Evidence map›Paper›PMID 16563698›Full record

ArticleCellular signalling2006

Regulation of type II PIP kinase by PKD phosphorylation.

Katherine A Hinchliffe, Robin F Irvine

Abstract read
In one paragraph

Article in Cellular signalling, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
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

15 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Striking a balance: PIPExploration of neuroprotective therapy · 2021
    Article
  6. Article
  7. Article
  8. Article
  9. PtdIns5P: news and views of its appearance, disappearance and deeds.Archives of biochemistry and biophysics · 2013
    Review
  10. Oxidative stress and sarcomeric proteins.Circulation research · 2013
    Review
  11. Regulation of protein kinase D1 activity.Molecular pharmacology · 2012
    Review
  12. Article
  13. Review
  14. Article
  15. 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

2 authors.

Katherine A HinchliffeFaculty of Life Sciences, The University of Manchester, Core Technology Facility, 46 Grafton Street, Manchester M13 9NT, United Kingdom. Katherine.a.hinchliffe@cam.ac.uk
Robin F Irvine

Funding

Wellcome Trust 063581
6 · The paper itself

Abstract

The type II PIP kinases phosphorylate the poorly understood inositol lipid PtdIns5P, producing the multi-functional lipid product PtdIns(4,5)P(2). To investigate the regulation of these enzymes by phosphorylation, we partially purified a protein kinase from pig platelets that phosphorylated type IIalpha PIP kinase on an activation loop threonine residue, T376. Pharmacological studies suggested this protein kinase was protein kinase D (PKD), and in vitro experiments confirmed this identification. A phospho-specific antibody was developed and used to demonstrate phosphorylation of T376 in living cells, and its enhancement under conditions in which PKD was activated. Although we were unable to determine the effects of phosphorylation on PIP kinase activity directly, mutation of T376 to aspartate significantly inhibited enzyme activity. We conclude that the type II PIP kinases are physiological targets for PKD phosphorylation, and that this modification is likely to regulate inositol lipid turnover by inhibition of these lipid kinases.

Indexed as

1-Phosphatidylinositol 4-KinaseAmino Acid SubstitutionAnimalsBlood PlateletsCells, CulturedEnzyme ActivationHumansMicePhosphatidylinositol 4,5-DiphosphatePhosphatidylinositol PhosphatesPhosphorylationProtein Kinase CSwineTransfection1-Phosphatidylinositol 4-KinasePhosphatidylinositol 4,5-Diphosphatephosphatidylinositol 5-phosphatePhosphatidylinositol PhosphatesProtein Kinase Cprotein kinase D

Identifiers

PMID16563698
PMCPMC1592545

What OpenQuestion holds

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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.