Evidence map›Paper›PMID 20861461›Full record

ArticleBlood2010

Phosphorylation of threonine 154 in p40phox is an important physiological signal for activation of the neutrophil NADPH oxidase.

Tamara A M Chessa, Karen E Anderson, Yanhua Hu, Qingbo Xu, Oliver Rausch, Len R Stephens, Phillip T Hawkins

Open access · greenAbstract read
In one paragraph

Article in Blood, 2010. 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
1.3field-weighted citation impact, top 21% 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, 46 citations in OpenAlex.

  1. Article
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  5. Article
  6. Dying to Defend: Neutrophil Death Pathways and their Implications in Immunity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Review
  7. Akt-2 Is a Potential Therapeutic Target for Disseminated Candidiasis.Journal of immunology (Baltimore, Md. : 1950) · 2022
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Chronic granulomatous disease: why an inflammatory disease?Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologica · 2014
    Review
  19. Article
  20. Review
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

7 authors at 2 institutions in 1 country.

Tamara A M ChessaInositide Laboratory, Babraham Institute, Cambridge, United Kingdom.
Karen E Anderson
Yanhua Hu
Qingbo Xu
Oliver Rausch
Len R Stephens
Phillip T Hawkins
Babraham Institute · GBKing's College London · GB

Funding

Biotechnology and Biological Sciences Research Council BBS/E/B/0000C218Wellcome TrustWellcome Trust WT085889MA
6 · The paper itself

Abstract

The neutrophil nicotinamide adenine dinucleotide phosphate-oxidase is a multisubunit enzyme (comprising gp91(phox), p22(phox), p67(phox), p40(phox), p47(phox), and Rac) that plays a vital role in microbial killing. The recent discovery of a chronic granulomatous disease patient who expresses a mutant p40(phox) subunit, together with the development of mouse models of p40(phox) function, indicate phosphatidylinositol 3-phosphate binding to the PX domain of p40(phox) is an important signal for oxidase activation. However, the presence of other conserved residues and domains in p40(phox) suggest further regulatory roles for this protein. To test this, we introduced wild-type and mutated versions of p40(phox) into fully differentiated mouse neutrophils by retroviral transduction of p40(phox)(-/-) bone marrow progenitors and repopulation of the bone marrow compartment in radiation chimaeras. Phosphorylation of p40(phox) on threonine 154, but not serine 315, was required for full oxidase activation in response to formylated bacterial peptide fMLP, serum-opsonized S aureus, and immunoglobulin-opsonized sheep red blood cells. A functional SH3 domain was not required for oxidase activation, and deletion of the entire domain resulted in enhanced oxidase responses. Phosphorylation of threonine 154 in response to S aureus was mediated by protein kinase Cδ and was required for full translocation of p47(phox) to phagosomes. These results define an important new element in the physiological activation of the oxidase.

Indexed as

ThreonineAnimalsBlotting, WesternBone MarrowErythrocytesFemaleMaleMiceMice, KnockoutNADPH OxidasesNeutrophilsN-Formylmethionine Leucyl-PhenylalaninePhagosomesPhosphoproteinsPhosphorylationProtein Kinase C-deltaNADPH Oxidasesneutrophil cytosol factor 40KN-Formylmethionine Leucyl-PhenylalaninePhosphoproteinsPrkcd protein, mouseProtein Kinase C-deltaReactive Oxygen SpeciesThreonine

Identifiers

PMID20861461
PMCPMC3031388
OpenAlexW2063899875

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.