Evidence map›Paper›PMID 30504233›Full record

ReviewJournal of lipid research2019

The interface between phosphatidylinositol transfer protein function and phosphoinositide signaling in higher eukaryotes.

Aby Grabon, Vytas A Bankaitis, Mark I McDermott

Open access · hybridAbstract readReview
In one paragraph

Review in Journal of lipid research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

48 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Phosphatidylinositol transfer protein α binds microcolins in its open conformation.Acta crystallographica. Section D, Structural biology · 2026
    Article
  9. Golgi Drivers of Cancer.Sub-cellular biochemistry · 2026
    Review
  10. Article
  11. An origin for a eukaryotic lipid transfer protein fold in Asgard archaea.bioRxiv : the preprint server for biology · 2025
    Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Reconstitution of ORP-mediated lipid exchange coupled to PI4P metabolism.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Aby GrabonE. L. Wehner-Welch Laboratory, Department of Molecular and Cellular Medicine, Texas A&M Health Science Center, College Station, TX 77843-1114 grabon@tamhsc.edu mcdermott@tamhsc.edu.
Vytas A BankaitisE. L. Wehner-Welch Laboratory, Department of Molecular and Cellular Medicine, Texas A&M Health Science Center, College Station, TX 77843-1114.
Mark I McDermottE. L. Wehner-Welch Laboratory, Department of Molecular and Cellular Medicine, Texas A&M Health Science Center, College Station, TX 77843-1114 grabon@tamhsc.edu mcdermott@tamhsc.edu.
Texas A&M Health Science Center · US

Funding

Role of the Phospholipids in Golgi Secretory FunctionR01GM044530 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI BANKAITIS, VYTAS A · 1991 to 2019
$5.6M
Functional Anatomy of Mammalian Phosphatidylinositol Transfer ProteinsR01GM112591 · NIGMS · TEXAS A&M UNIVERSITY HEALTH SCIENCE CTR · PI BANKAITIS, VYTAS A · 2015 to 2018
$1.7M
NIGMS NIH HHS R01 GM044530NIGMS NIH HHS R01 GM112591
6 · The paper itself

Abstract

Phosphoinositides are key regulators of a large number of diverse cellular processes that include membrane trafficking, plasma membrane receptor signaling, cell proliferation, and transcription. How a small number of chemically distinct phosphoinositide signals are functionally amplified to exert specific control over such a diverse set of biological outcomes remains incompletely understood. To this end, a novel mechanism is now taking shape, and it involves phosphatidylinositol (PtdIns) transfer proteins (PITPs). The concept that PITPs exert instructive regulation of PtdIns 4-OH kinase activities and thereby channel phosphoinositide production to specific biological outcomes, identifies PITPs as central factors in the diversification of phosphoinositide signaling. There are two evolutionarily distinct families of PITPs: the Sec14-like and the StAR-related lipid transfer domain (START)-like families. Of these two families, the START-like PITPs are the least understood. Herein, we review recent insights into the biochemical, cellular, and physiological function of both PITP families with greater emphasis on the START-like PITPs, and we discuss the underlying mechanisms through which these proteins regulate phosphoinositide signaling and how these actions translate to human health and disease.

Indexed as

Signal TransductionAnimalsEukaryotaHumansPhosphatidylinositolsPhospholipid Transfer ProteinsPhosphatidylinositolsPhospholipid Transfer Proteinscell signalingdiseaseslipid and membrane traffickinglipid signalinglipids • membranes

Identifiers

PMID30504233
PMCPMC6358302
OpenAlexW2902215067

What Socratic 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 Socratic graph.