Evidence map›Paper›PMID 19427041›Full record

ReviewTrends in pharmacological sciences2009

Shuttling and translocation of heterotrimeric G proteins and Ras.

Deepak K Saini, Mariangela Chisari, N Gautam

Open access · greenAbstract readReview
In one paragraph

Review in Trends in pharmacological sciences, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

33 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
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  11. Review
  12. Article
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  15. Article
  16. Article
  17. Review
  18. Article
  19. A tetra(ethylene glycol) derivative of benzothiazole aniline enhances Ras-mediated spinogenesis.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
    Article
  20. Optically triggering spatiotemporally confined GPCR activity in a cell and programming neurite initiation and extension.Proceedings of the National Academy of Sciences of the United States of America · 2013
    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

3 authors at 1 institution in 1 country.

Deepak K SainiDepartment of Anesthesiology, Box 8054, Washington University School of Medicine, St. Louis, MO 63110, USA.
Mariangela Chisari
N Gautam
Washington University in St. Louis · US

Funding

SIGNALING IN LIVING CELLSR01GM069027 · NIGMS · WASHINGTON UNIVERSITY · PI GAUTAM, NARASIMHAN · 2004 to 2016
$3.2M
G PROTEIN SUBUNIT FUNCTIONR01GM080558 · NIGMS · WASHINGTON UNIVERSITY · PI GAUTAM, NARASIMHAN · 2008 to 2011
$1.8M
NIGMS NIH HHS GM080558NIGMS NIH HHS GM69027NIGMS NIH HHS R01 GM069027NIGMS NIH HHS R01 GM080558
6 · The paper itself

Abstract

Heterotrimeric G proteins (alphabetagamma) and Ras proteins are activated by cell-surface receptors that sense extracellular signals. Both sets of proteins were traditionally thought to be constrained to the plasma membrane and some intracellular membranes. Live-cell-imaging experiments have now shown that these proteins are mobile inside a cell, shuttling continually between the plasma membrane and intracellular membranes in the basal state, maintaining these proteins in dynamic equilibrium in different membrane compartments. Furthermore, on receptor activation, a family of G protein betagamma subunits translocates rapidly and reversibly to the Golgi and endoplasmic reticulum enabling direct communication between the extracellular signal and intracellular membranes. A member of the Ras family has similarly been shown to translocate on activation. Although the impact of this unexpected intracellular movement of signaling proteins on cell physiology is likely to be distinct, there are striking similarities in the properties of these two families of signal-transducing proteins.

Indexed as

AnimalsCell MembraneGTP-Binding ProteinsHumansProtein Transportras ProteinsSignal TransductionGTP-Binding Proteinsras Proteins

Identifiers

PMID19427041
PMCPMC3097116
OpenAlexW2016209933

What OpenQuestion holds

Textmetadata
LicenceTDM
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.