Evidence map›Paper›PMID 25737955›Full record

ArticleMolecular metabolism2015

Seipin oligomers can interact directly with AGPAT2 and lipin 1, physically scaffolding critical regulators of adipogenesis.

Md Mesbah Uddin Talukder, M F Michelle Sim, Stephen O'Rahilly, J Michael Edwardson, Justin J Rochford

Open access · goldAbstract read
In one paragraph

Article in Molecular metabolism, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
7.0field-weighted citation impact, top 3% 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

50 citing papers in PubMed, 90 citations in OpenAlex.

  1. Article
  2. Article
  3. Targeting Seipin to Alleviate Hepatic Steatosis in Zebrafish (Danio Rerio).Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  4. Article
  5. The Role of theInternational journal of molecular sciences · 2025
    Review
  6. Article
  7. Review
  8. Review
  9. Concept of lipid droplet biogenesis.European journal of cell biology · 2023
    Review
  10. Structure and function of lipid droplet assembly complexes.Current opinion in structural biology · 2023
    Review
  11. Seipin-still a mysterious protein?Frontiers in cell and developmental biology · 2023
    Review
  12. Lipid Droplet-a New Target in Ischemic Heart Disease.Journal of cardiovascular translational research · 2022
    Review
  13. Review
  14. Review
  15. Article
  16. Review
  17. Review
  18. Celia's Encephalopathy (Journal of clinical medicine · 2021
    Review
  19. Severe insulin resistance syndromes.The Journal of clinical investigation · 2021
    Review
  20. Journal of clinical medicine · 2021
    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

5 authors at 3 institutions in 1 country.

Md Mesbah Uddin TalukderDepartment of Pharmacology, University of Cambridge, Cambridge CB2 1PD, UK.
M F Michelle SimUniversity of Cambridge Metabolic Research Laboratories, Institute of Metabolic Science, Addenbrooke's Hospital, Cambridge CB2 0QQ, UK.
Stephen O'RahillyUniversity of Cambridge Metabolic Research Laboratories, Institute of Metabolic Science, Addenbrooke's Hospital, Cambridge CB2 0QQ, UK.
J Michael EdwardsonDepartment of Pharmacology, University of Cambridge, Cambridge CB2 1PD, UK.
Justin J RochfordRowett Institute of Nutrition and Health, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, UK.
University of Cambridge · GBAddenbrooke's Hospital · GBUniversity of Aberdeen · GB

Funding

Medical Research Council G0600717Medical Research Council G0800203Medical Research Council MC_UU_12012/5Medical Research Council MR/L002620/1Wellcome Trust 095515Wellcome Trust 100574
6 · The paper itself

Abstract

objectiveDisruption of the genes encoding either seipin or 1-acylglycerol-3-phosphate O-acyltransferase 2 (AGPAT2) causes severe congenital generalized lipodystrophy (CGL) in humans. However, the function of seipin in adipogenesis remains poorly defined. We demonstrated recently that seipin can bind the key adipogenic phosphatidic acid (PA) phosphatase lipin 1 and that seipin forms stable dodecamers. As AGPAT2 generates PA, the substrate for lipin 1, we investigated whether seipin might bind both enzymes of this lipid biosynthetic pathway, which is required for adipogenesis to occur.

methodsWe employed co-immunoprecipitation and immunofluorescence methods to determine whether seipin can interact with AGPAT2 and the consequences of this in developing adipocytes. Atomic force microscopy was used to determine whether these interactions involved direct association of the proteins and to define the molecular architecture of these complexes.

resultsOur data reveal that seipin can bind AGPAT2 during adipogenesis and that stabilizing this interaction during adipogenesis can increase the nuclear accumulation of PPARγ. Both AGPAT2 and lipin 1 can directly associate with seipin dodecamers, and a single seipin complex can simultaneously bind both AGPAT2 and lipin with a defined orientation.

conclusionsOur study provides the first direct molecular link between seipin and AGPAT2, two proteins whose disruption causes CGL. Moreover, it provides the first example of an interaction between seipin and another protein that causally influences a key aspect of adipogenesis. Together our data suggest that the critical role of seipin in adipogenesis may involve its capacity to juxtapose important regulators of this process in a multi-protein complex.

Indexed as

AdipocyteAdipogenesisAGPAT2Atomic force microscopy (AFM)BSCL2Lipid synthesisLipinLipodystrophySeipin

Identifiers

PMID25737955
PMCPMC4338318
OpenAlexW2158225793

What OpenQuestion holds

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Registered trials

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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.