<i>SLI1</i>(<i>YGR212W</i>) is a major gene conferring resistance to the sphingolipid biosynthesis inhibitor ISP-1, and encodes an ISP-1 N-acetyltransferase in yeast

Momoi, M.; Tanoue, Daisuke; Sun, Yidi; Takematsu, Hiromu; Suzuki, Yusuke; Suzuki, Minoru; Suzuki, Akemi; Fujita, Tetsuro; Kozutsumi, Yasunori

doi:10.1042/bj20040108

Cited by 33 publications

(25 citation statements)

References 49 publications

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“…The most negative genetic interactions of PMP3 are with FAB1, PIL1 and SLI1. The latter is an N-acetyltransferase, which confers resistance to the sphingolipid biosynthesis inhibitor myriocin by converting it into N-acetylmyriocin (Momoi et al, 2004). The genes that had an epistatic microarray profile that was most correlated to that of PMP3 are SLA1, RVS161 and RVS167.…”

Section: Discussionmentioning

confidence: 99%

The yeast Pmp3p has a significant role in plasma membrane organization

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Szopinska

Guerriat

et al. 2015

Journal of Cell Science

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Pmp3p-related proteins are highly conserved proteins that exist in bacteria, yeast, nematodes and plants, and its transcript is regulated in response to abiotic stresses, such as low temperature or high salinity. Pmp3p was originally identified in Saccharomyces cerevisiae, and it belongs to the sensitive to Na + (SNA)-protein family, which comprises four members -Pmp3p/Sna1p, Sna2p, Sna3p and Sna4p. Deletion of the PMP3 gene conferred sensitivity to cytotoxic cations, whereas removal of the other SNA genes did not lead to clear phenotypic effects. It has long been believed that Pmp3p-related proteins have a common and important role in the modulation of plasma membrane potential and in the regulation of intracellular ion homeostasis. Here, we show that several growth phenotypes linked to PMP3 deletion can be modulated by the removal of specific genes involved in sphingolipid synthesis. These genetic interactions, together with lipid binding assays and epifluorescence microscopy, as well as other biochemical experiments, suggest that Pmp3p could be part of a phosphoinositide-regulated stress sensor.

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Section: Discussionmentioning

confidence: 99%

The yeast Pmp3p has a significant role in plasma membrane organization

Block

Szopinska

Guerriat

et al. 2015

Journal of Cell Science

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“…Sphingolipids were metabolically labeled with [ 3 H]serine and extracted, then separated on TLC plates as described (8). Sphingolipid biosynthesis of Mss4-overexpressing cells (lanes 3 and 4), Rho2-overexpressiong cells (lanes 5 and 6) and wild-type cells (KMY1006) (lanes 1 and 2) in the presence (lanes 2, 4, and 6) or absence (lanes 1, 3, and 5) of 500 ng/ml ISP-1.…”

Section: Fig 3 Expression Of Mss4 Did Not Affect Sphingolipid Biosymentioning

confidence: 99%

“…We have recently succeeded in isolating multicopy suppressor genes against ISP-1 by titrating its concentration for treatment in yeast. One such gene, SLI1, encodes ISP-1-inactivating enzyme, accounting for its strong resistance activity (8). Other type of ISP-1-resistant gene, SLI2/YPK1, encodes a protein kinase.…”

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confidence: 99%

Disturbance of Sphingolipid Biosynthesis Abrogates the Signaling of Mss4, Phosphatidylinositol-4-phosphate 5-Kinase, in Yeast

