Evidence map›Paper›PMID 31676965›Full record

ArticleGeroScience2020

The transfer of specific mitochondrial lipids and proteins to lipid droplets contributes to proteostasis upon stress and aging in the eukaryotic model system Saccharomyces cerevisiae.

Florian Geltinger, Julia Tevini, Peter Briza, Amrito Geiser, Johannes Bischof, Klaus Richter, Thomas Felder, Mark Rinnerthaler

Open access · hybridAbstract read
In one paragraph

Article in GeroScience, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

15 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
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  4. Inhibition of ACAT as a Therapeutic Target for Alzheimer's Disease Is Independent of ApoE4 Lipidation.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2023
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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

8 authors at 2 institutions in 1 country.

Florian GeltingerDepartment of Biosciences, University of Salzburg, Salzburg, Austria.
Julia TeviniDepartment of Laboratory Medicine, Paracelsus Medical University, Salzburg, Austria.
Peter BrizaDepartment of Biosciences, University of Salzburg, Salzburg, Austria.
Amrito GeiserDepartment of Biosciences, University of Salzburg, Salzburg, Austria.
Johannes BischofDepartment of Biosciences, University of Salzburg, Salzburg, Austria.
Klaus RichterDepartment of Biosciences, University of Salzburg, Salzburg, Austria.
Thomas FelderDepartment of Laboratory Medicine, Paracelsus Medical University, Salzburg, Austria. t.felder@salk.at.
Mark RinnerthalerDepartment of Biosciences, University of Salzburg, Salzburg, Austria. mark.rinnerthaler@sbg.ac.at.ORCID http://orcid.org/0000-0003-1190-0584
University of Salzburg · ATParacelsus Medical University · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Originally Lipid droplets (LDs) were considered as being droplets for lipid storage only. Increasing evidence, however, demonstrates that LDs fulfill a pleiotropy of additional functions. Among them is the modulation of protein as well as lipid homeostasis. Under unfavorable pro-oxidative conditions, proteins can form aggregates which may exceed the overall proteolytic capacity of the proteasome. After stress termination LDs can adjust and support the removal of these aggregates. Additionally, LDs interact with mitochondria, specifically take over certain proteins and thus prevent apoptosis. LDs, which are loaded with these harmful proteins, are subsequently eliminated via lipophagy. Recently it was demonstrated that this autophagic process is a modulator of longevity. LDs do not only eliminate potentially dangerous proteins, but they are also able to prevent lipotoxicity by storing specific lipids. In the present study we used the model organism Saccharomyces cerevisiae to compare the proteome as well as lipidome of mitochondria and LDs under different conditions: replicative aging, stress and apoptosis. In this context we found an accumulation of proteins at LDs, supporting the role of LDs in proteostasis. Additionally, the composition of main lipid classes such as phosphatidylcholines, phosphatidylethanolamines, phosphatidylinositols, phosphatidylglycerols, triacylglycerols, ceramides, phosphatidic acids and ergosterol of LDs and mitochondria changed during stress conditions and aging.

Indexed as

Lipid DropletsSaccharomyces cerevisiaeLipid MetabolismLipidsMitochondriaProteostasisLipidsLipid dropletsLipidomeMitochondriaProtein sinkProteomeReplicative aging

Identifiers

PMID31676965
PMCPMC7031196
OpenAlexW2988566186

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.