Evidence map›Paper›PMID 20051520›Full record

ArticleThe Journal of biological chemistry2010

The scaffold protein Shoc2/SUR-8 accelerates the interaction of Ras and Raf.

Rie Matsunaga-Udagawa, Yoshihisa Fujita, Sayaka Yoshiki, Kenta Terai, Yuji Kamioka, Etsuko Kiyokawa, Katsuyuki Yugi, Kazuhiro Aoki, Michiyuki Matsuda

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

41 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
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  7. Case report: AFrontiers in genetics · 2022
    Article
  8. Article
  9. Review
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  11. Review
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  14. Review
  15. SHOC2 complex-driven RAF dimerization selectively contributes to ERK pathway dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  16. Article
  17. M-Ras/Shoc2 signaling modulates E-cadherin turnover and cell-cell adhesion during collective cell migration.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  18. Review
  19. Article
  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 2 countries.

Rie Matsunaga-UdagawaLaboratory of Bioimaging and Cell Signaling, Graduate School of Biostudies, Kyoto University, Kyoto 606-8501, Japan.
Yoshihisa Fujita
Sayaka Yoshiki
Kenta Terai
Yuji Kamioka
Etsuko Kiyokawa
Katsuyuki Yugi
Kazuhiro Aoki
Michiyuki Matsuda
Kyoto University · JPToxicologie, Pharmacologie et Signalisation Cellulaire · FRKeio University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Shoc2/SUR-8 positively regulates Ras/ERK MAP kinase signaling by serving as a scaffold for Ras and Raf. Here, we examined the role of Shoc2 in the spatio-temporal regulation of Ras by using a fluorescence resonance energy transfer (FRET)-based biosensor, together with computational modeling. In epidermal growth factor-stimulated HeLa cells, RNA-mediated Shoc2 knockdown reduced the phosphorylation of MEK and ERK with half-maximal inhibition, but not the activation of Ras. For the live monitoring of Ras binding to Raf, we utilized a FRET biosensor wherein Ras and the Ras-binding domain of Raf were connected tandemly and sandwiched with acceptor and donor fluorescent proteins for the FRET measurement. With this biosensor, we found that Shoc2 was required for the rapid interaction of Ras with Raf upon epidermal growth factor stimulation. To decipher the molecular mechanisms underlying the kinetics, we developed two computational models that might account for the action of Shoc2 in the Ras-ERK signaling. One of these models, the Shoc2 accelerator model, provided a reasonable explanation of the experimental observations. In this Shoc2 accelerator model, Shoc2 accelerated both the association and dissociation of Ras-Raf interaction. We propose that Shoc2 regulates the spatio-temporal patterns of the Ras-ERK signaling pathway primarily by accelerating the Ras-Raf interaction.

Indexed as

AnimalsBiosensing TechniquesComputer SimulationEnzyme ActivationEpidermal Growth FactorExtracellular Signal-Regulated MAP KinasesFluorescence Resonance Energy TransferHeLa CellsHumansIntracellular Signaling Peptides and ProteinsMitogen-Activated Protein Kinase KinasesPhosphorylationProtein Bindingraf Kinasesras ProteinsRNA InterferenceEpidermal Growth FactorExtracellular Signal-Regulated MAP KinasesIntracellular Signaling Peptides and ProteinsMitogen-Activated Protein Kinase Kinasesraf Kinasesras ProteinsSHOC2 protein, human

Identifiers

PMID20051520
PMCPMC2844225
OpenAlexW2123535211

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.