Evidence map›Paper›PMID 26539917›Full record

ArticleCell death & disease2015

Mahogunin regulates fusion between amphisomes/MVBs and lysosomes via ubiquitination of TSG101.

P Majumder, O Chakrabarti

Open access · goldAbstract read
In one paragraph

Article in Cell death & disease, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

24 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
  2. Review
  3. The Machinery of Exosomes: Biogenesis, Release, and Uptake.International journal of molecular sciences · 2023
    Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Understanding amphisomes.The Biochemical journal · 2021
    Review
  11. Article
  12. A New Take on Prion Protein Dynamics in Cellular Trafficking.International journal of molecular sciences · 2020
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Lysosomal Quality Control in Prion Diseases.Molecular neurobiology · 2018
    Review
  20. 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

2 authors at 1 institution in 1 country.

P MajumderBiophysics and Structural Genomics Division, Saha Institute of Nuclear Physics, Sector 1, Block-AF, Bidhannagar, Kolkata 700064, India.
O ChakrabartiBiophysics and Structural Genomics Division, Saha Institute of Nuclear Physics, Sector 1, Block-AF, Bidhannagar, Kolkata 700064, India.
Saha Institute of Nuclear Physics · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aberrant metabolic forms of the prion protein (PrP), membrane-associated (Ctm)PrP and cytosolic (cyPrP) interact with the cytosolic ubiquitin E3 ligase, Mahogunin Ring Finger-1 (MGRN1) and affect lysosomes. MGRN1 also interacts with and ubiquitinates TSG101, an ESCRT-I protein, involved in endocytosis. We report that MGRN1 modulates macroautophagy. In cultured cells, functional depletion of MGRN1 or overexpression of (Ctm)PrP and cyPrP blocks autophagosome-lysosome fusion, alleviates the autophagic flux and its degradative competence. Concurrently, the degradation of cargo from the endo-lysosomal pathway is also affected. This is significant because catalytic inactivation of MGRN1 alleviates fusion of lysosomes with either autophagosomes (via amphisomes) or late endosomes (either direct or mediated through amphisomes), without drastically perturbing maturation of late endosomes, generation of amphisomes or lysosomal proteolytic activity. The compromised lysosomal fusion events are rescued by overexpression of TSG101 and/or its monoubiquitination in the presence of MGRN1. Thus, for the first time we elucidate that MGRN1 simultaneously modulates both autophagy and heterophagy via ubiquitin-mediated post-translational modification of TSG101.

Indexed as

AnimalsAutophagyCell Line, TumorDNA-Binding ProteinsEndosomal Sorting Complexes Required for TransportHeLa CellsHumansLysosomesMicePrionsTranscription FactorsTsg101 ProteinUbiquitinationUbiquitin-Protein LigasesDNA-Binding ProteinsEndosomal Sorting Complexes Required for TransportMGRN1 protein, humanMgrn1 protein, mousePrionsTranscription FactorsTsg101 ProteinUbiquitin-Protein Ligases

Identifiers

PMID26539917
PMCPMC4670916
OpenAlexW2131206779

What OpenQuestion holds

Textmetadata
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.