Glycerophosphocholine-dependent Growth Requires Gde1p (YPL110c) and Git1p in Saccharomyces cerevisiae

Fisher, Edward A.; Almaguer, Claudia; Holic̆, Roman; Griač, Peter; Patton‐Vogt, Jana

doi:10.1074/jbc.m507051200

Cited by 68 publications

(74 citation statements)

References 50 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Detailed analysis on the role of the SPX domain in other yeast proteins is missing, but virtually all other SPX domain-containing proteins have been associated with phosphate metabolism. This is the case for the CDK inhibitor Pho81, for the vacuole phosphate exporter Pho91, and for the glycerophosphocholine phosphodiesterase Gde1, whose enzymatic activity generates glycerol-phosphate to be utilised as a phosphate source [14]. The SPX domain is also present in Syg1, which additionally contains an EXS domain (see Glossary) ( Figure 1).…”

Section: The Association Between Spx Domains and Phosphate Metabolismmentioning

confidence: 99%

Eukaryotic Phosphate Homeostasis: The Inositol Pyrophosphate Perspective

Azevedo

Saiardi

2017

Trends in Biochemical Sciences

125

123

View full text Add to dashboard Cite

Section: The Association Between Spx Domains and Phosphate Metabolismmentioning

confidence: 99%

Eukaryotic Phosphate Homeostasis: The Inositol Pyrophosphate Perspective

Azevedo

Saiardi

2017

Trends in Biochemical Sciences

125

123

View full text Add to dashboard Cite

“…In addition, it has been shown that wild type yeast cells could use glycerophosphocholine as sole source of P for cell growth, with Gde1 and Git1 being required for this process, strengthening the function of Gde1 in scavenging Pi [61]. Surprisingly, several studies failed to detect any in vitro phosphodiesterase activity in cell lysates or fractions derived from wild type or GDE1 overexpressing strains, raising the hypothesis that phosphodiesterase activity was physically dependent on another protein [59,62]. Indeed, in addition to the SPX domain, which has been shown to be involved in protein interaction, Gde1, possesses ankyrins repeats, also involved in protein-protein interaction [37].…”

Section: Gde1 a Role In Scavenging Pimentioning

confidence: 99%

“…2, Table 1). Consequently, deletion and overexpression of GDE1 resulted in the accumulation and reduction of the intracellular levels of glycerophosphocholine, respectively [59]. Under optimal growth conditions, phosphatidylcholine, like other phospholipids, such as glycerophosphoinositol, can be excreted into the external medium and transported back into the cell upon nutritional stresses [60].…”

Section: Gde1 a Role In Scavenging Pimentioning

confidence: 99%

Phosphate homeostasis in the yeast Saccharomyces cerevisiae, the key role of the SPX domain‐containing proteins

et al. 2012

View full text Add to dashboard Cite

a b s t r a c tIn the yeast Saccharomyces cerevisiae, a working model for nutrient homeostasis in eukaryotes, inorganic phosphate (Pi) homeostasis is regulated by the PHO pathway, a set of phosphate starvation induced genes, acting to optimize Pi uptake and utilization. Among these, a subset of proteins containing the SPX domain has been shown to be key regulators of Pi homeostasis. In this review, we summarize the recent progresses in elucidating the mechanisms controlling Pi homeostasis in yeast, focusing on the key roles of the SPX domain-containing proteins in these processes, as well as describing the future challenges and opportunities in this fast-moving field.

show abstract

“…erophosphodiesterase, which cleaves GPC into glycerol-3-phosphate (G3P) and choline (20,21). Intracellular reutilization of GPC as a choline source is also partially dependent on Gde1 (16).…”

mentioning

confidence: 99%

Identification of a novel GPCAT activity and a new pathway for phosphatidylcholine biosynthesis in S. cerevisiae

Stålberg

Neal

Ronne

et al. 2008

Journal of Lipid Research

View full text Add to dashboard Cite

Turnover of phospholipids in the yeast Saccharomyces cerevisiae generates intracellular glycerophosphocholine (GPC). Here we show that GPC can be reacylated in an acylCoA-dependent reaction by yeast microsomal membranes. The lysophosphatidylcholine that is formed in this reaction is efficiently further acylated to phosphatidylcholine (PC) by yeast microsomes, thus providing a new pathway for PC biosynthesis that can either recycle endogenously generated GPC or utilize externally provided GPC. Genetic and biochemical evidence suggests that this new enzymatic activity, which we call GPC acyltransferase (GPCAT), is not mediated by any of the previously known acyltransferases in yeast. The GPCAT activity has an apparent V max of 8.7 nmol/min/mg protein and an apparent K m of 2.5 mM. It has a neutral pH optimum, similar to yeast glycerol-3-phosphate acyltransferase, but differs from the latter in being more heat stable. The GPCAT activity is sensitive to N-ethylmaleimide, phenanthroline, and Zn 21 ions. In vivo experiments showed that PC is efficiently labeled when yeast cells are fed with [ 3 H]choline-GPC, and that this reaction occurs also in pct1 knockout strains, where de novo synthesis of PC by the CDP-choline pathway is blocked.This suggests that GPCAT can provide an alternative pathway for PC biosynthesis in vivo.-Stålberg, K., A. C. Neal, H. Ronne, and U. Ståhl. Identification of a novel GPCAT activity and a new pathway for phosphatidylcholine biosynthesis in S. cerevisiae.

show abstract

Glycerophosphocholine-dependent Growth Requires Gde1p (YPL110c) and Git1p in Saccharomyces cerevisiae

Cited by 68 publications

References 50 publications

Eukaryotic Phosphate Homeostasis: The Inositol Pyrophosphate Perspective

Eukaryotic Phosphate Homeostasis: The Inositol Pyrophosphate Perspective

Phosphate homeostasis in the yeast Saccharomyces cerevisiae, the key role of the SPX domain‐containing proteins

Identification of a novel GPCAT activity and a new pathway for phosphatidylcholine biosynthesis in S. cerevisiae

Contact Info

Product

Resources

About