Evidence map›Paper›PMID 25495476›Full record

ArticleAutophagy2014

RAB3GAP1 and RAB3GAP2 modulate basal and rapamycin-induced autophagy.

Natalie Spang, Anne Feldmann, Heike Huesmann, Fazilet Bekbulat, Verena Schmitt, Christof Hiebel, Ingrid Koziollek-Drechsler, Albrecht M Clement, Bernd Moosmann, Jennifer Jung and 4 more

Open access · hybridAbstract read
In one paragraph

Article in Autophagy, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

49 citing papers in PubMed, 90 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. First Clinical Report of TwoJournal of pediatric genetics · 2023
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Autophagy Dysfunction in ALS: from Transport to Protein Degradation.Journal of molecular neuroscience : MN · 2022
    Review
  14. Article
  15. NovelJournal of clinical neurology (Seoul, Korea) · 2022
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  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

14 authors at 4 institutions in 2 countries.

Natalie Spanga Institute for Pathobiochemistry ; University Medical Center of the Johannes Gutenberg University ; Mainz , Germany.
Anne Feldmann
Heike Huesmann
Fazilet Bekbulat
Verena Schmitt
Christof Hiebel
Ingrid Koziollek-Drechsler
Albrecht M Clement
Bernd Moosmann
Jennifer Jung
Christian Behrends
Ivan Dikic
Andreas Kern
Christian Behl
University Medical Center of the Johannes Gutenberg University Mainz · DEJohannes Gutenberg University Mainz · DEGoethe University Frankfurt · DEGoethe Institute · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Macroautophagy is a degradative pathway that sequesters and transports cytosolic cargo in autophagosomes to lysosomes, and its deterioration affects intracellular proteostasis. Membrane dynamics accompanying autophagy are mostly elusive and depend on trafficking processes. RAB GTPase activating proteins (RABGAPs) are important factors for the coordination of cellular vesicle transport systems, and several TBC (TRE2-BUB2-CDC16) domain-containing RABGAPs are associated with autophagy. Employing C. elegans and human primary fibroblasts, we show that RAB3GAP1 and RAB3GAP2, which are components of the TBC domain-free RAB3GAP complex, influence protein aggregation and affect autophagy at basal and rapamycin-induced conditions. Correlating the activity of RAB3GAP1/2 with ATG3 and ATG16L1 and analyzing ATG5 punctate structures, we illustrate that the RAB3GAPs modulate autophagosomal biogenesis. Significant levels of RAB3GAP1/2 colocalize with members of the Atg8 family at lipid droplets, and their autophagy modulatory activity depends on the GTPase-activating activity of RAB3GAP1 but is independent of the RAB GTPase RAB3. Moreover, we analyzed RAB3GAP1/2 in relation to the previously reported suppressive autophagy modulators FEZ1 and FEZ2 and demonstrate that both reciprocally regulate autophagy. In conclusion, we identify RAB3GAP1/2 as novel conserved factors of the autophagy and proteostasis network.

Indexed as

AnimalsAutophagyBiological TransportCaenorhabditis elegansGTPase-Activating ProteinsHumansLysosomesPhagosomesrab3 GTP-Binding ProteinsSirolimusGTPase-Activating ProteinsRAB3GAP1 protein, humanRAB3GAP2 protein, humanrab3 GTP-Binding ProteinsSirolimusATG16L1ATG3ATG, autophagy-relatedautophagyBafi, bafilomycin A1BSA, bovine serum albuminCALCOCO2, calcium binding and coiled-coil domain 2C. elegans, Caenorhabditis elegansDAPI, 4’, 6-diamidino-2-phenylindoleDMSO, dimethyl sulfoxideDPH, 1, 6-diphenyl-1, 3, 5-hexatrieneeV, empty vectorFEZ1FEZ2FEZ, fasciculation and elongation protein zetaGABARAP, GABA(A) receptor-associated proteinGEF, guanine nucleotide exchange factorGFP, green fluorescent proteinlipid dropletsMAP1LC3, microtubule-associated protein 1 light chain 3NBR1, neighbor of BRCA1 gene 1PBS, phosphate-buffered salinePE, phosphatidylethanolamineproteostasisRAB3GAP1RAB3GAP2RABGAP, RAB GTPase activating proteinsiRNA, small interfering RNASQSTM1, sequestosome 1TBC domain, TRE2-BUB2-CDC16 domain

Identifiers

PMID25495476
PMCPMC4502700
OpenAlexW2036681019

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.