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Phosphoglycolate phosphatase homologs act as glycerol-3-phosphate phosphatase to control stress and healthspan in C. elegans.

Authors:
Elite Possik Clémence Schmitt Anfal Al-Mass Ying Bai Laurence Côté Johanne Morin Heidi Erb Abel Oppong Wahab Kahloan J Alex Parker S R Murthy Madiraju Marc Prentki

Nat Commun 2022 01 11;13(1):177. Epub 2022 Jan 11.

Department of Nutrition, Université de Montréal, Montreal Diabetes Research Center, CRCHUM, Montréal, Canada.

Metabolic stress due to nutrient excess and lipid accumulation is at the root of many age-associated disorders and the identification of therapeutic targets that mimic the beneficial effects of calorie restriction has clinical importance. Here, using C. elegans as a model organism, we study the roles of a recently discovered enzyme at the heart of metabolism in mammalian cells, glycerol-3-phosphate phosphatase (G3PP) (gene name Pgp) that hydrolyzes glucose-derived glycerol-3-phosphate to glycerol. We identify three Pgp homologues in C. elegans (pgph) and demonstrate in vivo that their protein products have G3PP activity, essential for glycerol synthesis. We demonstrate that PGPH/G3PP regulates the adaptation to various stresses, in particular hyperosmolarity and glucotoxicity. Enhanced G3PP activity reduces fat accumulation, promotes healthy aging and acts as a calorie restriction mimetic at normal food intake without altering fertility. Thus, PGP/G3PP can be considered as a target for age-related metabolic disorders.

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http://dx.doi.org/10.1038/s41467-021-27803-6DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8752807PMC
January 2022

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Phosphoglycolate phosphatase homologs act as glycerol-3-phosphate phosphatase to control stress and healthspan in C. elegans.

Authors:
Elite Possik Clémence Schmitt Anfal Al-Mass Ying Bai Laurence Côté Johanne Morin Heidi Erb Abel Oppong Wahab Kahloan J Alex Parker S R Murthy Madiraju Marc Prentki

Nat Commun 2022 01 11;13(1):177. Epub 2022 Jan 11.

Department of Nutrition, Université de Montréal, Montreal Diabetes Research Center, CRCHUM, Montréal, Canada.

Metabolic stress due to nutrient excess and lipid accumulation is at the root of many age-associated disorders and the identification of therapeutic targets that mimic the beneficial effects of calorie restriction has clinical importance. Here, using C. elegans as a model organism, we study the roles of a recently discovered enzyme at the heart of metabolism in mammalian cells, glycerol-3-phosphate phosphatase (G3PP) (gene name Pgp) that hydrolyzes glucose-derived glycerol-3-phosphate to glycerol. Read More

View Article and Full-Text PDF
January 2022
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Comparative analysis on the key enzymes of the glycerol cycle metabolic pathway in Dunaliella salina under osmotic stresses.

Authors:
Hui Chen Yan Lu Jian-Guo Jiang

PLoS One 2012 4;7(6):e37578. Epub 2012 Jun 4.

College of Food Bioengineering, South China University of Technology, Guangzhou, China.

The glycerol metabolic pathway is a special cycle way; glycerol-3-phosphate dehydrogenase (G3pdh), glycerol-3-phosphate phosphatase (G3pp), dihydroxyacetone reductase (Dhar), and dihydroxyacetone kinase (Dhak) are the key enzymes around the pathway. Glycerol is an important osmolyte for Dunaliella salina to resist osmotic stress. In this study, comparative activities of the four enzymes in D. Read More

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October 2012
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Cloning and characterization of a putative human glycerol 3-phosphate permease gene (SLC37A1 or G3PP) on 21q22.3: mutation analysis in two candidate phenotypes, DFNB10 and a glycerol kinase deficiency.

Authors:
L Bartoloni M Wattenhofer J Kudoh A Berry K Shibuya K Kawasaki J Wang S Asakawa I Talior B Bonne-Tamir C Rossier J Michaud E R McCabe S Minoshima N Shimizu H S Scott S E Antonarakis

Genomics 2000 Dec;70(2):190-200

Division of Medical Genetics, University of Geneva Medical School and Cantonal Hospital of Geneva, Switzerland.

Using multiple exons trapped from human chromosome 21 (HC21)-specific cosmids with homology to a putative Arabidopsis thaliana glycerol 3-phosphate permease, we have determined the full-length cDNA sequence of a novel HC21 gene encoding a putative sugar-phosphate transporter (HGMW-approved symbol SLC37A1, aka G3PP). The predicted protein has 12 putative transmembrane domains and is also highly homologous to bacterial glpT proteins. The transcript was precisely mapped to 21q22. Read More

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December 2000
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