Evidence map›Paper›PMID 25887399›Full record

ArticleThe Journal of biological chemistry2015

Phosphatidylinositol 4,5-Bisphosphate Homeostasis Regulated by Nir2 and Nir3 Proteins at Endoplasmic Reticulum-Plasma Membrane Junctions.

Chi-Lun Chang, Jen Liou

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed, 1 pooled it
6.1field-weighted citation impact, top 3% 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

83 citing papers in PubMed, 1 synthesis or guideline pooled it, 138 citations in OpenAlex.

  1. Stay in touch with the endoplasmic reticulum.Science China. Life sciences · 2024
    Pooled it
  2. Article
  3. Article
  4. Article
  5. bioRxiv : the preprint server for biology · 2026
    Article
  6. Subcellular Cartography of the Phosphoinositide Multiverse.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2026
    Review
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. STIM1 and lipid interactions at ER-PM contact sites.American journal of physiology. Cell physiology · 2025
    Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review

23 more citing papers are in PubMed but not listed here.

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 at 2 institutions in 1 country.

Chi-Lun ChangFrom the Department of Physiology, University of Texas Southwestern Medical Center, Dallas, Texas 75390.ORCID http://orcid.org/0000-0003-0017-2243
Jen LiouFrom the Department of Physiology, University of Texas Southwestern Medical Center, Dallas, Texas 75390 jen.liou@utsouthwestern.edu.ORCID http://orcid.org/0000-0003-1546-3115
Southwestern Medical Center · USThe University of Texas Southwestern Medical Center · US

Funding

Howard Hughes Medical Institute 56006776
6 · The paper itself

Abstract

Phosphatidylinositol (PI) 4,5-bisphosphate (PIP2) at the plasma membrane (PM) constitutively controls many cellular functions, and its hydrolysis via receptor stimulation governs cell signaling. The PI transfer protein Nir2 is essential for replenishing PM PIP2 following receptor-induced hydrolysis, but key mechanistic aspects of this process remain elusive. Here, we demonstrate that PI at the membrane of the endoplasmic reticulum (ER) is required for the rapid replenishment of PM PIP2 mediated by Nir2. Nir2 detects PIP2 hydrolysis and translocates to ER-PM junctions via binding to phosphatidic acid. With distinct phosphatidic acid binding abilities and PI transfer protein activities, Nir2 and its homolog Nir3 differentially regulate PIP2 homeostasis in cells during intense receptor stimulation and in the resting state, respectively. Our study reveals that Nir2 and Nir3 work in tandem to achieve different levels of feedback based on the consumption of PM PIP2 and function at ER-PM junctions to mediate nonvesicular lipid transport between the ER and the PM.

Indexed as

Calcium-Binding ProteinsCell MembraneEndoplasmic ReticulumEye ProteinsHeLa CellsHomeostasisHumansHydrolysisMembrane ProteinsMembrane Transport ProteinsPhosphatidic AcidsPhosphatidylinositol 4,5-DiphosphateCalcium-Binding ProteinsEye ProteinsMembrane ProteinsMembrane Transport ProteinsPhosphatidic AcidsPhosphatidylinositol 4,5-DiphosphatePITPNM1 protein, humanPITPNM2 protein, humanendoplasmic reticulum (ER)lipid transportphosphatidic acidphosphatidylinositolphosphatidylinositol signalingphospholipid metabolismplasma membraneprotein translocationsubcellular organelle

Identifiers

PMID25887399
PMCPMC4505499
OpenAlexW2011447168

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.