Evidence map›Paper›PMID 28232524›Full record

ArticleJournal of cell science2017

Lineage-specific proteins essential for endocytosis in trypanosomes.

Paul T Manna, Samson O Obado, Cordula Boehm, Catarina Gadelha, Andrej Sali, Brian T Chait, Michael P Rout, Mark C Field

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

9 citing papers in PubMed, 23 citations in OpenAlex.

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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

8 authors at 4 institutions in 2 countries.

Paul T MannaSchool of Life Sciences, University of Dundee, Dundee, Scotland DD1 5EH, UK.
Samson O ObadoThe Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
Cordula BoehmSchool of Life Sciences, University of Dundee, Dundee, Scotland DD1 5EH, UK.ORCID 0000-0002-1746-2450
Catarina GadelhaSchool of Life Sciences, University of Nottingham, Nottingham NG2 7UH, UK.
Andrej SaliCalifornia Institute for Quantitative Biosciences, University of California, San Francisco, CA 94158, USA.
Brian T ChaitThe Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
Michael P RoutThe Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
Mark C FieldSchool of Life Sciences, University of Dundee, Dundee, Scotland DD1 5EH, UK mfield@mac.com.ORCID 0000-0002-4817-6035
Rockefeller University · USUniversity of Dundee · GBQB3 · USUniversity of Nottingham · GB

Funding

TR&D Project 4. The Imaging Stage: Multiscale Spatiotemporal Modeling of Macromolecular Systems in Cellular NeighborhoodsP41GM109824 · NIGMS · ROCKEFELLER UNIVERSITY · PI ROUT, MICHAEL P · 2014 to 2023
$18.8M
National Resource for Mass Spectrom of Biological MacromoleculesP41GM103314 · NIGMS · ROCKEFELLER UNIVERSITY · PI CHAIT, BRIAN T · 2012 to 2017
$9.9M
The development of tools for proteomic analysis in trypanosomesR21AI096069 · NIAID · ROCKEFELLER UNIVERSITY · PI ROUT, MICHAEL P · 2011 to 2012
$466k
Medical Research Council G0900255Medical Research Council MR/N01037X/1NIAID NIH HHS R21 AI096069NIGMS NIH HHS P41 GM103314NIGMS NIH HHS P41 GM109824Wellcome Trust 203134/Z/16/Z
6 · The paper itself

Abstract

Clathrin-mediated endocytosis (CME) is the most evolutionarily ancient endocytic mechanism known, and in many lineages the sole mechanism for internalisation. Significantly, in mammalian cells CME is responsible for the vast bulk of endocytic flux and has likely undergone multiple adaptations to accommodate specific requirements by individual species. In African trypanosomes, we previously demonstrated that CME is independent of the AP-2 adaptor protein complex, that orthologues to many of the animal and fungal CME protein cohort are absent, and that a novel, trypanosome-restricted protein cohort interacts with clathrin and drives CME. Here, we used a novel cryomilling affinity isolation strategy to preserve transient low-affinity interactions, giving the most comprehensive trypanosome clathrin interactome to date. We identified the trypanosome AP-1 complex,

Indexed as

EndocytosisTrypanosoma brucei bruceiAdaptor Protein Complex 2Adaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAnimalsBiological EvolutionClathrinCytoskeletal ProteinsHumansPhylogenyProtein Serine-Threonine KinasesProtozoan ProteinsSNARE ProteinsTranscription Factor AP-1TrypanosomiasisAAK1 protein, humanAdaptor Protein Complex 2Adaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportClathrinCLINT1 protein, humanCytoskeletal ProteinsKIFAP3 protein, humanProtein Serine-Threonine KinasesProtozoan ProteinsSNARE ProteinsTranscription Factor AP-1ClathrinCytoskeletonEvolutionFlagellumMorphologyTraffickingTrypanosoma

Identifiers

PMID28232524
PMCPMC5399782
OpenAlexW2590309117

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.