Evidence map›Paper›PMID 22096541›Full record

ArticlePloS one2011

Phosphatidylinositol (4,5) bisphosphate controls T cell activation by regulating T cell rigidity and organization.

Yi Sun, Radhika D Dandekar, Yuntao S Mao, Helen L Yin, Christoph Wülfing

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

19 citing papers in PubMed, 40 citations in OpenAlex.

  1. PIP4K attenuates PIP5K lipid kinase activity by disrupting membrane-mediated dimerization.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. The Swing of Lipids at Peroxisomes and Endolysosomes in T Cell Activation.International journal of molecular sciences · 2020
    Review
  11. Review
  12. Article
  13. T cell immunoengineering with advanced biomaterials.Integrative biology : quantitative biosciences from nano to macro · 2017
    Review
  14. Review
  15. The multifaceted role of PIP2 in leukocyte biology.Cellular and molecular life sciences : CMLS · 2015
    Review
  16. Review
  17. Article
  18. Article
  19. Article
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

5 authors at 2 institutions in 1 country.

Yi SunDepartment of Immunology, UT Southwestern Medical Center, Dallas, Texas, United States of America.
Radhika D Dandekar
Yuntao S Mao
Helen L Yin
Christoph Wülfing
The University of Texas Southwestern Medical Center · USSouthwestern Medical Center · US

Funding

SIGNAL REGULATION OF CARDIAC CYTOKINE SYNTHESIS AND MECHANICAL FUNCTIONP50GM021681 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI NWARIAKU, FIEMU E. · 1985 to 2009
$12.8M
NCI NIH HHS R01 CA96733NIGMS NIH HHS P50 GM021681NIGMS NIH HHS P50-GM21681
6 · The paper itself

Abstract

Here we investigate the role of Phosphatidylinositol (4,5) bisphosphate (PIP(2)) in the physiological activation of primary murine T cells by antigen presenting cells (APC) by addressing two principal challenges in PIP(2) biology. First, PIP(2) is a regulator of cytoskeletal dynamics and a substrate for second messenger generation. The relative importance of these two processes needs to be determined. Second, PIP(2) is turned over by multiple biosynthetic and metabolizing enzymes. The joint effect of these enzymes on PIP(2) distributions needs to be determined with resolution in time and space. We found that T cells express four isoforms of the principal PIP(2)-generating enzyme phosphatidylinositol 4-phosphate 5-kinase (PIP5K) with distinct spatial and temporal characteristics. In the context of a larger systems analysis of T cell signaling, these data identify the T cell/APC interface and the T cell distal pole as sites of differential PIP(2) turnover. Overexpression of different PIP5K isoforms, as corroborated by knock down and PIP(2) blockade, yielded an increase in PIP(2) levels combined with isoform-specific changes in the spatiotemporal distributions of accessible PIP(2). It rigidified the T cell, likely by impairing the inactivation of Ezrin Moesin Radixin, delayed and diminished the clustering of the T cell receptor at the cellular interface, reduced the efficiency of T cell proximal signaling and IL-2 secretion. These effects were consistently more severe for distal PIP5K isoforms. Thus spatially constrained cytoskeletal roles of PIP(2) in the control of T cell rigidity and spatiotemporal organization dominate the effects of PIP(2) on T cell activation.

Indexed as

ActinsAnimalsCells, CulturedInterleukin-2Lymphocyte ActivationMiceMice, TransgenicPhosphatidylinositol 4,5-DiphosphatePhosphotransferases (Alcohol Group Acceptor)Protein IsoformsReal-Time Polymerase Chain ReactionReceptors, Antigen, T-CellT-Lymphocytes1-phosphatidylinositol-4-phosphate 5-kinaseActinsInterleukin-2Phosphatidylinositol 4,5-DiphosphatePhosphotransferases (Alcohol Group Acceptor)Protein IsoformsReceptors, Antigen, T-Cell

Identifiers

PMID22096541
PMCPMC3214035
OpenAlexW2086149271

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.