Evidence map›Paper›PMID 26711178›Full record

ArticleThe EMBO journal2016

TBC1D14 regulates autophagy via the TRAPP complex and ATG9 traffic.

Christopher A Lamb, Stefanie Nühlen, Delphine Judith, David Frith, Ambrosius P Snijders, Christian Behrends, Sharon A Tooze

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
110citing papers in PubMed, 1 pooled it
14.8field-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

110 citing papers in PubMed, 1 synthesis or guideline pooled it, 174 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Where and how do mammalian cells shape autophagosomes?The Journal of biological chemistry · 2026
    Review
  5. Article
  6. Article
  7. Progress on multifunctional transmembrane protein ATG9A.Cell communication and signaling : CCS · 2025
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
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  19. Article
  20. Review

50 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

7 authors at 2 institutions in 2 countries.

Christopher A LambMolecular Cell Biology of Autophagy Group, Francis Crick Institute, London, UK.
Stefanie NühlenInstitute of Biochemistry II, Medical School Goethe University, Frankfurt, Germany.
Delphine JudithMolecular Cell Biology of Autophagy Group, Francis Crick Institute, London, UK.
David FrithThe Francis Crick Institute Mass Spectrometry Core Technology Platform Clare Hall Laboratories, Potters Bar, UK.
Ambrosius P SnijdersThe Francis Crick Institute Mass Spectrometry Core Technology Platform Clare Hall Laboratories, Potters Bar, UK.
Christian BehrendsInstitute of Biochemistry II, Medical School Goethe University, Frankfurt, Germany.
Sharon A ToozeMolecular Cell Biology of Autophagy Group, Francis Crick Institute, London, UK Sharon.tooze@crick.ac.uk.
The Francis Crick Institute · GBGoethe University Frankfurt · DE

Funding

Cancer Research UK 15153Medical Research CouncilWellcome Trust
6 · The paper itself

Abstract

Macroautophagy requires membrane trafficking and remodelling to form the autophagosome and deliver its contents to lysosomes for degradation. We have previously identified the TBC domain-containing protein, TBC1D14, as a negative regulator of autophagy that controls delivery of membranes from RAB11-positive recycling endosomes to forming autophagosomes. In this study, we identify the TRAPP complex, a multi-subunit tethering complex and GEF for RAB1, as an interactor of TBC1D14. TBC1D14 binds to the TRAPP complex via an N-terminal 103 amino acid region, and overexpression of this region inhibits both autophagy and secretory traffic. TRAPPC8, the mammalian orthologue of a yeast autophagy-specific TRAPP subunit, forms part of a mammalian TRAPPIII-like complex and both this complex and TBC1D14 are needed for RAB1 activation. TRAPPC8 modulates autophagy and secretory trafficking and is required for TBC1D14 to bind TRAPPIII. Importantly, TBC1D14 and TRAPPIII regulate ATG9 trafficking independently of ULK1. We propose a model whereby TBC1D14 and TRAPPIII regulate a constitutive trafficking step from peripheral recycling endosomes to the early Golgi, maintaining the cycling pool of ATG9 required for initiation of autophagy.

Indexed as

AutophagyAutophagy-Related ProteinsCell LineCytoplasmic VesiclesGTPase-Activating ProteinsHumansMembrane ProteinsModels, BiologicalProtein BindingProtein Interaction Mappingrab1 GTP-Binding ProteinsVesicular Transport ProteinsATG9A protein, humanAutophagy-Related ProteinsGTPase-Activating ProteinsMembrane Proteinsrab1 GTP-Binding ProteinsTBC1D14 protein, humantransport protein particle, TRAPPTRAPPC8 protein, humanVesicular Transport ProteinsAutophagyMembrane TraffickingRab proteinsTRAPP

Identifiers

PMID26711178
PMCPMC4741301
OpenAlexW2217094724

What OpenQuestion holds

Textmetadata
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.