Evidence map›Paper›PMID 12429840›Full record

ArticleMolecular biology of the cell2002

Localization of phospholipase D1 to caveolin-enriched membrane via palmitoylation: implications for epidermal growth factor signaling.

Jung Min Han, Yong Kim, Jun Sung Lee, Chang Sup Lee, Byoung Dae Lee, Motoi Ohba, Toshio Kuroki, Pann-Ghill Suh, Sung Ho Ryu

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

26 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Pharmacological and Genetic Inhibition of Caveolin-1 Promotes Epithelialization and Wound Closure.Molecular therapy : the journal of the American Society of Gene Therapy · 2019
    Article
  6. Article
  7. Inhibition ofJournal of Cancer · 2018
    Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Protein kinase C: the "masters" of calcium and lipid.Cold Spring Harbor perspectives in biology · 2011
    Review
  13. Article
  14. Caveolin-1: a critical regulator of lung injury.American journal of physiology. Lung cellular and molecular physiology · 2011
    Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Phospholipase D in the Golgi apparatus.Biochimica et biophysica acta · 2009
    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 2 institutions in 2 countries.

Jung Min HanDivision of Molecular and Life Sciences, Pohang University of Science and Technology, Pohang, 790-784, Korea.
Yong Kim
Jun Sung Lee
Chang Sup Lee
Byoung Dae Lee
Motoi Ohba
Toshio Kuroki
Pann-Ghill Suh
Sung Ho Ryu
Pohang University of Science and Technology · KRShowa University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phospholipase D (PLD) has been suggested to mediate epidermal growth factor (EGF) signaling. However, the molecular mechanism of EGF-induced PLD activation has not yet been elucidated. We investigated the importance of the phosphorylation and compartmentalization of PLD1 in EGF signaling. EGF treatment of COS-7 cells transiently expressing PLD1 stimulated PLD1 activity and induced PLD1 phosphorylation. The EGF-induced phosphorylation of threonine147 was completely blocked and the activity of PLD1 attenuated by point mutations (S2A/T147A/S561A) of PLD1 phosphorylation sites. The expression of a dominant negative PKCalpha mutant by adenovirus-mediated gene transfer greatly inhibited the phosphorylation and activation of PLD1 induced by EGF in PLD1-transfected COS-7 cells. EGF-induced PLD1 phosphorylation occurred primarily in the caveolin-enriched membrane (CEM) fraction, and the kinetics of PLD1 phosphorylation in the CEM were strongly correlated with PLD1 phosphorylation in the total membrane. Interestingly, EGF-induced PLD1 phosphorylation and activation and the coimmunoprecipitation of PLD1 with caveolin-1 and the EGF receptor in the CEM were significantly attenuated in the palmitoylation-deficient C240S/C241S mutant, which did not localize to the CEM. Immunocytochemical analysis revealed that wild-type PLD1 colocalized with caveolin-1 and the EGF receptor and that phosphorylated PLD1 was localized exclusively in the plasma membrane, although some PLD1 was also detected in vesicular structures. Transfection of wild-type PLD1 but not of C240S/C241S mutant increased EGF-induced raf-1 translocation to the CEM and ERK phosphorylation. This study shows, for the first time, that EGF-induced PLD1 phosphorylation and activation occur in the CEM and that the correct localization of PLD1 to the CEM via palmitoylation is critical for EGF signaling.

Indexed as

AnimalsCaveolin 1CaveolinsCell FractionationCell MembraneCOS CellsEnzyme ActivationEpidermal Growth FactorErbB ReceptorsPhospholipase DPhosphorylationPoint MutationProtein Kinase CProtein Kinase C-alphaProtein TransportRatsCav1 protein, ratCaveolin 1CaveolinsEpidermal Growth FactorErbB ReceptorsPhospholipase Dphospholipase D1Protein Kinase CProtein Kinase C-alphaprotein kinase C gammaRecombinant Fusion ProteinsTetradecanoylphorbol Acetate

Identifiers

PMID12429840
PMCPMC133608
OpenAlexW2156579546

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.