Evidence map›Paper›PMID 28100635›Full record

ArticleMolecular biology of the cell2017

Phospholipase Lpl1 links lipid droplet function with quality control protein degradation.

Nina Weisshaar, Hendrik Welsch, Angel Guerra-Moreno, John Hanna

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

19 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
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  5. Mechanism of autocatalytic activation during proteasome assembly.Nature structural & molecular biology · 2024
    Article
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  13. The yeastJournal of cell science · 2020
    Article
  14. Review
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  17. Review
  18. Lipid droplet functions beyond energy storage.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017
    Review
  19. Article
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

4 authors at 1 institution in 1 country.

Nina WeisshaarDepartment of Pathology, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115.
Hendrik WelschDepartment of Pathology, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115.
Angel Guerra-MorenoDepartment of Pathology, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115.
John HannaDepartment of Pathology, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115 jwhanna@partners.org.
Brigham and Women's Hospital · US

Funding

New Ubiquitin-Proteasome System Components that Protect against ProteotoxicityDP5OD019800 · OD · BRIGHAM AND WOMEN'S HOSPITAL · PI HANNA, JOHN W · 2014 to 2018
$2.2M
NIH HHS DP5 OD019800
6 · The paper itself

Abstract

Protein misfolding is toxic to cells and is believed to underlie many human diseases, including many neurodegenerative diseases. Accordingly, cells have developed stress responses to deal with misfolded proteins. The transcription factor Rpn4 mediates one such response and is best known for regulating the abundance of the proteasome, the complex multisubunit protease that destroys proteins. Here we identify Lpl1 as an unexpected target of the Rpn4 response. Lpl1 is a phospholipase and a component of the lipid droplet. Lpl1 has dual functions: it is required for both efficient proteasome-mediated protein degradation and the dynamic regulation of lipid droplets. Lpl1 shows a synthetic genetic interaction with Hac1, the master regulator of a second proteotoxic stress response, the unfolded protein response (UPR). The UPR has long been known to regulate phospholipid metabolism, and Lpl1's relationship with Hac1 appears to reflect Hac1's role in stimulating phospholipid synthesis under stress. Thus two distinct proteotoxic stress responses control phospholipid metabolism. Furthermore, these results provide a direct link between the lipid droplet and proteasomal protein degradation and suggest that dynamic regulation of lipid droplets is a key aspect of some proteotoxic stress responses.

Indexed as

Basic-Leucine Zipper Transcription FactorsDNA-Binding ProteinsEndoplasmic ReticulumGene Expression Regulation, FungalLipid DropletsPhospholipasesProteasome Endopeptidase ComplexProtein FoldingProteolysisRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsUnfolded Protein ResponseBasic-Leucine Zipper Transcription FactorsDNA-Binding ProteinsHAC1 protein, S cerevisiaePhospholipasesProteasome Endopeptidase ComplexRepressor ProteinsRPN4 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTranscription Factors

Identifiers

PMID28100635
PMCPMC5349779
OpenAlexW2579606904

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.