Evidence map›Paper›PMID 33856341›Full record

ArticleeLife2021

Exceptional stability of a perilipin on lipid droplets depends on its polar residues, suggesting multimeric assembly.

Manuel Giménez-Andrés, Tadej Emeršič, Sandra Antoine-Bally, Juan Martin D'Ambrosio, Bruno Antonny, Jure Derganc, Alenka Čopič

Open access · goldAbstract read
In one paragraph

Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
5.8field-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

21 citing papers in PubMed, 42 citations in OpenAlex.

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  19. Perilipins at a glance.Journal of cell science · 2022
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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

7 authors at 2 institutions in 2 countries.

Manuel Giménez-AndrésInstitut Jacques Monod, CNRS, Université de Paris, Paris, France.ORCID 0000-0002-4100-306X
Tadej EmeršičInstitute of Biophysics, Faculty of Medicine, University of Ljubljana, Ljubljana, Slovenia.ORCID 0000-0002-6084-5182
Sandra Antoine-BallyInstitut Jacques Monod, CNRS, Université de Paris, Paris, France.
Juan Martin D'AmbrosioInstitut Jacques Monod, CNRS, Université de Paris, Paris, France.ORCID 0000-0003-2834-1838
Bruno AntonnyUniversité Côte d'Azur, CNRS, IPMC, Valbonne, France.ORCID 0000-0002-9166-8668
Jure DergancInstitute of Biophysics, Faculty of Medicine, University of Ljubljana, Ljubljana, Slovenia.ORCID 0000-0001-5135-2231
Alenka ČopičInstitut Jacques Monod, CNRS, Université de Paris, Paris, France.ORCID 0000-0003-0166-7731
Centre National de la Recherche Scientifique · FRUniversity of Ljubljana · SI

Funding

EFFECT OF AGE ON OSTEOGENIC ACTIVITYZ01AG000055 · NIA · AGING · PI LIANG, C T · 1990 to 1997
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Centre National de la Recherche Scientifique CNRS-PICS No 214454CNRS CNRS-PICS No 214454European Research Council Synergy #856404Fondation ARC pour la Recherche sur le Cancer DOC20190509052Slovenian Research Agency No. P1-0055
6 · The paper itself

Abstract

Numerous proteins target lipid droplets (LDs) through amphipathic helices (AHs). It is generally assumed that AHs insert bulky hydrophobic residues in packing defects at the LD surface. However, this model does not explain the targeting of perilipins, the most abundant and specific amphipathic proteins of LDs, which are weakly hydrophobic. A striking example is Plin4, whose gigantic and repetitive AH lacks bulky hydrophobic residues. Using a range of complementary approaches, we show that Plin4 forms a remarkably immobile and stable protein layer at the surface of cellular or in vitro generated oil droplets, and decreases LD size. Plin4 AH stability on LDs is exquisitely sensitive to the nature and distribution of its polar residues. These results suggest that Plin4 forms stable arrangements of adjacent AHs via polar/electrostatic interactions, reminiscent of the organization of apolipoproteins in lipoprotein particles, thus pointing to a general mechanism of AH stabilization via lateral interactions.

Indexed as

Hydrophobic and Hydrophilic InteractionsLipid DropletsPerilipin-4Protein BindingProtein Structure, SecondaryPerilipin-4PLIN4 protein, humanadipocyteamphipathic helixapolipoproteincell biologyhumanlipid dropletlipid droplet sizeperilipin 4physics of living systemsS. cerevisiae

Identifiers

PMID33856341
PMCPMC8064757
OpenAlexW3155127781

What OpenQuestion holds

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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.