Evidence map›Paper›PMID 20569199›Full record

ArticleThe Biochemical journal2010

Genomic tagging reveals a random association of endogenous PtdIns5P 4-kinases IIalpha and IIbeta and a partial nuclear localization of the IIalpha isoform.

Minchuan Wang, Nicholas J Bond, Andrew J Letcher, Jonathan P Richardson, Kathryn S Lilley, Robin F Irvine, Jonathan H Clarke

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

30 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Subcellular Cartography of the Phosphoinositide Multiverse.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2026
    Review
  3. Review
  4. Article
  5. Development of potent and selective degraders of PI5P4Kγ.European journal of medicinal chemistry · 2023
    Article
  6. Article
  7. Article
  8. 25 Years of PI5P.Frontiers in cell and developmental biology · 2023
    Review
  9. Review
  10. Pharmacological inhibition of PI5P4Kα/β disrupts cell energy metabolism and selectively kills p53-null tumor cells.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. Article
  12. Review
  13. Article
  14. Phosphatidylinositol Kinases and Phosphatases inFrontiers in cellular and infection microbiology · 2019
    Review
  15. Article
  16. Article
  17. In B cells, phosphatidylinositol 5-phosphate 4-kinase-α synthesizes PI(4,5)P2 to impact mTORC2 and Akt signaling.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  18. Deletion of the gene Pip4k2c, a novel phosphatidylinositol kinase, results in hyperactivation of the immune system.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  19. Review
  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 2 countries.

Minchuan WangDepartment of Pharmacology, Tennis Court Road, Cambridge, U.K.
Nicholas J Bond
Andrew J Letcher
Jonathan P Richardson
Kathryn S Lilley
Robin F Irvine
Jonathan H Clarke
Tenneco (United States) · USUniversity of Cambridge · GB

Funding

Biotechnology and Biological Sciences Research Council BB/F011067/1Wellcome Trust 079194/Z/06
6 · The paper itself

Abstract

PtdIns5P 4-kinases IIalpha and IIbeta are cytosolic and nuclear respectively when transfected into cells, including DT40 cells [Richardson, Wang, Clarke, Patel and Irvine (2007) Cell. Signalling 19, 1309-1314]. In the present study we have genomically tagged both type II PtdIns5P 4-kinase isoforms in DT40 cells. Immunoprecipitation of either isoform from tagged cells, followed by MS, revealed that they are associated directly with each other, probably by heterodimerization. We quantified the cellular levels of the type II PtdIns5P 4-kinase mRNAs by real-time quantitative PCR and the absolute amount of each isoform in immunoprecipitates by MS using selective reaction monitoring with 14N,13C-labelled internal standard peptides. The results suggest that the dimerization is complete and random, governed solely by the relative concentrations of the two isoforms. Whereas PtdIns5P 4-kinase IIbeta is >95% nuclear, as expected, the distribution of PtdIns4P 4-kinase IIalpha is 60% cytoplasmic (all bound to membranes) and 40% nuclear. In vitro, PtdIns5P 4-kinase IIalpha was 2000-fold more active as a PtdIns5P 4-kinase than the IIbeta isoform. Overall the results suggest a function of PtdIns5P 4-kinase IIbeta may be to target the more active IIalpha isoform into the nucleus.

Indexed as

GenomicsAnimalsCell Line, TransformedCell NucleusChickensCytoplasmDimerizationIsoenzymesPhosphotransferasesProtein BindingProtein TransportIsoenzymesPhosphotransferases

Identifiers

PMID20569199
PMCPMC2943749
OpenAlexW1984086305

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.