Evidence map›Paper›PMID 22822086›Full record

ArticleThe Journal of biological chemistry2012

Phosphatidylinositol transfer protein, cytoplasmic 1 (PITPNC1) binds and transfers phosphatidic acid.

Kathryn Garner, Alan N Hunt, Grielof Koster, Pentti Somerharju, Emily Groves, Michelle Li, Padinjat Raghu, Roman Holic, Shamshad Cockcroft

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 54 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed, 2 pooled it
1.4field-weighted citation impact, top 21% 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

54 citing papers in PubMed, 2 syntheses or guidelines pooled it, 90 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Phosphatidylinositol transfer protein α binds microcolins in its open conformation.Acta crystallographica. Section D, Structural biology · 2026
    Article
  4. Phosphatidylinositol 4-phosphate; A minor lipid with multiple personalities.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2025
    Review
  5. Review
  6. Article
  7. Review
  8. The Plasma Membrane H+-ATPase Promoter Driving the Expression ofJournal of fungi (Basel, Switzerland) · 2024
    Article
  9. PITPNC1 Suppress CD8Journal of translational medicine · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. International journal of molecular sciences · 2023
    Article
  16. Article
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  19. Article
  20. Role of theFrontiers in cell and developmental biology · 2022
    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

9 authors at 4 institutions in 3 countries.

Kathryn GarnerDepartment of Neuroscience, Physiology and Pharmacology, University College London, London WC1E 6JJ, United Kingdom.
Alan N Hunt
Grielof Koster
Pentti Somerharju
Emily Groves
Michelle Li
Padinjat Raghu
Roman Holic
Shamshad Cockcroft
University College London · GBUniversity of Southampton · GBTata Institute of Fundamental Research · INUniversity of Helsinki · FI

Funding

British Heart Foundation FS/08/044/25498
6 · The paper itself

Abstract

Phosphatidylinositol transfer proteins (PITPs) are versatile proteins required for signal transduction and membrane traffic. The best characterized mammalian PITPs are the Class I PITPs, PITPα (PITPNA) and PITPβ (PITPNB), which are single domain proteins with a hydrophobic cavity that binds a phosphatidylinositol (PI) or phosphatidylcholine molecule. In this study, we report the lipid binding properties of an uncharacterized soluble PITP, phosphatidylinositol transfer protein, cytoplasmic 1 (PITPNC1) (alternative name, RdgBβ), of the Class II family. We show that the lipid binding properties of this protein are distinct to Class I PITPs because, besides PI, RdgBβ binds and transfers phosphatidic acid (PA) but hardly binds phosphatidylcholine. RdgBβ when purified from Escherichia coli is preloaded with PA and phosphatidylglycerol. When RdgBβ was incubated with permeabilized HL60 cells, phosphatidylglycerol was released, and PA and PI were now incorporated into RdgBβ. After an increase in PA levels following activation of endogenous phospholipase D or after addition of bacterial phospholipase D, binding of PA to RdgBβ was greater at the expense of PI binding. We propose that RdgBβ, when containing PA, regulates an effector protein or can facilitate lipid transfer between membrane compartments.

Indexed as

AnimalsCytosolEscherichia coliHL-60 CellsHumansLipidsMass SpectrometryMembrane Transport ProteinsModels, BiologicalNeovascularization, PathologicPhosphatidic AcidsPhosphatidylglycerolsPhospholipase DPhospholipidsProtein BindingRecombinant ProteinsLipidsMembrane Transport ProteinsPhosphatidic AcidsPhosphatidylglycerolsPhospholipase DPhospholipidsPITPNC1 protein, humanRecombinant Proteins

Identifiers

PMID22822086
PMCPMC3442557
OpenAlexW2051444072

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.