Evidence map›Paper›PMID 19307600›Full record

ArticleThe Journal of cell biology2009

A role for ubiquitin ligases and Spartin/SPG20 in lipid droplet turnover.

Scott W Eastman, Mina Yassaee, Paul D Bieniasz

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed
3.9field-weighted citation impact, top 5% 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

88 citing papers in PubMed, 140 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Spartin-mediated lipid transfer facilitates lipid droplet turnover.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Review
  12. Spartin-mediated lipid transfer facilitates lipid droplet turnover.bioRxiv : the preprint server for biology · 2023
    Article
  13. Feedback regulation of ubiquitination and phase separation of HECT E3 ligases.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Lipophagy at a glance.Journal of cell science · 2022
    Article

28 more citing papers are in PubMed but not listed here.

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 1 country.

Scott W EastmanHoward Hughes Medical Institute, The Rockefeller University, New York, NY 10065, USA.
Mina Yassaee
Paul D Bieniasz
Aaron Diamond AIDS Research Center · USHoward Hughes Medical Institute · US

Funding

Mechanism of Action of Retroviral Late-Budding DomainsR01AI052774 · NIAID · AARON DIAMOND AIDS RESEARCH CENTER · PI BIENIASZ, PAUL D. · 2002 to 2011
$3.4M
The role of HECT ubiquitin ligases in viral egress.F32AI065094 · NIAID · AARON DIAMOND AIDS RESEARCH CENTER · PI EASTMAN, SCOTT W · 2006 to 2007
$106k
NIAID NIH HHS F32 AI 065094NIAID NIH HHS F32 AI065094NIAID NIH HHS R01 AI052774NIAID NIH HHS R01 AI 52774
6 · The paper itself

Abstract

HECT (homologous to the E6AP C terminus) ubiquitin ligases have diverse functions in eukaryotic cells. In screens for proteins that bind to the HECT ubiquitin ligase WWP1, we identified Spartin, which is also known as SPG20. This protein is truncated in a neurological disease, Troyer syndrome. In this study, we show that SPG20 associates with the surface of lipid droplets (LDs) and can regulate their size and number. SPG20 binds to another LD protein, TIP47, and both proteins compete with an additional LD protein, adipophilin/adipocyte differentiation-related protein, for occupancy of LDs. The mutant SPG20 present in Troyer syndrome does not possess these activities. Depletion of SPG20 using RNA interference increases the number and size of LDs when cells are fed with oleic acid. Binding of WWP1 to SPG20 and the consequent ubiquitin transfer remove SPG20 from LDs and reduce the levels of coexpressed SPG20. These experiments suggest functions for ubiquitin ligases and SPG20 in the regulation of LD turnover and potential pathological mechanisms in Troyer syndrome.

Indexed as

Lipid MetabolismCell Cycle ProteinsDNA-Binding ProteinsHeLa CellsHumansInclusion BodiesIntracellular Signaling Peptides and ProteinsMembrane ProteinsMutationNeuronsOleic AcidPerilipin-2Perilipin-3Pregnancy ProteinsProteinsRecombinant Fusion ProteinsCell Cycle ProteinsDNA-Binding ProteinsIntracellular Signaling Peptides and ProteinsMembrane ProteinsOleic AcidPerilipin-2Perilipin-3PLIN2 protein, humanPLIN3 protein, humanPregnancy ProteinsProteinsRecombinant Fusion ProteinsRNA, Small InterferingSPART protein, humanUbiquitinUbiquitin-Protein LigasesVesicular Transport ProteinsWWP1 protein, human

Identifiers

PMID19307600
PMCPMC2699154
OpenAlexW2061063821

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.