Evidence map›Paper›PMID 12876278›Full record

ArticleThe Journal of cell biology2003

Regulation of phospholipase D1 subcellular cycling through coordination of multiple membrane association motifs.

Guangwei Du, Yelena M Altshuller, Nicolas Vitale, Ping Huang, Sylvette Chasserot-Golaz, Andrew J Morris, Marie-France Bader, Michael A Frohman

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

76 citing papers in PubMed, 162 citations in OpenAlex.

  1. Article
  2. bioRxiv : the preprint server for biology · 2026
    Article
  3. Subcellular Cartography of the Phosphoinositide Multiverse.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2026
    Review
  4. Review
  5. Article
  6. Article
  7. Imaging and Editing the Phospholipidome.Accounts of chemical research · 2022
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Phosphoinositide Recognition Sites Are Blocked by Metabolite Attachment.Frontiers in cell and developmental biology · 2021
    Article
  14. Structure and regulation of human phospholipase D.Advances in biological regulation · 2021
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

16 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

8 authors at 3 institutions in 2 countries.

Guangwei DuDepartment of Pharmacology, University Medical Center, State University of New York at Stony Brook, Stony Brook, NY 11794, USA.
Yelena M Altshuller
Nicolas Vitale
Ping Huang
Sylvette Chasserot-Golaz
Andrew J Morris
Marie-France Bader
Michael A Frohman
Stony Brook University · USCentre National de la Recherche Scientifique · FRUniversity Medical Center · US

Funding

Role of Lipid Phosphatases in Cholesterol and Triglyceride SynthesisR01GM050388 · NIGMS · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI MORRIS, ANDREW J · 1994 to 2011
$2.7M
ROLE OF DROSOSPHIA PHOSPHOLIPASE D IN CELLULARIZATIONR01GM060452 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI FROHMAN, MICHAEL A · 2000 to 2003
$806k
MAMMALIAN PHOSPHOLIPASE D GENESR01GM054813 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI FROHMAN, MICHAEL A · 1998 to 2001
$495k
NIGMS NIH HHS GM50388NIGMS NIH HHS GM54813NIGMS NIH HHS GM60452NIGMS NIH HHS R01 GM050388
6 · The paper itself

Abstract

The signaling enzyme phospholipase D1 (PLD1) facilitates membrane vesicle trafficking. Here, we explore how PLD1 subcellular localization is regulated via Phox homology (PX) and pleckstrin homology (PH) domains and a PI4,5P2-binding site critical for its activation. PLD1 localized to perinuclear endosomes and Golgi in COS-7 cells, but on cellular stimulation, translocated to the plasma membrane in an activity-facilitated manner and then returned to the endosomes. The PI4,5P2-interacting site sufficed to mediate outward translocation and association with the plasma membrane. However, in the absence of PX and PH domains, PLD1 was unable to return efficiently to the endosomes. The PX and PH domains appear to facilitate internalization at different steps. The PH domain drives PLD1 entry into lipid rafts, which we show to be a step critical for internalization. In contrast, the PX domain appears to mediate binding to PI5P, a lipid newly recognized to accumulate in endocytosing vesicles. Finally, we show that the PH domain-dependent translocation step, but not the PX domain, is required for PLD1 to function in regulated exocytosis in PC12 cells. We propose that PLD1 localization and function involves regulated and continual cycling through a succession of subcellular sites, mediated by successive combinations of membrane association interactions.

Indexed as

Gene Expression Regulation, EnzymologicAmino Acid MotifsAnimalsCell MembraneChlorocebus aethiopsCOS CellsEndosomesEnzyme ActivationExocytosisGolgi ApparatusMembrane MicrodomainsModels, BiologicalMutagenesis, Site-DirectedPC12 CellsPhosphatidylinositol PhosphatesPhospholipase DPhosphatidylinositol PhosphatesPhospholipase Dphospholipase D1

Identifiers

PMID12876278
PMCPMC2172799
OpenAlexW1974289741

What Socratic holds

Textmetadata
LicenceCC BY-NC-SA
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.