Evidence map›Paper›PMID 19401330›Full record

ArticleJournal of cell science2009

An integrin-alpha4-14-3-3zeta-paxillin ternary complex mediates localised Cdc42 activity and accelerates cell migration.

Nicholas O Deakin, Mark D Bass, Stacey Warwood, Julia Schoelermann, Zohreh Mostafavi-Pour, David Knight, Christoph Ballestrem, Martin J Humphries

Open access · greenAbstract read
In one paragraph

Article in Journal of cell science, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

26 citing papers in PubMed, 48 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Interaction between Rho GTPases and 14-3-3 Proteins.International journal of molecular sciences · 2017
    Review
  7. Article
  8. Chemistry and biology of the compounds that modulate cell migration.Journal of industrial microbiology & biotechnology · 2016
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. SHARPINing integrin inhibition.Nature cell biology · 2011
    Article
  19. The tail of integrin activation.Trends in biochemical sciences · 2011
    Review
  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

8 authors at 3 institutions in 2 countries.

Nicholas O DeakinWellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Oxford Road, Manchester M13 9PT, UK.
Mark D Bass
Stacey Warwood
Julia Schoelermann
Zohreh Mostafavi-Pour
David Knight
Christoph Ballestrem
Martin J Humphries
University of Manchester · GBWellcome Centre for Cell-Matrix Research · GBHeidelberg University · DE

Funding

Biotechnology and Biological Sciences Research CouncilWellcome Trust 045225Wellcome Trust 074941
6 · The paper itself

Abstract

Alpha4 integrins are used by leukocytes and neural crest derivatives for adhesion and migration during embryogenesis, immune responses and tumour invasion. The pro-migratory activity of alpha4 integrin is mediated in part through the direct binding of the cytoplasmic domain to paxillin. Here, using intermolecular FRET and biochemical analyses, we report a novel interaction of the alpha4 integrin cytoplasmic domain with 14-3-3zeta. This interaction depends on serine phosphorylation of alpha4 integrin at a site (S978) distinct from that which regulates paxillin binding (S988). Using a combination of metabolic labelling and targeted mass spectrometry by multiple reaction monitoring we demonstrate the low stoichiometry phosphorylation of S978. The interaction between alpha4 integrin and 14-3-3zeta is enhanced by the direct association between 14-3-3zeta and paxillin, resulting in the formation of a ternary complex that stabilises the recruitment of each component. Although pair-wise interaction between alpha4 integrin and paxillin is sufficient for normal Rac1 regulation, the integrity of the ternary complex is essential for focused Cdc42 activity at the lamellipodial leading edge and directed cell movement. Taken together, these data identify a key signalling nexus mediating alpha4 integrin-dependent migration.

Indexed as

Cell MovementSignal Transduction14-3-3 ProteinsAmino Acid MotifsAmino Acid SequenceAnimalsBinding Sitescdc42 GTP-Binding ProteinCHO CellsCricetinaeCricetulusFibronectinsFluorescence Resonance Energy TransferHumansIntegrin alpha4Integrin alpha4beta114-3-3 Proteinscdc42 GTP-Binding ProteinFibronectinsIntegrin alpha4Integrin alpha4beta1Multiprotein ComplexesPaxillinPXN protein, humanrac1 GTP-Binding ProteinRecombinant Fusion ProteinsSerine

Identifiers

PMID19401330
PMCPMC2680104
OpenAlexW2123546248

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.