Evidence map›Paper›PMID 22942276›Full record

ArticleThe Journal of biological chemistry2012

Phosphatidylinositol-4-phosphate 5-kinase isoforms exhibit acyl chain selectivity for both substrate and lipid activator.

Yulia V Shulga, Richard A Anderson, Matthew K Topham, Richard M Epand

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

35 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. Review
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  4. Reconstitution of ORP-mediated lipid exchange coupled to PI4P metabolism.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  14. First insights into the honey bee (Journal of advanced research · 2022
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  15. Review
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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

4 authors at 3 institutions in 2 countries.

Yulia V ShulgaDepartment of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario L8S 4K1, Canada.
Richard A Anderson
Matthew K Topham
Richard M Epand
McMaster University · CAUniversity of Utah · USUniversity of Wisconsin–Madison · US

Funding

UW COMPREHENSIVE CANCER CENTER SUPPORTP30CA014520 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI Christian Capitini · 1985 to 2026
$142.6M
Targeting of Phosphoinositide Signaling in Migration, Invasion and MetastasisR01GM057549 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI ANDERSON, RICHARD A. · 1998 to 2019
$5.7M
PI Signaling Role in Epithelial/Mesenchymal TransitionR01CA104708 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI ANDERSON, RICHARD A. · 2004 to 2014
$2.9M
Diacylglycerol Kinase Delta in Growth and DevelopmentR01CA095463 · NCI · UNIVERSITY OF UTAH · PI TOPHAM, MATTHEW KENT · 2002 to 2011
$2.4M
NCI NIH HHS CA095463NCI NIH HHS P30 CA014520NCI NIH HHS R01 CA095463NCI NIH HHS R01 CA104708NCI NIH HHS R01CA104708NIGMS NIH HHS R01 GM057549
6 · The paper itself

Abstract

Phosphatidylinositol 4,5-bisphosphate is mostly produced in the cell by phosphatidylinositol-4-phosphate 5-kinases (PIP5K) and has a crucial role in numerous signaling events. Here we demonstrate that in vitro all three isoforms of PIP5K, α, β, and γ, discriminate among substrates with different acyl chains for both the substrates phosphatidylinositol 4-phosphate (PtdIns4P) and phosphatidylinositol (PtdIns) although to different extents, with isoform γ being the most selective. Fully saturated dipalmitoyl-PtdIns4P was a poor substrate for all three isoforms, but both the 1-stearoyl-2-arachidonoyl and the 1-stearoyl-2-oleoyl forms of PtdIns4P were good substrates. V(max) was greater for the 1-stearoyl-2-arachidonoyl form compared with the 1-stearoyl-2-oleoyl form, although for PIP5Kβ the difference was small. For the α and γ isoforms, K(m) was much lower for 1-stearoyl-2-oleoyl PtdIns4P, making this lipid the better substrate of the two under most conditions. Activation of PIP5K by phosphatidic acid is also acyl chain-dependent. Species of phosphatidic acid with two unsaturated acyl chains are much better activators of PIP5K than those containing one saturated and one unsaturated acyl chain. PtdIns is a poor substrate for PIP5K, but it also shows acyl chain selectivity. Curiously, there is no acyl chain discrimination among species of phosphatidic acid in the activation of the phosphorylation of PtdIns. Together, our findings indicate that PIP5K isoforms α, β, and γ act selectively on substrates and activators with different acyl chains. This could be a tightly regulated mechanism of producing physiologically active unsaturated phosphatidylinositol 4,5-bisphosphate species in the cell.

Indexed as

AnimalsChlorocebus aethiopsCOS CellsEnzyme ActivationHumansIsoenzymesPhosphatidylinositol PhosphatesPhosphotransferases (Alcohol Group Acceptor)Substrate SpecificityU937 CellsIsoenzymesphosphatidylinositol 4-phosphatePhosphatidylinositol PhosphatesPhosphotransferases (Alcohol Group Acceptor)

Identifiers

PMID22942276
PMCPMC3476263
OpenAlexW2033108103

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.