Evidence map›Paper›PMID 29626194›Full record

ArticleNature communications2018

A giant amphipathic helix from a perilipin that is adapted for coating lipid droplets.

Alenka Čopič, Sandra Antoine-Bally, Manuel Giménez-Andrés, César La Torre Garay, Bruno Antonny, Marco M Manni, Sophie Pagnotta, Jeanne Guihot, Catherine L Jackson

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
8.1field-weighted citation impact, top 2% 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

76 citing papers in PubMed, 133 citations in OpenAlex.

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16 more citing papers are in PubMed but not listed here.

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

9 authors at 2 institutions in 1 country.

Alenka ČopičInstitut Jacques Monod, CNRS, UMR 7592, Université Paris Diderot, Sorbonne Paris Cité, 75013, Paris, France. alenka.copic@ijm.fr.ORCID http://orcid.org/0000-0003-0166-7731
Sandra Antoine-BallyInstitut Jacques Monod, CNRS, UMR 7592, Université Paris Diderot, Sorbonne Paris Cité, 75013, Paris, France.
Manuel Giménez-AndrésInstitut Jacques Monod, CNRS, UMR 7592, Université Paris Diderot, Sorbonne Paris Cité, 75013, Paris, France.ORCID http://orcid.org/0000-0002-4100-306X
César La Torre GarayInstitut Jacques Monod, CNRS, UMR 7592, Université Paris Diderot, Sorbonne Paris Cité, 75013, Paris, France.
Bruno AntonnyUniversité Côte d'Azur, CNRS, IPMC, 06560, Valbonne, France.ORCID http://orcid.org/0000-0002-9166-8668
Marco M ManniUniversité Côte d'Azur, CNRS, IPMC, 06560, Valbonne, France.ORCID http://orcid.org/0000-0002-3823-9688
Sophie PagnottaUniversité Côte d'Azur, CNRS, IPMC, 06560, Valbonne, France.
Jeanne GuihotInstitut Jacques Monod, CNRS, UMR 7592, Université Paris Diderot, Sorbonne Paris Cité, 75013, Paris, France.
Catherine L JacksonInstitut Jacques Monod, CNRS, UMR 7592, Université Paris Diderot, Sorbonne Paris Cité, 75013, Paris, France.ORCID http://orcid.org/0000-0002-0843-145X
Centre National de la Recherche Scientifique · FRUniversité Paris-Sud · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

How proteins are targeted to lipid droplets (LDs) and distinguish the LD surface from the surfaces of other organelles is poorly understood, but many contain predicted amphipathic helices (AHs) that are involved in targeting. We have focused on human perilipin 4 (Plin4), which contains an AH that is exceptional in terms of length and repetitiveness. Using model cellular systems, we show that AH length, hydrophobicity, and charge are important for AH targeting to LDs and that these properties can compensate for one another, albeit at a loss of targeting specificity. Using synthetic lipids, we show that purified Plin4 AH binds poorly to lipid bilayers but strongly interacts with pure triglycerides, acting as a coat and forming small oil droplets. Because Plin4 overexpression alleviates LD instability under conditions where their coverage by phospholipids is limiting, we propose that the Plin4 AH replaces the LD lipid monolayer, for example during LD growth.

Indexed as

AnimalsCell LineDrosophilaHeLa CellsHumansHydrophobic and Hydrophilic InteractionsLipid BilayersLipid DropletsModels, MolecularPerilipin-4Protein BindingProtein Conformation, alpha-HelicalProtein UnfoldingRecombinant ProteinsLipid BilayersPerilipin-4PLIN4 protein, humanRecombinant Proteins

Identifiers

PMID29626194
PMCPMC5889406
OpenAlexW2950869313

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.