Evidence map›Paper›PMID 27248498›Full record

ArticlePloS one2016

Regulation of G0/G1 Switch Gene 2 (G0S2) Protein Ubiquitination and Stability by Triglyceride Accumulation and ATGL Interaction.

Bradlee L Heckmann, Xiaodong Zhang, Alicia M Saarinen, Jun Liu

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.5field-weighted citation impact, top 19% of its field
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

16 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
  2. Recent advances on the role of G0S2.Discover oncology · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Protein Quality Control and Lipid Droplet Metabolism.Annual review of cell and developmental biology · 2020
    Review
  10. Review
  11. Article
  12. Article
  13. Adipose Triglyceride Lipase Regulation: An Overview.Current protein & peptide science · 2018
    Review
  14. Article
  15. Establishing the lipid droplet proteome: Mechanisms of lipid droplet protein targeting and degradation.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017
    Review
  16. G0S2: A small giant controller of lipolysis and adipose-liver fatty acid flux.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017
    Review
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

4 authors at 1 institution in 1 country.

Bradlee L HeckmannDepartment of Biochemistry & Molecular Biology, Mayo Clinic College of Medicine, Scottsdale, Arizona, United States of America.
Xiaodong ZhangDepartment of Biochemistry & Molecular Biology, Mayo Clinic College of Medicine, Scottsdale, Arizona, United States of America.
Alicia M SaarinenDepartment of Biochemistry & Molecular Biology, Mayo Clinic College of Medicine, Scottsdale, Arizona, United States of America.
Jun LiuDepartment of Biochemistry & Molecular Biology, Mayo Clinic College of Medicine, Scottsdale, Arizona, United States of America.
Mayo Clinic in Arizona · US

Funding

Inhibition of ATGL-Mediated Lipolysis by G0S2R01DK089178 · NIDDK · UNIVERSITY OF KENTUCKY · PI LIU, JUN · 2010 to 2014
$1.7M
Regulation of Hepatic Lipid Accumulation and Insulin ResistanceR01DK109096 · NIDDK · MAYO CLINIC ROCHESTER · PI LIU, JUN · 2016 to 2019
$1.5M
G0S2: a dual-function regulator of lipid and energy metabolismR56DK089178 · NIDDK · MAYO CLINIC ARIZONA · PI LIU, JUN · 2015 to 2015
$125k
NIDDK NIH HHS R01 DK089178NIDDK NIH HHS R01 DK109096NIDDK NIH HHS R56 DK089178
6 · The paper itself

Abstract

Intracellular triglyceride (TG) hydrolysis or lipolysis is catalyzed by the key intracellular triglyceride hydrolase, adipose triglyceride lipase (ATGL). The G0/G1 Switch Gene 2 (G0S2) was recently identified as the major selective inhibitor of ATGL and its hydrolase function. Since G0S2 levels are dynamically linked and rapidly responsive to nutrient status or metabolic requirements, the identification of its regulation at the protein level is of significant value. Earlier evidence from our laboratory demonstrated that G0S2 is a short-lived protein degraded through the proteasomal pathway. However, little is currently known regarding the underlying mechanisms. In the current study we find that 1) protein degradation is initiated by K48-linked polyubiquitination of the lysine- 25 in G0S2; and 2) G0S2 protein is stabilized in response to ATGL expression and TG accumulation. Mutation of lysine-25 of G0S2 abolished ubiquitination and increased protein stability. More importantly, G0S2 was stabilized via different mechanisms in the presence of ATGL vs. in response to fatty acid (FA)-induced TG accumulation. Furthermore, G0S2 protein but not mRNA levels were reduced in the adipose tissue of ATGL-deficient mice, corroborating the involvement of ATGL in the stabilization of G0S2. Taken together our data illustrate for the first time a crucial multifaceted mechanism for the stabilization of G0S2 at the protein level.

Indexed as

G1 PhaseResting Phase, Cell Cycle3T3-L1 CellsAcyltransferasesAnimalsCell Cycle ProteinsLipaseMiceMice, Inbred C57BLMice, KnockoutProtein BindingTriglyceridesUbiquitinationAcyltransferasesCell Cycle ProteinsG0S2 protein, mouseLipasePNPLA2 protein, mouseTriglycerides

Identifiers

PMID27248498
PMCPMC4889065
OpenAlexW2417444435

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.