Evidence map›Paper›PMID 25172666›Full record

ArticleBiochemical and biophysical research communications2014

Surface features of the lipid droplet mediate perilipin 2 localization.

Arthur Sletten, Alison Seline, Andrew Rudd, Michelle Logsdon, Laura L Listenberger

Abstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

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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

5 authors.

Arthur SlettenDepartment of Biology, St. Olaf College, 1520 St. Olaf Avenue, Northfield, MN 55057, United States; Department of Chemistry, St. Olaf College, 1520 St. Olaf Avenue, Northfield, MN 55057, United States.
Alison SelineDepartment of Biology, St. Olaf College, 1520 St. Olaf Avenue, Northfield, MN 55057, United States; Department of Chemistry, St. Olaf College, 1520 St. Olaf Avenue, Northfield, MN 55057, United States.
Andrew RuddDepartment of Biology, St. Olaf College, 1520 St. Olaf Avenue, Northfield, MN 55057, United States; Department of Chemistry, St. Olaf College, 1520 St. Olaf Avenue, Northfield, MN 55057, United States.
Michelle LogsdonDepartment of Biology, St. Olaf College, 1520 St. Olaf Avenue, Northfield, MN 55057, United States; Department of Chemistry, St. Olaf College, 1520 St. Olaf Avenue, Northfield, MN 55057, United States.
Laura L ListenbergerDepartment of Biology, St. Olaf College, 1520 St. Olaf Avenue, Northfield, MN 55057, United States; Department of Chemistry, St. Olaf College, 1520 St. Olaf Avenue, Northfield, MN 55057, United States. Electronic address: listenbe@stolaf.edu.

Funding

ADRP function and lipid droplet localizationF32GM074453 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI LISTENBERGER, LAURA · 2005 to 2007
$151k
NIGMS NIH HHS 1 F32 GM-074453-01NIGMS NIH HHS F32 GM074453
6 · The paper itself

Abstract

All eukaryotic organisms store excess lipid in intracellular lipid droplets. These dynamic structures are associated with and regulated by numerous proteins. Perilipin 2, an abundant protein on most lipid droplets, promotes neutral lipid accumulation in lipid droplets. However, the mechanism by which perilipin 2 binds to and remains anchored on the lipid droplet surface is unknown. Here we identify features of the lipid droplet surface that influence perilipin 2 localization. We show that perilipin 2 binding to the lipid droplet surface requires both hydrophobic and electrostatic interactions. Reagents that disrupt these interactions also decrease binding. Moreover, perilipin 2 binding does not depend on other lipid droplet-associated proteins but is influenced by the lipid composition of the surface. Perilipin 2 binds to synthetic vesicles composed of dioleoylphosphatidylcholine, a phospholipid with unsaturated acyl chains. Decreasing the temperature of the binding reaction, or introducing phospholipids with saturated acyl chains, decreases binding. We therefore demonstrate a role for surface lipids and acyl chain packing in perilipin 2 binding to lipid droplets. The ability of the lipid droplet phospholipid composition to impact protein binding may link changes in nutrient availability to lipid droplet homeostasis.

Indexed as

Binding SitesGene ExpressionHEK293 CellsHumansHydrophobic and Hydrophilic InteractionsLipid DropletsLiposomesMembrane ProteinsPerilipin-2PhosphatidylcholinesProtein BindingProteolysisStatic Electricity1,2-oleoylphosphatidylcholineLiposomesMembrane ProteinsPerilipin-2PhosphatidylcholinesLipid dropletPerilipin 2Phospholipid monolayer

Identifiers

PMID25172666
PMCPMC4184465

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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.