Evidence map›Paper›PMID 17122360›Full record

ArticleMolecular biology of the cell2007

A regulated adaptor function of p40phox: distinct p67phox membrane targeting by p40phox and by p47phox.

Takehiko Ueyama, Toshihiko Tatsuno, Takumi Kawasaki, Satoshi Tsujibe, Yasuhito Shirai, Hideki Sumimoto, Thomas L Leto, Naoaki Saito

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

45 citing papers in PubMed, 82 citations in OpenAlex.

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  15. The Role of Cysteine String Protein α Phosphorylation at Serine 10 and 34 by Protein Kinase Cγ for Presynaptic Maintenance.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
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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 3 institutions in 2 countries.

Takehiko UeyamaLaboratory of Molecular Pharmacology, Biosignal Research Center, Kobe University, Kobe 657-8501, Japan.
Toshihiko Tatsuno
Takumi Kawasaki
Satoshi Tsujibe
Yasuhito Shirai
Hideki Sumimoto
Thomas L Leto
Naoaki Saito
Kobe University · JPKyushu University · JPNational Institutes of Health · US

Funding

NOX family NADPH oxidases: roles in innate immunity and inflammatory diseaseZIAAI000614 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI LETO, THOMAS · 2009 to 2024
$16.2M
STRUCTURE AND FUNCTION OF PHAGOCYTE PROTEINSZ01AI000614 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI LETO, THOMAS · 1991 to 2008
$3.3M
6 · The paper itself

Abstract

In the phagocytic cell, NADPH oxidase (Nox2) system, cytoplasmic regulators (p47(phox), p67(phox), p40(phox), and Rac) translocate and associate with the membrane-spanning flavocytochrome b(558), leading to activation of superoxide production. We examined membrane targeting of phox proteins and explored conformational changes in p40(phox) that regulate its translocation to membranes upon stimulation. GFP-p40(phox) translocates to early endosomes, whereas GFP-p47(phox) translocates to the plasma membrane in response to arachidonic acid. In contrast, GFP-p67(phox) does not translocate to membranes when expressed alone, but it is dependent on p40(phox) and p47(phox) for its translocation to early endosomes or the plasma membrane, respectively. Translocation of GFP-p40(phox) or GFP-p47(phox) to their respective membrane-targeting sites is abolished by mutations in their phox (PX) domains that disrupt their interactions with their cognate phospholipid ligands. Furthermore, GFP-p67(phox) translocation to either membrane is abolished by mutations that disrupt its interaction with p40(phox) or p47(phox). Finally, we detected a head-to-tail (PX-Phox and Bem1 [PB1] domain) intramolecular interaction within p40(phox) in its resting state by deletion mutagenesis, cell localization, and binding experiments, suggesting that its PX domain is inaccessible to interact with phosphatidylinositol 3-phosphate without cell stimulation. Thus, both p40(phox) and p47(phox) function as diverse p67(phox) "carrier proteins" regulated by the unmasking of membrane-targeting domains in distinct mechanisms.

Indexed as

AnimalsCell MembraneChlorocebus aethiopsCOS CellsHumansMiceMutationNADPH OxidasesPhagocytosisPhagosomesPhosphatidylinositol PhosphatesPhosphoproteinsProtein Structure, TertiaryProtein TransportReceptors, IgGSequence Analysis, DNANADPH Oxidasesneutrophil cytosol factor 40Kneutrophil cytosol factor 67Kneutrophil cytosolic factor 1phosphatidylinositol 3-phosphatePhosphatidylinositol PhosphatesPhosphoproteinsReceptors, IgG

Identifiers

PMID17122360
PMCPMC1783789
OpenAlexW2162215029

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.