Evidence map›Paper›PMID 28800633›Full record

ArticlePloS one2017

Feeding-fasting dependent recruitment of membrane microdomain proteins to lipid droplets purified from the liver.

Kritika Sadh, Priyanka Rai, Roop Mallik

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.6field-weighted citation impact, top 32% 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

15 citing papers in PubMed, 19 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Imaging and proteomics toolkits for studying organelle contact sites.Frontiers in cell and developmental biology · 2024
    Review
  6. Article
  7. Article
  8. Metabolic and immune-sensitive contacts between lipid droplets and endoplasmic reticulum reconstituted in vitro.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Article
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  15. 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

3 authors at 1 institution in 1 country.

Kritika SadhDepartment of Biological Sciences, Tata Institute of Fundamental Research, Mumbai, India.
Priyanka RaiDepartment of Biological Sciences, Tata Institute of Fundamental Research, Mumbai, India.
Roop MallikDepartment of Biological Sciences, Tata Institute of Fundamental Research, Mumbai, India.ORCID http://orcid.org/0000-0001-6820-6556
Tata Institute of Fundamental Research · IN

Funding

Wellcome Trust
6 · The paper itself

Abstract

Lipid droplets (LDs) are cellular stores of neutral fat that facilitate lipid and protein trafficking in response to metabolic cues. Unlike other vesicles, the phospholipid membrane on the LD is a monolayer. Interestingly, this monolayer membrane has free cholesterol, and may therefore contain lipid microdomains that serve as a platform for assembling proteins involved in signal transduction, cell polarity, pathogen entry etc. In support of this, cell culture studies have detected microdomain-associated "raftophilic" proteins on LDs. However, the physiological significance of this observation has been unclear. Here we show that two proteins (Flotillin-1 and SNAP23) that bind to membrane microdomains associate differently with LDs purified from rat liver depending on the feeding/fasting state of the animal. Flotillin-1 increases on LDs in the fed state, possibly because LDs interact with the endoplasmic reticulum (ER), facilitating supply of flotillin-1 from ER to LDs. Interestingly, this increase in flotillin-1 is correlated with an increase in free cholesterol on the LDs in fed state. In opposite behaviour to flotillin-1, SNAP23 increases on LDs in the fasted state and this appears to mediate LD-mitochondria interactions. Such LD-mitochondria interactions may provide fatty acids to mitochondria for promoting beta-oxidation in hepatocytes in response to fasting. Our work brings out physiologically relevant aspects of lipid droplet biology that are different from, and may not be entirely possible to replicate and study in cell culture.

Indexed as

AnimalsCentrifugation, Density GradientCholesterolEatingEndoplasmic ReticulumFastingGene ExpressionLipid DropletsLiverMaleMembrane MicrodomainsMembrane ProteinsMicrosomes, LiverMitochondriaProtein TransportRatsCholesterolflotillinsMembrane ProteinsSnap23 protein, ratVesicular Transport Proteins

Identifiers

PMID28800633
PMCPMC5553754
OpenAlexW2743149282

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.