Evidence map›Paper›PMID 22744009›Full record

ArticleAmerican journal of physiology. Cell physiology2012

Direct interaction of Plin2 with lipids on the surface of lipid droplets: a live cell FRET analysis.

Avery L McIntosh, Subramanian Senthivinayagam, Kenneth C Moon, Shipra Gupta, Joel S Lwande, Cameron C Murphy, Stephen M Storey, Barbara P Atshaves

Abstract read
In one paragraph

Article in American journal of physiology. Cell physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

42 citing papers in PubMed, 74 citations in OpenAlex.

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  14. Perilipins at a glance.Journal of cell science · 2022
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Avery L McIntoshDept. of Biochemistry and Molecular Biology, Michigan State Univ., East Lansing, MI 48824, USA.
Subramanian Senthivinayagam
Kenneth C Moon
Shipra Gupta
Joel S Lwande
Cameron C Murphy
Stephen M Storey
Barbara P Atshaves
Michigan State University · USTexas A&M University · US

Funding

Lipid droplet domains foster lipid storageR01DK070965 · NIDDK · TEXAS A&M AGRILIFE RESEARCH · PI ATSHAVES, BARBARA P · 2007 to 2011
$1.4M
Lipid droplet domains foster lipid storageR56DK070965 · NIDDK · TEXAS A&M UNIVERSITY SYSTEM · PI ATSHAVES, BARBARA P · 2005 to 2005
$73k
NIDDK NIH HHS DK-70965
6 · The paper itself

Abstract

Despite increasing awareness of the health risks associated with excess lipid storage in cells and tissues, knowledge of events governing lipid exchange at the surface of lipid droplets remains unclear. To address this issue, fluorescence resonance energy transfer (FRET) was performed to examine live cell interactions of Plin2 with lipids involved in maintaining lipid droplet structure and function. FRET efficiencies (E) between CFP-labeled Plin2 and fluorescently labeled phosphatidylcholine, sphingomyelin, stearic acid, and cholesterol were quantitated on a pixel-by-pixel basis to generate FRET image maps that specified areas with high E (>60%) in lipid droplets. The mean E and the distance R between the probes indicated a high yield of energy transfer and demonstrated molecular distances on the order of 44-57 Å, in keeping with direct molecular contact. In contrast, FRET between CFP-Plin2 and Nile red was not detected, indicating that the CFP-Plin2/Nile red interaction was beyond FRET proximity (>100 Å). An examination of the effect of Plin2 on cellular metabolism revealed that triacylglycerol, fatty acid, and cholesteryl ester content increased while diacylglycerol remained constant in CFP-Plin2-overexpressing cells. Total phospholipids also increased, reflecting increased phosphatidylcholine and sphingomyelin. Consistent with these results, expression levels of enzymes involved in triacylglycerol, cholesteryl ester, and phospholipid synthesis were significantly upregulated in CFP-Plin2-expressing cells while those associated with lipolysis either decreased or were unaffected. Taken together, these data show for the first time that Plin2 interacts directly with lipids on the surface of lipid droplets and influences levels of key enzymes and lipids involved in maintaining lipid droplet structure and function.

Indexed as

AnimalsCells, CulturedFibroblastsFluorescence Resonance Energy TransferHumansLipid MetabolismMembrane ProteinsMicePerilipin-2Protein BindingStructure-Activity RelationshipSurface PropertiesMembrane ProteinsPerilipin-2PLIN2 protein, humanPlin2 protein, mouse

Identifiers

PMID22744009
PMCPMC3469596
OpenAlexW2117222922

What OpenQuestion holds

Textmetadata
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.