Evidence map›Paper›PMID 32179693›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

ER membranes exhibit phase behavior at sites of organelle contact.

Christopher King, Prabuddha Sengupta, Arnold Y Seo, Jennifer Lippincott-Schwartz

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers.

0numbers the graph read from it
0cells of the map it votes in
102citing papers in PubMed
10.4field-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

102 citing papers in PubMed, 166 citations in OpenAlex.

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  5. How endosomal PIKfyve inhibition prevents viral membrane fusion and entry.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. PMF proteins mediate mitochondrial fusion in Arabidopsis.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  8. Cytoplasmic crowding acts as a porous medium reducing macromolecule diffusion.Proceedings of the National Academy of Sciences of the United States of America · 2026
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42 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Christopher KingJanelia Research Campus, Howard Hughes Medical Institute, Ashburn, VA 20175.
Prabuddha SenguptaJanelia Research Campus, Howard Hughes Medical Institute, Ashburn, VA 20175.
Arnold Y SeoJanelia Research Campus, Howard Hughes Medical Institute, Ashburn, VA 20175.ORCID 0000-0002-4607-8925
Jennifer Lippincott-SchwartzJanelia Research Campus, Howard Hughes Medical Institute, Ashburn, VA 20175 lippincottschwartzj@janelia.hhmi.org.ORCID 0000-0002-8601-3501
Howard Hughes Medical Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The endoplasmic reticulum (ER) is the site of synthesis of secretory and membrane proteins and contacts every organelle of the cell, exchanging lipids and metabolites in a highly regulated manner. How the ER spatially segregates its numerous and diverse functions, including positioning nanoscopic contact sites with other organelles, is unclear. We demonstrate that hypotonic swelling of cells converts the ER and other membrane-bound organelles into micrometer-scale large intracellular vesicles (LICVs) that retain luminal protein content and maintain contact sites with each other through localized organelle tethers. Upon cooling, ER-derived LICVs phase-partition into microscopic domains having different lipid-ordering characteristics, which is reversible upon warming. Ordered ER lipid domains mark contact sites with ER and mitochondria, lipid droplets, endosomes, or plasma membrane, whereas disordered ER lipid domains mark contact sites with lysosomes or peroxisomes. Tethering proteins concentrate at ER-organelle contact sites, allowing time-dependent behavior of lipids and proteins to be studied at these sites. These findings demonstrate that LICVs provide a useful model system for studying the phase behavior and interactive properties of organelles in intact cells.

Indexed as

AnimalsBiological TransportCell LineCell MembraneChlorocebus aethiopsCOS CellsEndoplasmic ReticulumEndosomesHEK293 CellsHumansLipidsMembrane ProteinsMitochondriaMitochondrial MembranesPeroxisomesProtein TransportLipidsMembrane Proteinscontact sitesendoplasmic reticulumorganelle tethersphase partitioning

Identifiers

PMID32179693
PMCPMC7132286
OpenAlexW3011374555

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.