Evidence map›Paper›PMID 35017476›Full record

ArticleNature communications2022

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

Elite Possik, Clémence Schmitt, Anfal Al-Mass, Ying Bai, Laurence Côté, Johanne Morin, Heidi Erb, Abel Oppong, Wahab Kahloan, J Alex Parker and 2 more

Abstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed.

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  11. Application ofInternational journal of molecular sciences · 2023
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors.

Elite PossikDepartment of Nutrition, Université de Montréal, Montreal Diabetes Research Center, CRCHUM, Montréal, Canada.ORCID http://orcid.org/0000-0003-1578-5819
Clémence SchmittDepartment of Nutrition, Université de Montréal, Montreal Diabetes Research Center, CRCHUM, Montréal, Canada.ORCID http://orcid.org/0000-0003-3434-7718
Anfal Al-MassDepartment of Nutrition, Université de Montréal, Montreal Diabetes Research Center, CRCHUM, Montréal, Canada.ORCID http://orcid.org/0000-0003-1558-4734
Ying BaiDepartment of Nutrition, Université de Montréal, Montreal Diabetes Research Center, CRCHUM, Montréal, Canada.
Laurence CôtéDepartment of Nutrition, Université de Montréal, Montreal Diabetes Research Center, CRCHUM, Montréal, Canada.ORCID http://orcid.org/0000-0002-3674-4218
Johanne MorinDepartment of Nutrition, Université de Montréal, Montreal Diabetes Research Center, CRCHUM, Montréal, Canada.
Heidi ErbDepartment of Nutrition, Université de Montréal, Montreal Diabetes Research Center, CRCHUM, Montréal, Canada.
Abel OppongDepartment of Nutrition, Université de Montréal, Montreal Diabetes Research Center, CRCHUM, Montréal, Canada.ORCID http://orcid.org/0000-0002-8006-1537
Wahab KahloanDepartment of Nutrition, Université de Montréal, Montreal Diabetes Research Center, CRCHUM, Montréal, Canada.ORCID http://orcid.org/0000-0003-2628-1149
J Alex ParkerDepartment of Neurosciences, CRCHUM, Montréal, Canada.ORCID http://orcid.org/0000-0002-3333-2445
S R Murthy MadirajuDepartment of Nutrition, Université de Montréal, Montreal Diabetes Research Center, CRCHUM, Montréal, Canada. s.r.murthy.madiraju.chum@ssss.gouv.qc.ca.ORCID http://orcid.org/0000-0002-2613-2074
Marc PrentkiDepartment of Nutrition, Université de Montréal, Montreal Diabetes Research Center, CRCHUM, Montréal, Canada. marc.prentki@umontreal.ca.

Funding

CIHR
6 · The paper itself

Abstract

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.

Indexed as

Adaptation, PhysiologicalAmino Acid SequenceAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCaloric RestrictionEatingGene Expression RegulationGlucoseGlycerolGlycerol-3-Phosphate O-AcyltransferaseGlycerophosphatesHelminth ProteinsIsoenzymesLongevityOsmolar ConcentrationAcl-6 protein, C elegansalpha-glycerophosphoric acidCaenorhabditis elegans Proteinsfat-6 protein, C elegansGlucoseGlycerolglycerol-1-phosphataseGlycerol-3-Phosphate O-AcyltransferaseGlycerophosphatesHelminth ProteinsIsoenzymesPhosphoric Monoester HydrolasesStearoyl-CoA Desaturase

Identifiers

PMID35017476
PMCPMC8752807

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.