Evidence map›Paper›PMID 32267208›Full record

ArticleMolecular biology of the cell2020

ESCRT-III and ER-PM contacts maintain lipid homeostasis.

Jeff R Jorgensen, Reika Tei, Jeremy M Baskin, Agnès H Michel, Benoît Kornmann, Scott D Emr

Open access · bronzeAbstract read
In one paragraph

Article in Molecular biology of the cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

11 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
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  4. Tissue-specific knockout inbioRxiv : the preprint server for biology · 2023
    Article
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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

6 authors at 2 institutions in 2 countries.

Jeff R JorgensenWeill Institute for Cell and Molecular Biology and Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853.
Reika TeiWeill Institute for Cell and Molecular Biology and Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853.
Jeremy M BaskinWeill Institute for Cell and Molecular Biology and Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853.
Agnès H MichelDepartment of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom.
Benoît KornmannDepartment of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom.
Scott D EmrWeill Institute for Cell and Molecular Biology and Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853.
Cornell University · USUniversity of Oxford · GB

Funding

Phosphoinositide-Binding Proteins as Regulators of Ubiquitination and Wnt SignalingR01GM131101 · NIGMS · CORNELL UNIVERSITY · PI BASKIN, JEREMY · 2018 to 2022
$1.7M
NIGMS NIH HHS R01 GM131101Wellcome TrustWellcome Trust 214291/Z/18/Z
6 · The paper itself

Abstract

Eukaryotic cells are compartmentalized into organelles by intracellular membranes. While the organelles are distinct, many of them make intimate contact with one another. These contacts were first observed in the 1950s, but only recently have the functions of these contact sites begun to be understood. In yeast, the endoplasmic reticulum (ER) makes extensive intermembrane contacts with the plasma membrane (PM), covering ∼40% of the PM. Many functions of ER-PM contacts have been proposed, including nonvesicular lipid trafficking, ion transfer, and as signaling hubs. Surprisingly, cells that lack ER-PM contacts grow well, indicating that alternative pathways may be compensating for the loss of ER-PM contact. To better understand the function of ER-PM contact sites we used saturating transposon mutagenesis to identify synthetic lethal mutants in a yeast strain lacking ER-PM contact sites. The strongest hits were components of the ESCRT complexes. The synthetic lethal mutants have low levels of some lipid species but accumulate free fatty acids and lipid droplets. We found that only ESCRT-III components are synthetic lethal, indicating that Vps4 and other ESCRT complexes do not function in this pathway. These data suggest that ESCRT-III proteins and ER-PM contact sites act in independent pathways to maintain lipid homeostasis.

Indexed as

Cell MembraneEndoplasmic ReticulumEndosomal Sorting Complexes Required for TransportLipidsMembrane ProteinsMitochondrial MembranesProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsEndosomal Sorting Complexes Required for TransportLipidsMembrane ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID32267208
PMCPMC7353149
OpenAlexW3014914378

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.