Evidence map›Paper›PMID 20200225›Full record

ArticleMolecular biology of the cell2010

A myosin IK-Abp1-PakB circuit acts as a switch to regulate phagocytosis efficiency.

Régis Dieckmann, Yosuke von Heyden, Claudia Kistler, Navin Gopaldass, Stéphanie Hausherr, Scott William Crawley, Eva C Schwarz, Ralph P Diensthuber, Graham P Côté, Georgios Tsiavaliaris and 1 more

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

20 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Phagocytosis at a glance.Journal of cell science · 2025
    Review
  3. Review
  4. Frontiers in cell and developmental biology · 2021
    Review
  5. Article
  6. Article
  7. Article
  8. Eat Prey, Live:Frontiers in immunology · 2017
    Review
  9. Article
  10. Target shape dependence in a simple model of receptor-mediated endocytosis and phagocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  11. Article
  12. Article
  13. The noodle defense.The Journal of cell biology · 2013
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Principles of unconventional myosin function and targeting.Annual review of cell and developmental biology · 2011
    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

11 authors at 6 institutions in 4 countries.

Régis DieckmannDépartment de Biochimie, Faculté des Sciences, Université de Genève, Sciences II, CH-1211-Genève-4, Switzerland.
Yosuke von Heyden
Claudia Kistler
Navin Gopaldass
Stéphanie Hausherr
Scott William Crawley
Eva C Schwarz
Ralph P Diensthuber
Graham P Côté
Georgios Tsiavaliaris
Thierry Soldati
University of Geneva · CHMedizinische Hochschule Hannover · DEQueen's University · CAImperial College London · GBMax Planck Institute for Medical Research · DESaarland University · DE

Funding

Biotechnology and Biological Sciences Research CouncilWellcome Trust
6 · The paper itself

Abstract

Actin dynamics and myosin (Myo) contractile forces are necessary for formation and closure of the phagocytic cup. In Dictyostelium, the actin-binding protein Abp1 and myosin IK are enriched in the closing cup and especially at an actin-dense constriction furrow formed around the neck of engulfed budded yeasts. This phagocytic furrow consists of concentric overlapping rings of MyoK, Abp1, Arp3, coronin, and myosin II, following an order strikingly reminiscent of the overall organization of the lamellipodium of migrating cells. Mutation analyses of MyoK revealed that both a C-terminal farnesylation membrane anchor and a Gly-Pro-Arg domain that interacts with profilin and Abp1 were necessary for proper localization in the furrow and efficient phagocytosis. Consequently, we measured the binding affinities of these interactions and unraveled further interactions with profilins, dynamin A, and PakB. Due to the redundancy of the interaction network, we hypothesize that MyoK and Abp1 are restricted to regulatory roles and might affect the dynamic of cup progression. Indeed, phagocytic uptake was regulated antagonistically by MyoK and Abp1. MyoK is phosphorylated by PakB and positively regulates phagocytosis, whereas binding of Abp1 negatively regulates PakB and MyoK. We conclude that a MyoK-Abp1-PakB circuit acts as a switch regulating phagocytosis efficiency of large particles.

Indexed as

AnimalsDictyosteliumGreen Fluorescent ProteinsImmunoblottingMicrofilament ProteinsMicroscopy, ElectronMicroscopy, FluorescenceMutationMyosin Type IPhagocytosisPhosphorylationProtein BindingProtein KinasesProtein PrenylationProtozoan ProteinsRecombinant Fusion Proteins110 kDa protein kinase, DictyosteliumGreen Fluorescent ProteinsMicrofilament ProteinsMyosin Type IProtein KinasesProtozoan ProteinsRecombinant Fusion Proteins

Identifiers

PMID20200225
PMCPMC2861610
OpenAlexW2121333884

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.