, A Positive Regulator of Lipid Biosynthesis, Is Essential for the Formation of Inducible Membranes in Yeast

Glycerophosphoinositol, a Novel Phosphate Source Whose Transport Is Regulated by Multiple Factors in Saccharomyces cerevisiae

Multiple bHLH proteins regulate CIT2 expression in Saccharomyces cerevisiae

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