Evidence map›Paper›PMID 20417104›Full record

ArticleCurrent biology : CB2010

c-Abl, Lamellipodin, and Ena/VASP proteins cooperate in dorsal ruffling of fibroblasts and axonal morphogenesis.

Magdalene Michael, Anne Vehlow, Christel Navarro, Matthias Krause

Open access · hybridAbstract read
In one paragraph

Article in Current biology : CB, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed, 1 pooled it
3.9field-weighted citation impact, top 6% 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

55 citing papers in PubMed, 1 synthesis or guideline pooled it, 84 citations in OpenAlex.

  1. Pooled it
  2. Ena/VASP-EVH1 inhibition prevents chemotaxis and metastasis by blocking the EVH1-WAVE2 interaction.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Allosteric regulation of autoinhibition and activation of c-Abl.Computational and structural biotechnology journal · 2022
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Molecularly-targeted therapy for the oral cancer stem cells.The Japanese dental science review · 2018
    Review
  18. G-Protein GαJournal of molecular biology · 2017
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Magdalene MichaelRandall Division of Cell and Molecular Biophysics, King's College London, New Hunt's House, Guy's Campus, London SE1 1UL, UK.
Anne Vehlow
Christel Navarro
Matthias Krause
King's College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/G00319X/1Medical Research CouncilWellcome Trust 077429Wellcome Trust 077429/Z/05/Z
6 · The paper itself

Abstract

backgroundTight regulation of cell motility is essential for many physiological processes, such as formation of a functional nervous system and wound healing. Drosophila Abl negatively regulates the actin cytoskeleton effector protein Ena during neuronal development in flies, and it has been postulated that this may occur through an unknown intermediary. Lamellipodin (Lpd) regulates cell motility and recruits Ena/VASP proteins (Ena, Mena, VASP, EVL) to the leading edge of cells. However, the regulation of this recruitment has remained unsolved.

resultsHere we show that Lpd is a substrate of Abl kinases and binds to the Abl SH2 domain. Phosphorylation of Lpd positively regulates the interaction between Lpd and Ena/VASP proteins. Consistently, efficient recruitment of Mena and EVL to Lpd at the leading edge requires Abl kinases. Furthermore, transient Lpd phosphorylation by Abl kinases upon netrin-1 stimulation of primary cortical neurons positively correlates with an increase in Lpd-Mena coprecipitation. Lpd is also transiently phosphorylated by Abl kinases upon platelet-derived growth factor (PDGF) stimulation, regulates PDGF-induced dorsal ruffling of fibroblasts and axonal morphogenesis, and cooperates with c-Abl in an Ena/VASP-dependent manner.

conclusionsOur findings suggest that Abl kinases positively regulate Lpd-Ena/VASP interaction, Ena/VASP recruitment to Lpd at the leading edge, and Lpd-Ena/VASP function in axonal morphogenesis and in PDGF-induced dorsal ruffling. Our data do not support the suggested negative regulatory role of Abl for Ena. Instead, we propose that Lpd is the hitherto unknown intermediary between Abl and Ena/VASP proteins.

Indexed as

AnimalsAxonsBlotting, WesternCell LineDNA-Binding ProteinsDrosophila melanogasterFibroblastsImmunoprecipitationMorphogenesisNerve Growth FactorsNetrin-1PhosphorylationPlatelet-Derived Growth FactorProto-Oncogene Proteins c-ablTumor Suppressor ProteinsDNA-Binding ProteinsENA-VASP proteinsNerve Growth FactorsNetrin-1Platelet-Derived Growth FactorProto-Oncogene Proteins c-ablTumor Suppressor Proteins

Identifiers

PMID20417104
PMCPMC2946563
OpenAlexW2099809076

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.