Evidence map›Paper›PMID 26061644›Full record

ArticleAutophagy2015

A defect of the vacuolar putative lipase Atg15 accelerates degradation of lipid droplets through lipolysis.

Yuichiro Maeda, Masahide Oku, Yasuyoshi Sakai

Open access · bronzeAbstract read
In one paragraph

Article in Autophagy, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.6field-weighted citation impact, top 12% 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

16 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Article
  3. Lipid Droplets in EndosymbioticPlants (Basel, Switzerland) · 2024
    Review
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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

3 authors at 2 institutions in 3 countries.

Yuichiro Maedaa Division of Applied Life Sciences; Graduate School of Agriculture; Research Unit for Physiological Chemistry; Center for the Promotion of Interdisciplinary Education and Research; Kyoto University; Kitashirakawa-Oiwake ; Sakyo , Kyoto Japan.
Masahide Oku
Yasuyoshi Sakai
Kyoto University · JPGraduate School USA · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lipid droplets (LDs) are the conserved organelles for the deposit of neutral lipids, and function as reservoirs of membrane and energy sources. To date, functional links between autophagy and LD dynamics have not been fully elucidated. Here, we report that a vacuolar putative lipase, Atg15, required for degradation of autophagic bodies, is crucial for the maintenance of LD amount in the yeast Saccharomyces cerevisiae in the stationary phase. Mutant analyses revealed that the putative lipase motif and vacuolar localization of Atg15 are important for the maintenance of LD amount. Loss of autophagosome formation by simultaneous deletion of core ATG genes cancelled the reduction in the LD amount in ATG15-deleted cells, indicating that degradation of autophagic bodies accounts for the functional involvement of Atg15 in LD dynamics. The reduced level of LDs in the mutant strain was dependent on Tgl3 and Tgl4, major lipases for lipolysis in S. cerevisiae. An altered phosphorylation status of Tgl3, higher accumulation of Tgl4, and closer associations of Tgl3 and Tgl4 with LDs were detected in the ATG15-deleted cells. Furthermore, increased levels of downstream metabolites of lipolysis in the mutant strain strongly suggested enhanced lipolytic activity caused by loss of ATG15. Our data provide evidence for a novel link between autophagic flux and LD dynamics integrated with Atg15 activity.

Indexed as

LipolysisAmino Acid MotifsAutophagy-Related ProteinsCarboxylic Ester HydrolasesCell SurvivalCytoplasmGene DeletionLipaseLipidsMembrane GlycoproteinsMicroscopy, FluorescenceMutationPhenotypePhosphorylationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsATG15 protein, S cerevisiaeAutophagy-Related ProteinsCarboxylic Ester HydrolasesLipaseLipidsMembrane GlycoproteinsSaccharomyces cerevisiae ProteinsTGL3 protein, S cerevisiaeTgl4 protein, S cerevisiaeAtg15autophagylipid dropletlipolysisTgl3Tgl4triacylglycerol

Identifiers

PMID26061644
PMCPMC4590595
OpenAlexW1655290979

What OpenQuestion holds

Textmetadata
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.