Evidence map›Paper›PMID 14749369›Full record

ArticleMolecular and cellular biology2004

Activation of H-Ras in the endoplasmic reticulum by the RasGRF family guanine nucleotide exchange factors.

Imanol Arozarena, David Matallanas, María T Berciano, Victoria Sanz-Moreno, Fernando Calvo, María T Muñoz, Gustavo Egea, Miguel Lafarga, Piero Crespo

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2004. 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
6.8field-weighted citation impact, top 2% 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, 96 citations in OpenAlex.

  1. Article
  2. RASGRF1 Fusions Activate Oncogenic RAS Signaling and Confer Sensitivity to MEK Inhibition.Clinical cancer research : an official journal of the American Association for Cancer Research · 2022
    Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Ras and Rap1: A tale of two GTPases.Seminars in cancer biology · 2019
    Review
  8. Article
  9. RasGRF Couples Nox4-Dependent Endoplasmic Reticulum Signaling to Ras.Arteriosclerosis, thrombosis, and vascular biology · 2017
    Article
  10. Article
  11. Article
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  14. Article
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  19. Review
  20. 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

9 authors at 3 institutions in 1 country.

Imanol ArozarenaInstituto de Investigaciones Biomédicas, Consejo Superior de Investigaciones Científicas, Departamento de Biología Molecular, Unidad de Biomedicina de la Universidad de Cantabria-CSIC, Santander 39011, Spain.
David Matallanas
María T Berciano
Victoria Sanz-Moreno
Fernando Calvo
María T Muñoz
Gustavo Egea
Miguel Lafarga
Piero Crespo
Consejo Superior de Investigaciones Científicas · ESConsorci Institut D'Investigacions Biomediques August Pi I Sunyer · ESUniversidad de Cantabria · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recent findings indicate that in addition to its location in the peripheral plasma membrane, H-Ras is found in endomembranes like the endoplasmic reticulum and the Golgi complex. In these locations H-Ras is functional and can efficiently engage downstream effectors, but little is known about how its activation is regulated in these environments. Here we show that the RasGRF family exchange factors, both endogenous and ectopically expressed, are present in the endoplasmic reticulum but not in the Golgi complex. With the aid of H-Ras constructs specifically tethered to the plasma membrane, endoplasmic reticulum, and Golgi complex, we demonstrate that RasGRF1 and RasGRF2 can activate plasma membrane and reticular, but not Golgi-associated, H-Ras. We also show that RasGRF DH domain is required for the activation of H-Ras in the endoplasmic reticulum but not in the plasma membrane. Furthermore, we demonstrate that RasGRF mediation favors the activation of reticular H-Ras by lysophosphatidic acid treatment whereas plasma membrane H-Ras is made more responsive to stimulation by ionomycin. Overall, our results provide the initial insights into the regulation of H-Ras activation in the endoplasmic reticulum.

Indexed as

AnimalsCell MembraneCOS CellsEndoplasmic ReticulumGanglia, SpinalGolgi ApparatusHeLa CellsHippocampusHumansMaleNeuronsProtein Structure, TertiaryProtein TransportProto-Oncogene Proteins p21(ras)ras-GRF1ras Guanine Nucleotide Exchange FactorsHRAS protein, humanProto-Oncogene Proteins p21(ras)ras-GRF1RASGRF2 protein, humanRasgrf2 protein, ratras Guanine Nucleotide Exchange Factors

Identifiers

PMID14749369
PMCPMC344182
OpenAlexW2158511919

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.