Evidence map›Paper›PMID 25908855›Full record

ArticleJournal of cell science2015

ENTH and ANTH domain proteins participate in AP2-independent clathrin-mediated endocytosis.

Paul T Manna, Catarina Gadelha, Amy E Puttick, Mark C Field

Abstract read
In one paragraph

Article in Journal of cell science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
–field-weighted citation impact
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

22 citing papers in PubMed.

  1. Article
  2. Drug resistance in animal trypanosomiases: Epidemiology, mechanisms and control strategies.International journal for parasitology. Drugs and drug resistance · 2024
    Review
  3. The myxozoansFrontiers in cellular and infection microbiology · 2024
    Article
  4. Lessons from the deep: mechanisms behind diversification of eukaryotic protein complexes.Biological reviews of the Cambridge Philosophical Society · 2023
    Article
  5. Article
  6. Article
  7. To the Surface and Back: Exo- and Endocytic Pathways inFrontiers in cell and developmental biology · 2021
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
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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

4 authors.

Paul T MannaDepartment of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, UK.
Catarina GadelhaSchool of Life Sciences, University of Nottingham, Queen's Medical Centre, Nottingham NG7 2UH, UK.
Amy E PuttickDepartment of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, UK.
Mark C FieldDivision of Biological Chemistry and Drug Discovery, University of Dundee, Dundee DD1 5EH, UK m.c.field@dundee.ac.uk.

Funding

Medical Research Council G0900255Wellcome TrustWellcome Trust 090007/Z/09/Z
6 · The paper itself

Abstract

Clathrin-mediated endocytosis (CME) is a major route of entry into eukaryotic cells. A core of evolutionarily ancient genes encodes many components of this system but much of our mechanistic understanding of CME is derived from a phylogenetically narrow sampling of a few model organisms. In the parasite Trypanosoma brucei, which is distantly related to the better characterised animals and fungi, exceptionally fast endocytic turnover aids its evasion of the host immune system. Although clathrin is absolutely essential for this process, the adaptor protein complex 2 (AP2) has been secondarily lost, suggesting mechanistic divergence. Here, we characterise two phosphoinositide-binding monomeric clathrin adaptors, T. brucei (Tb)EpsinR and TbCALM, which in trypanosomes are represented by single genes, unlike the expansions present in animals and fungi. Depletion of these gene products reveals essential, but partially redundant, activities in CME. Ultrastructural analysis of TbCALM and TbEpsinR double-knockdown cells demonstrated severe defects to clathrin-coated pit formation and morphology associated with a dramatic inhibition of endocytosis. Depletion of TbCALM alone, however, produced a distinct lysosomal segregation phenotype, indicating an additional non-redundant role for this protein. Therefore, TbEpsinR and TbCALM represent ancient phosphoinositide-binding proteins with distinct and vital roles in AP2-independent endocytosis.

Indexed as

Adaptor Protein Complex 2Adaptor Proteins, Vesicular TransportAnimalsCarrier ProteinsCells, CulturedClathrinCoated Pits, Cell-MembraneEndocytosisEvolution, MolecularPhosphatidylinositolsPhylogenyProtein Structure, TertiaryTrypanosoma brucei bruceiAdaptor Protein Complex 2Adaptor Proteins, Vesicular TransportCarrier ProteinsClathrinPhosphatidylinositolsEndocytosisEvolutionPhosphoinositideTraffickingTrypanosome

Identifiers

PMID25908855
PMCPMC4450294

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Registered trials

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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.