Evidence map›Paper›PMID 22337875›Full record

ArticleThe Journal of biological chemistry2012

Rac1 protein regulates glycogen phosphorylase activation and controls interleukin (IL)-2-dependent T cell proliferation.

Onetsine Arrizabalaga, Hadriano M Lacerda, Ana M Zubiaga, José L Zugaza

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

19 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
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  8. McArdle Disease: New Insights into Its Underlying Molecular Mechanisms.International journal of molecular sciences · 2019
    Review
  9. Article
  10. Article
  11. The regulation of glycogenolysis in the brain.The Journal of biological chemistry · 2018
    Review
  12. Article
  13. Taking advantage of an old concept, "illegitimate transcription", for a proposed novel method of genetic diagnosis of McArdle disease.Genetics in medicine : official journal of the American College of Medical Genetics · 2016
    Article
  14. Article
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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

4 authors at 3 institutions in 2 countries.

Onetsine ArrizabalagaDepartment of Genetics, Physical Anthropology and Animal Physiology, University of the Basque Country, 48940 Leioa, Spain.
Hadriano M Lacerda
Ana M Zubiaga
José L Zugaza
University of the Basque Country · ESCIC bioGUNE · ESUniversity of Turin · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Small GTPases of the Rho family have been implicated in important cellular processes such as cell migration and adhesion, protein secretion, and/or gene transcription. In the lymphoid system, these GTPases participate in the signaling cascades that are activated after engagement of antigen receptors. However, little is known about the role that Rho GTPases play in IL-2-mediated responses. Here, we show that IL-2 induces Rac1 activation in Kit 225 T cells. We identified by mass spectrometry the muscle isoform of glycogen phosphorylase (PYGM) as a novel Rac1 effector molecule in IL-2-stimulated cells. The interaction between the active form of Rac1 (Rac1-GTP) and PYGM was established directly through a domain comprising amino acids 191-270 of PYGM that exhibits significant homology with the Rac binding domain of PAK1. The integrity of this region was crucial for PYGM activation. Importantly, IL-2-dependent cellular proliferation was inhibited upon blocking both the activation of Rac1 and the activity of PYGM. These results reveal a new role for Rac1 in cell signaling, showing that this GTPase triggers T cell proliferation upon IL-2 stimulation by associating with PYGM and modulating its enzymatic activity.

Indexed as

Cell ProliferationEnzyme ActivationAmino Acid SequenceCell LineGene ExpressionGlycogen Phosphorylase, Muscle FormHumansInterleukin-2Molecular Sequence DataPeptide FragmentsPeptide MappingProtein BindingProtein Structure, Tertiaryrac1 GTP-Binding ProteinSequence Homology, Amino AcidSignal TransductionGlycogen Phosphorylase, Muscle FormIL2 protein, humanInterleukin-2Peptide Fragmentsrac1 GTP-Binding ProteinRAC1 protein, human

Identifiers

PMID22337875
PMCPMC3320936
OpenAlexW1976141600

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.