Kobayashi

Takematsu

Yamaji

et al. 2005

Journal of Biological Chemistry

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The functional relationships between phosphoinositides and sphingolipids have not been well characterized to date. ISP-1/myriocin is a potent inhibitor of sphingolipid biosynthesis and induces severe growth defects in eukaryotic cells because of the sphingolipid deprivation. We characterized a novel multicopy suppressor gene of ISP-1-mediated cell death in yeast, MSS4. MSS4 encodes a phosphatidylinositol-4-phosphate 5-kinase that synthesizes phosphatidylinositol (4,5)-bisphosphate (PI4,5P 2 ). We demonstrate here that ISP-1 treatment of yeast causes defects both in the activity and subcellular localization of Mss4. The effect of the Mss4 defect on the downstream signaling was examined, because interaction between the Mss4 product, PI4,5P 2 , and the pleckstrin-homology domain of Rom2 mediates recruitment of Rom2 to the membrane, which is the crucial step for subsequent Rho1/2 activation. Indeed, failure of Rom2 recruitment was observed in ISP-1-treated cells as well as in csg2-deleted cells, which have reduced mannosylated inositolphosphorylceramide. These data suggested that proper sphingolipids are required for the signaling pathway involving Mss4.

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“…Pkh1 preferentially activates Ypk1 and Pkh2 preferentially activates Ypk2 (Roelants et al, 2002), and these two modules participate in signalling pathways necessary for maintenance of cell wall integrity (Roelants et al, 2002;Schmelzle et al, 2002) and for efficient endocytosis (deHart et al, 2002). These pathways respond to the level of sphingolipids in the plasma membrane (Momoi et al, 2004;Roelants et al, 2002;Sun et al, 2000). In vitro, Pkh1 and Pkh2 activity against physiological substrates is stimulated by nanomolar concentrations of the long-chain sphingoid base present in yeast, phytosphingosine (Friant et al, 2001;Zhang et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Differential roles of PDK1- and PDK2-phosphorylation sites in the yeast AGC kinases Ypk1, Pkc1 and Sch9

2004

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Saccharomyces cerevisiae Pkh1 and Pkh2 (orthologues of mammalian protein kinase, PDK1) are functionally redundant. These kinases activate three AGC family kinases involved in the maintenance of cell wall integrity: Ypk1 and Ypk2, two closely related, functionally redundant enzymes (orthologues of mammalian protein kinase SGK), and Pkc1 (orthologue of mammalian protein kinase PRK2). Pkh1 and Pkh2 activate Ypk1, Ypk2 and Pkc1 by phosphorylating a Thr in a conserved sequence motif (PDK1 site) within the activation loop of these proteins. A fourth protein kinase involved in growth control and stress response, Sch9 (orthologue of mammalian protein kinase c-Akt/PKB), also carries the conserved activation loop motif. Like other AGC family kinases, Ypk1, Ypk2, Pkc1 and Sch9 also carry a second conserved sequence motif situated in a region C-terminal to the catalytic domain, called the hydrophobic motif (PDK2 site). Currently, there is still controversy surrounding the identity of the enzyme responsible for phosphorylating this second site and the necessity for phosphorylation at this site for in vivo function. Here, genetic and biochemical methods have been used to investigate the physiological consequences of phosphorylation at the PDK1 and PDK2 sites of Ypk1, Pkc1 and Sch9. It was found that phosphorylation at the PDK1 site in the activation loop is indispensable for the essential functions of all three kinases in vivo, whereas phosphorylation at the PDK2 motif plays a non-essential and much more subtle role in modulating the ability of these kinases to regulate the downstream processes in which they participate.

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SLI1(YGR212W) is a major gene conferring resistance to the sphingolipid biosynthesis inhibitor ISP-1, and encodes an ISP-1 N-acetyltransferase in yeast

Cited by 33 publications

References 49 publications

The yeast Pmp3p has a significant role in plasma membrane organization

The yeast Pmp3p has a significant role in plasma membrane organization

Disturbance of Sphingolipid Biosynthesis Abrogates the Signaling of Mss4, Phosphatidylinositol-4-phosphate 5-Kinase, in Yeast

Differential roles of PDK1- and PDK2-phosphorylation sites in the yeast AGC kinases Ypk1, Pkc1 and Sch9

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