Evidence map›Paper›PMID 38828991›Full record

ArticleMolecular and cellular biology2024

Regulation of PPARγ2 Stability and Activity by SHP-1.

Amit Kumar, Beisy Laborit Labrada, Marie-Hélène Lavallée-Bourget, Marie-Pier Forest, Michael Schwab, Kerstin Bellmann, Vanessa Houde, Nicole Beauchemin, Mathieu Laplante, André Marette

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular and cellular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Frontiers in pharmacology · 2024
    Article
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

10 authors.

Amit KumarCentre de recherche de l'Institut universitaire de cardiologie et de pneumologie de Québec (CRIUCPQ), Faculté de Médecine, Université Laval, Québec, QC, Canada.
Beisy Laborit LabradaCentre de recherche de l'Institut universitaire de cardiologie et de pneumologie de Québec (CRIUCPQ), Faculté de Médecine, Université Laval, Québec, QC, Canada.
Marie-Hélène Lavallée-BourgetCentre de recherche de l'Institut universitaire de cardiologie et de pneumologie de Québec (CRIUCPQ), Faculté de Médecine, Université Laval, Québec, QC, Canada.
Marie-Pier ForestCentre de recherche de l'Institut universitaire de cardiologie et de pneumologie de Québec (CRIUCPQ), Faculté de Médecine, Université Laval, Québec, QC, Canada.
Michael SchwabCentre de recherche de l'Institut universitaire de cardiologie et de pneumologie de Québec (CRIUCPQ), Faculté de Médecine, Université Laval, Québec, QC, Canada.
Kerstin BellmannCentre de recherche de l'Institut universitaire de cardiologie et de pneumologie de Québec (CRIUCPQ), Faculté de Médecine, Université Laval, Québec, QC, Canada.
Vanessa HoudeCentre de recherche de l'Institut universitaire de cardiologie et de pneumologie de Québec (CRIUCPQ), Faculté de Médecine, Université Laval, Québec, QC, Canada.
Nicole BeaucheminRosalind and Morris Goodman Cancer Research Centre, Departments of Oncology, Medicine and Biochemistry, McGill University, Montreal, QC, Canada.
Mathieu LaplanteCentre de recherche de l'Institut universitaire de cardiologie et de pneumologie de Québec (CRIUCPQ), Faculté de Médecine, Université Laval, Québec, QC, Canada.
André MaretteCentre de recherche de l'Institut universitaire de cardiologie et de pneumologie de Québec (CRIUCPQ), Faculté de Médecine, Université Laval, Québec, QC, Canada.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The protein tyrosine phosphatase Src homology region 2 domain-containing phosphatase-1 (SHP-1) plays an important role in modulating glucose and lipid homeostasis. We previously suggested a potential role of SHP-1 in the regulation of peroxisome proliferator-activated receptor γ2 (PPARγ2) expression and activity but the mechanisms were unexplored. PPARγ2 is the master regulator of adipogenesis, but how its activity is regulated by tyrosine phosphorylation is largely unknown. Here, we found that SHP-1 binds to PPARγ2 primarily via its N-terminal SH2-domain. We confirmed the phosphorylation of PPARγ2 on tyrosine-residue 78 (Y78), which was reduced by SHP-1 in vitro resulting in decreased PPARγ2 stability. Loss of SHP-1 led to elevated, agonist-induced expression of the classical PPARγ2 targets

Indexed as

AdipogenesisPPAR gammaProtein Tyrosine Phosphatase, Non-Receptor Type 63T3-L1 CellsAnimalsCD36 AntigensFatty Acid-Binding ProteinsHEK293 CellsHumansMicePhosphorylationProtein BindingProtein Stabilitysrc Homology DomainsCD36 AntigensFABP4 protein, humanFatty Acid-Binding ProteinsPPAR gammaProtein Tyrosine Phosphatase, Non-Receptor Type 6PTPN6 protein, humanadipogenesisPPARγ2protein stabilitySHP-1/PTPN6

Identifiers

PMID38828991
PMCPMC11253886

What OpenQuestion holds

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LicenceCC BY-NC
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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.