Evidence map›Paper›PMID 30705059›Full record

ArticleThe Journal of cell biology2019

The AAA+ ATPase/ubiquitin ligase mysterin stabilizes cytoplasmic lipid droplets.

Munechika Sugihara, Daisuke Morito, Shiori Ainuki, Yoshinobu Hirano, Kazutoyo Ogino, Akira Kitamura, Hiromi Hirata, Kazuhiro Nagata

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
12.3field-weighted citation impact, top 1% 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

80 citing papers in PubMed, 133 citations in OpenAlex.

  1. Trial
  2. Lipid metabolism in moyamoya disease: Emerging evidence, vascular remodeling, and therapeutic implications.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2026
    Review
  3. Review
  4. Review
  5. Article
  6. Long-term outcomes in the pre-moyamoya stage ofThe Lancet regional health. Western Pacific · 2026
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Moyamoya Disease and the Risk of Parkinson's Disease.Annals of clinical and translational neurology · 2025
    Article
  14. TheeLife · 2025
    Article
  15. Article
  16. Review
  17. Review
  18. Genes · 2025
    Review
  19. ThebioRxiv : the preprint server for biology · 2025
    Article
  20. Article

20 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

8 authors at 3 institutions in 1 country.

Munechika SugiharaFaculty of Life Sciences, Kyoto Sangyo University, Kyoto, Japan.
Daisuke MoritoInstitute for Protein Dynamics, Kyoto Sangyo University, Kyoto, Japan morito@med.showa-u.ac.jp.ORCID 0000-0003-2263-8200
Shiori AinukiFaculty of Life Sciences, Kyoto Sangyo University, Kyoto, Japan.
Yoshinobu HiranoDepartment of Chemistry and Biological Science, College of Science and Engineering, Aoyama Gakuin University, Sagamihara, Japan.
Kazutoyo OginoDepartment of Chemistry and Biological Science, College of Science and Engineering, Aoyama Gakuin University, Sagamihara, Japan.
Akira KitamuraLaboratory of Molecular Cell Dynamics, Faculty of Advanced Life Science, Hokkaido University, Sapporo, Japan.ORCID 0000-0001-8357-8593
Hiromi HirataDepartment of Chemistry and Biological Science, College of Science and Engineering, Aoyama Gakuin University, Sagamihara, Japan.
Kazuhiro NagataFaculty of Life Sciences, Kyoto Sangyo University, Kyoto, Japan.
Kyoto Sangyo University · JPAoyama Gakuin University · JPHokkaido University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mysterin, also known as RNF213, is an intracellular protein that forms large toroidal oligomers. Mysterin was originally identified in genetic studies of moyamoya disease (MMD), a rare cerebrovascular disorder of unknown etiology. While mysterin is known to exert ubiquitin ligase and putative mechanical ATPase activities with a RING finger domain and two adjacent AAA+ modules, its biological role is poorly understood. Here, we report that mysterin is targeted to lipid droplets (LDs), ubiquitous organelles specialized for neutral lipid storage, and markedly increases their abundance in cells. This effect was exerted primarily through specific elimination of adipose triglyceride lipase (ATGL) from LDs. The ubiquitin ligase and ATPase activities of mysterin were both important for its proper LD targeting. Notably, MMD-related mutations in the ubiquitin ligase domain of mysterin significantly impaired its fat-stabilizing activity. Our findings identify a unique new regulator of cytoplasmic LDs and suggest a potential link between the pathogenesis of MMD and fat metabolism.

Indexed as

Lipid MetabolismAcyltransferasesAdenosine TriphosphatasesAnimalsHEK293 CellsHeLa CellsHep G2 CellsHumansLipaseLipid DropletsMoyamoya DiseaseMutationProtein DomainsUbiquitin-Protein LigasesZebrafishZebrafish ProteinsAcyltransferasesAdenosine TriphosphatasesLipasePNPLA2 protein, humanRNF213 protein, humanUbiquitin-Protein LigasesZebrafish Proteins

Identifiers

PMID30705059
PMCPMC6400562
OpenAlexW2913778884

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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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.