Evidence map›Paper›PMID 26212136›Full record

ArticleDevelopmental cell2015

Protein Crowding Is a Determinant of Lipid Droplet Protein Composition.

Nora Kory, Abdou-Rachid Thiam, Robert V Farese, Tobias C Walther

Open access · bronzeAbstract read
In one paragraph

Article in Developmental cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
11.7field-weighted citation impact, top 1% 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

85 citing papers in PubMed, 158 citations in OpenAlex.

  1. Article
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  5. Review
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  8. Essential Biology of Lipid Droplets.Annual review of biochemistry · 2025
    Review
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  12. Review
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25 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

4 authors at 3 institutions in 2 countries.

Nora KoryDepartment of Genetics and Complex Diseases, Harvard T.H. Chan School of Public Health, Boston, MA 02115, USA; Department of Cell Biology, Yale School of Medicine, New Haven, CT 06510, USA.
Abdou-Rachid ThiamDepartment of Cell Biology, Yale School of Medicine, New Haven, CT 06510, USA; Laboratoire de Physique Statistique, École Normale Supérieure de Paris, Université Pierre et Marie Curie, Université Paris Diderot, Centre National de la Recherche Scientifique, 24 Rue Lhomond, 75005 Paris, France.
Robert V FareseDepartment of Genetics and Complex Diseases, Harvard T.H. Chan School of Public Health, Boston, MA 02115, USA; Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA; Broad Institute of MIT and Harvard, Cambridge, MA 02142, USA. Electronic address: robert@hsph.harvard.edu.
Tobias C WaltherDepartment of Genetics and Complex Diseases, Harvard T.H. Chan School of Public Health, Boston, MA 02115, USA; Department of Cell Biology, Yale School of Medicine, New Haven, CT 06510, USA; Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA; Broad Institute of MIT and Harvard, Cambridge, MA 02142, USA. Electronic address: twalther@hsph.harvard.edu.
Broad Institute · USCentre National de la Recherche Scientifique · FRHarvard University · US

Funding

Mechanisms of Lipid Droplet Protein TargetingR01GM097194 · NIGMS · YALE UNIVERSITY · PI WALTHER, TOBIAS C · 2011 to 2024
$4.9M
The Mechanisms of Lipid Droplet Formation and RegulationR01GM099844 · NIGMS · J. DAVID GLADSTONE INSTITUTES · PI FARESE, ROBERT V · 2012 to 2015
$1.9M
Cellular Functions of Plasma Membrane Organization by EisosomesR01GM095982 · NIGMS · YALE UNIVERSITY · PI WALTHER, TOBIAS C · 2012 to 2015
$1.2M
NIGMS NIH HHS R01 GM095982NIGMS NIH HHS R01 GM097194NIGMS NIH HHS R01GM-097194NIGMS NIH HHS R01 GM099844NIGMS NIH HHS R01GM-099844
6 · The paper itself

Abstract

Lipid droplets (LDs) are lipid storage organelles that grow or shrink, depending on the availability of metabolic energy. Proteins recruited to LDs mediate many metabolic functions, including phosphatidylcholine and triglyceride synthesis. How the LD protein composition is tuned to the supply and demand for lipids remains unclear. We show that LDs, in contrast to other organelles, have limited capacity for protein binding. Consequently, macromolecular crowding plays a major role in determining LD protein composition. During lipolysis, when LDs and their surfaces shrink, some, but not all, proteins become displaced. In vitro studies show that macromolecular crowding, rather than changes in monolayer lipid composition, causes proteins to fall off the LD surface. As predicted by a crowding model, proteins compete for binding to the surfaces of LDs. Moreover, the LD binding affinity determines protein localization during lipolysis. Our findings identify protein crowding as an important principle in determining LD protein composition.

Indexed as

Lipid MetabolismAnimalsCell LineCholine-Phosphate CytidylyltransferaseDrosophila melanogasterDrosophila ProteinsGlycerol-3-Phosphate O-AcyltransferaseHydrophobic and Hydrophilic InteractionsLipid DropletsLipolysisMultiprotein ComplexesProtein BindingCct1protein, DrosophilaCholine-Phosphate CytidylyltransferaseDrosophila ProteinsGlycerol-3-Phosphate O-AcyltransferaseMultiprotein Complexes

Identifiers

PMID26212136
PMCPMC4536137
OpenAlexW1820136232

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.