Evidence map›Paper›PMID 25158650›Full record

ArticleJournal of cellular physiology2015

The differential palmitoylation states of N-Ras and H-Ras determine their distinct Golgi subcompartment localizations.

Stephen J Lynch, Harriet Snitkin, Iwona Gumper, Mark R Philips, David Sabatini, Angel Pellicer

Open access · greenAbstract read
In one paragraph

Article in Journal of cellular physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.0field-weighted citation impact, top 16% 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

35 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Golgi Drivers of Cancer.Sub-cellular biochemistry · 2026
    Review
  3. Review
  4. bioRxiv : the preprint server for biology · 2025
    Article
  5. Attenuating ABHD17 isoforms augments thebioRxiv : the preprint server for biology · 2025
    Article
  6. Article
  7. Article
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  9. Article
  10. Article
  11. Article
  12. CD40 induces selective routing of Ras isoforms to subcellular compartments.Journal of cell communication and signaling · 2023
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Adaptation of the Golgi Apparatus in Cancer Cell Invasion and Metastasis.Frontiers in cell and developmental biology · 2021
    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

6 authors at 1 institution in 1 country.

Stephen J LynchDepartment of Pathology, New York University School of Medicine, New York, New York.
Harriet Snitkin
Iwona Gumper
Mark R Philips
David Sabatini
Angel Pellicer
New York University · US

Funding

Membrane Targeting of GTPasesR01GM055279 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI PHILIPS, MARK REID · 1997 to 2010
$3.2M
Structure/Function Analysis of IcmtR01CA118495 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI PHILIPS, MARK REID · 2006 to 2010
$1.5M
NCI NIH HHS CA118495NIGMS NIH HHS GM055279NIGMS NIH HHS R01 GM055279
6 · The paper itself

Abstract

Despite a high degree of structural homology and shared exchange factors, effectors and GTPase activating proteins, a large body of evidence suggests functional heterogeneity among Ras isoforms. One aspect of Ras biology that may explain this heterogeneity is the differential subcellular localizations driven by the C-terminal hypervariable regions of Ras proteins. Spatial heterogeneity has been documented at the level of organelles: palmitoylated Ras isoforms (H-Ras and N-Ras) localize on the Golgi apparatus whereas K-Ras4B does not. We tested the hypothesis that spatial heterogeneity also exists at the sub-organelle level by studying the localization of differentially palmitoylated Ras isoforms within the Golgi apparatus. Using confocal, live-cell fluorescent imaging and immunogold electron microscopy we found that, whereas the doubly palmitoylated H-Ras is distributed throughout the Golgi stacks, the singly palmitoylated N-Ras is polarized with a relative paucity of expression on the trans Golgi. Using palmitoylation mutants, we show that the different sub-Golgi distributions of the Ras proteins are a consequence of their differential degree of palmitoylation. Thus, the acylation state of Ras proteins controls not only their distribution between the Golgi apparatus and the plasma membrane, but also their distribution within the Golgi stacks.

Indexed as

Genes, rasCell CompartmentationCell LineGolgi ApparatusHumansLipoylationProtein IsoformsProtein Transportras ProteinsSignal TransductionProtein Isoformsras Proteins

Identifiers

PMID25158650
PMCPMC4269384
OpenAlexW1581417572

What OpenQuestion holds

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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.