Evidence map›Paper›PMID 28581508›Full record

ArticleOncogenesis2017

Regulation of cargo transfer between ESCRT-0 and ESCRT-I complexes by flotillin-1 during endosomal sorting of ubiquitinated cargo.

M Meister, S Bänfer, U Gärtner, J Koskimies, M Amaddii, R Jacob, R Tikkanen

Open access · goldAbstract read
In one paragraph

Article in Oncogenesis, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

32 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Revealing the architecture of the membrane-bound Flotillin cage assembly.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Diversity, Origin and Evolution of the ESCRT Systems.bioRxiv : the preprint server for biology · 2024
    Article
  11. Article
  12. Article
  13. Breaking free: endocytosis and endosomal escape of extracellular vesicles.Extracellular vesicles and circulating nucleic acids · 2023
    Review
  14. Article
  15. Review
  16. Review
  17. Article
  18. Review
  19. Article
  20. Review
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

7 authors at 2 institutions in 1 country.

M MeisterInstitute of Biochemistry, Medical Faculty, Justus-Liebig University of Giessen, Giessen, Germany.
S BänferDepartment of Cell Biology and Cell Pathology, Philipps University of Marburg, Marburg, Germany.
U GärtnerInstitute of Anatomy and Cell Biology, Medical Faculty, Justus-Liebig University of Giessen, Giessen, Germany.
J KoskimiesInstitute of Biochemistry, Medical Faculty, Justus-Liebig University of Giessen, Giessen, Germany.
M AmaddiiInstitute of Biochemistry, Medical Faculty, Justus-Liebig University of Giessen, Giessen, Germany.
R JacobDepartment of Cell Biology and Cell Pathology, Philipps University of Marburg, Marburg, Germany.
R TikkanenInstitute of Biochemistry, Medical Faculty, Justus-Liebig University of Giessen, Giessen, Germany.
University of Giessen · DEPhilipps University of Marburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitin-dependent sorting of membrane proteins in endosomes directs them to lysosomal degradation. In the case of receptors such as the epidermal growth factor receptor (EGFR), lysosomal degradation is important for the regulation of downstream signalling. Ubiquitinated proteins are recognised in endosomes by the endosomal sorting complexes required for transport (ESCRT) complexes, which sequentially interact with the ubiquitinated cargo. Although the role of each ESCRT complex in sorting is well established, it is not clear how the cargo is passed on from one ESCRT to the next. We here show that flotillin-1 is required for EGFR degradation, and that it interacts with the subunits of ESCRT-0 and -I complexes (hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs) and Tsg101). Flotillin-1 is required for cargo recognition and sorting by ESCRT-0/Hrs and for its interaction with Tsg101. In addition, flotillin-1 is also required for the sorting of human immunodeficiency virus 1 Gag polyprotein, which mimics ESCRT-0 complex during viral assembly. We propose that flotillin-1 functions in cargo transfer between ESCRT-0 and -I complexes.

Identifiers

PMID28581508
PMCPMC5519196
OpenAlexW2621894760

What OpenQuestion holds

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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.