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Rabbit Anti-Glucose-6-Phosphate Dehydrogenase (G-6-PDH) Antibody, Unconjugated

RRID:AB_258454

Antibody ID

AB_258454

Target Antigen

Glucose-6-Phosphate Dehydrogenase (G-6-PDH) yeast, yeast

Proper Citation

(Sigma-Aldrich Cat# A9521, RRID:AB_258454)

Clonality

unknown

Comments

Vendor recommendations:

Host Organism

rabbit

Vendor

Sigma-Aldrich

Lipid Homeostasis Is Maintained by Dual Targeting of the Mitochondrial PE Biosynthesis Enzyme to the ER.

  • Friedman JR
  • Dev. Cell
  • 2018 Jan 22

Literature context:


Abstract:

Spatial organization of phospholipid synthesis in eukaryotes is critical for cellular homeostasis. The synthesis of phosphatidylcholine (PC), the most abundant cellular phospholipid, occurs redundantly via the ER-localized Kennedy pathway and a pathway that traverses the ER and mitochondria via membrane contact sites. The basis of the ER-mitochondrial PC synthesis pathway is the exclusive mitochondrial localization of a key pathway enzyme, phosphatidylserine decarboxylase Psd1, which generates phosphatidylethanolamine (PE). We find that Psd1 is localized to both mitochondria and the ER. Our data indicate that Psd1-dependent PE made at mitochondria and the ER has separable cellular functions. In addition, the relative organellar localization of Psd1 is dynamically modulated based on metabolic needs. These data reveal a critical role for ER-localized Psd1 in cellular phospholipid homeostasis, question the significance of an ER-mitochondrial PC synthesis pathway to cellular phospholipid homeostasis, and establish the importance of fine spatial regulation of lipid biosynthesis for cellular functions.

Funding information:
  • Intramural NIH HHS - Z01 HL005101-04(United States)

A Metabolic Function for Phospholipid and Histone Methylation.

  • Ye C
  • Mol. Cell
  • 2017 Apr 20

Literature context:


Abstract:

S-adenosylmethionine (SAM) is the methyl donor for biological methylation modifications that regulate protein and nucleic acid functions. Here, we show that methylation of a phospholipid, phosphatidylethanolamine (PE), is a major consumer of SAM. The induction of phospholipid biosynthetic genes is accompanied by induction of the enzyme that hydrolyzes S-adenosylhomocysteine (SAH), a product and inhibitor of methyltransferases. Beyond its function for the synthesis of phosphatidylcholine (PC), the methylation of PE facilitates the turnover of SAM for the synthesis of cysteine and glutathione through transsulfuration. Strikingly, cells that lack PE methylation accumulate SAM, which leads to hypermethylation of histones and the major phosphatase PP2A, dependency on cysteine, and sensitivity to oxidative stress. Without PE methylation, particular sites on histones then become methyl sinks to enable the conversion of SAM to SAH. These findings reveal an unforeseen metabolic function for phospholipid and histone methylation intrinsic to the life of a cell.

Funding information:
  • NCI NIH HHS - P30 CA142543()
  • NIGMS NIH HHS - R01 GM094314()