Evidence map›Paper›PMID 26995697›Full record

ReviewTrends in cell biology2016

Targeting Fat: Mechanisms of Protein Localization to Lipid Droplets.

Nora Kory, Robert V Farese, Tobias C Walther

Abstract readReview
In one paragraph

Review in Trends in cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 181 papers.

0numbers the graph read from it
0cells of the map it votes in
181citing papers in PubMed
–field-weighted citation impact
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

181 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
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  6. Article
  7. Selective targeting of kinesin on lipid droplets in the liver reduces plasma lipids.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  11. Article
  12. Article
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  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article

121 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

3 authors.

Nora KoryDepartment of Genetics and Complex Diseases, Harvard T.H. Chan School of Public Health, Boston, MA, USA.
Robert V FareseDepartment of Genetics and Complex Diseases, Harvard T.H. Chan School of Public Health, Boston, MA, USA; Department of Cell Biology, Harvard Medical School, Boston, MA, USA; Broad Institute of Massachusetts Institute of Technology (MIT) and Harvard, Cambridge, MA, 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, USA; Department of Cell Biology, Harvard Medical School, Boston, MA, USA; Broad Institute of Massachusetts Institute of Technology (MIT) and Harvard, Cambridge, MA, USA; Howard Hughes Medical Institute (HHMI), Boston, MA, USA. Electronic address: twalther@hsph.harvard.edu.

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
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM097194NIGMS NIH HHS R01 GM099844
6 · The paper itself

Abstract

How proteins specifically localize to the phospholipid monolayer surface of lipid droplets (LDs) is being unraveled. We review here the major known pathways of protein targeting to LDs and suggest a classification framework based on the localization origin for the protein. Class I proteins often have a membrane-embedded, hydrophobic 'hairpin' motif, and access LDs from the endoplasmic reticulum (ER) either during LD formation or after formation via ER-LD membrane bridges. Class II proteins access the LD surface from the cytosol and bind through amphipathic helices or other hydrophobic domains. Other proteins require lipid modifications or protein-protein interactions to bind to LDs. We summarize knowledge for targeting and removal of the different classes, and highlight areas needing investigation.

Indexed as

AnimalsCytosolHumansLipid DropletsModels, BiologicalOrganellesProteinsProtein TransportProteinsamphipathic α-helixhydrophobic hairpinlipolysisorganelle protein compositiontriglyceride storage

Identifiers

PMID26995697
PMCPMC4976449

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.