Evidence map›Paper›PMID 9736710›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1998

An essential role for the phosphatidylinositol transfer protein in the scission of coatomer-coated vesicles from the trans-Golgi network.

J P Simon, T Morimoto, V A Bankaitis, T A Gottlieb, I E Ivanov, M Adesnik, D D Sabatini

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

17 citing papers in PubMed, 52 citations in OpenAlex.

  1. Review
  2. Review
  3. Courier service for phosphatidylinositol: PITPs deliver on demand.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2021
    Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. COPI budding within the Golgi stack.Cold Spring Harbor perspectives in biology · 2011
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. 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

7 authors at 2 institutions in 1 country.

J P SimonDepartment of Cell Biology, New York University School of Medicine, New York, NY 10016, USA.
T Morimoto
V A Bankaitis
T A Gottlieb
I E Ivanov
M Adesnik
D D Sabatini
University of Alabama · USNew York University · US

Funding

SYNTHESIS &DISTRIBUTION OF PROTEINS IN MEMBRANESR01GM043583 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI SABATINI, DAVID D · 1991 to 2004
$2.3M
NIGMS NIH HHS GM43583NIGMS NIH HHS R01 GM043583
6 · The paper itself

Abstract

We identified the phosphatidylinositol transfer protein (PITP) as being responsible for a powerful latent, nucleotide-independent, Golgi-vesiculating activity that is present in the cytosol but is only manifested as an uncontrolled activity in a cytosolic protein subfraction, in which it is separated from regulatory components that appear to normally limit its action to the scission of COPI-coated buds from trans-Golgi network membranes. A specific anti-PITP antibody that recognizes the two mammalian PITP isoforms fully inhibited the capacity of the cytosol to support normal vesicle generation as well as the uncontrolled vesiculating activity manifested by the cytosolic protein subfraction. The phosphatidylinositol- (PI) loaded form of the yeast PITP, Sec14p, but not the phosphatidylcholine- (PC) loaded form of the protein, was capable of substituting for the cytosolic subfraction in promoting the scission of coated buds from the trans-Golgi network. At higher concentration, however, Sec14p, when loaded with PI, but not with PC or phosphatidylglycerol, caused by itself an indiscriminate vesiculation of uncoated Golgi membranes that could be suppressed by PC-Sec14p, which also suppresses the uncontrolled vesiculation caused by the cytosolic subfraction. We propose that, by delivering PI to specific sites in the Golgi membrane near the necks of coated buds, PITP induces local changes in the organization of the lipid bilayer, possibly involving PI metabolites, that triggers the fusion of the ectoplasmic faces of the Golgi membrane necessary for the scission of COPI-coated vesicles.

Indexed as

Membrane GlycoproteinsSaccharomyces cerevisiae ProteinsAnimalsCarrier ProteinsCoated VesiclesCoatomer ProteinCytosolEthylmaleimideFungal ProteinsGolgi ApparatusLiposomesMembrane FusionMembrane ProteinsMicroscopy, ElectronPhosphatidylcholinesPhosphatidylinositolsCarrier ProteinsCoatomer ProteinEthylmaleimideFungal ProteinsG protein, vesicular stomatitis virusLiposomesMembrane GlycoproteinsMembrane ProteinsPhosphatidylcholinesPhosphatidylinositolsPhospholipid Transfer ProteinsSaccharomyces cerevisiae ProteinsSEC24 protein, S cerevisiaeViral Envelope Proteins

Identifiers

PMID9736710
PMCPMC21616
OpenAlexW2018355386

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.