Evidence map›Paper›PMID 24569991›Full record

ArticleThe Journal of biological chemistry2014

The efficacy of Raf kinase recruitment to the GTPase H-ras depends on H-ras membrane conformer-specific nanoclustering.

Camilo Guzmán, Maja Šolman, Alessio Ligabue, Olga Blaževitš, Débora M Andrade, Luc Reymond, Christian Eggeling, Daniel Abankwa

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

31 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Multiplexed imaging for probing RAS-RAF interactions in living cells.Biochimica et biophysica acta. Biomembranes · 2023
    Article
  6. The kinase occupancy of T cell coreceptors reconsidered.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. Review
  8. Raf promotes dimerization of the Ras G-domain with increased allosteric connections.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  9. FLIM-FRET Analysis of Ras Nanoclustering and Membrane-Anchorage.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. 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

8 authors at 2 institutions in 3 countries.

Camilo GuzmánFrom the Turku Centre for Biotechnology, Åbo Akademi University, Tykistökatu 6B, 20520 Turku, Finland.
Maja Šolman
Alessio Ligabue
Olga Blaževitš
Débora M Andrade
Luc Reymond
Christian Eggeling
Daniel Abankwa
École Polytechnique Fédérale de Lausanne · CHUniversity of Oxford · GB

Funding

Medical Research Council MC_UU_12010/9Medical Research Council MR/K01577X/1
6 · The paper itself

Abstract

Solution structures and biochemical data have provided a wealth of mechanistic insight into Ras GTPases. However, information on how much the membrane organization of these lipid-modified proteins impacts on their signaling is still scarce. Ras proteins are organized into membrane nanoclusters, which are necessary for Ras-MAPK signaling. Using quantitative conventional and super-resolution fluorescence methods, as well as mathematical modeling, we investigated nanoclustering of H-ras helix α4 and hypervariable region mutants that have different bona fide conformations on the membrane. By following the emergence of conformer-specific nanoclusters in the plasma membrane of mammalian cells, we found that conformers impart distinct nanoclustering responses depending on the cytoplasmic levels of the nanocluster scaffold galectin-1. Computational modeling revealed that complexes containing H-ras conformers and galectin-1 affect both the number and lifetime of nanoclusters and thus determine the specific Raf effector recruitment. Our results show that mutations in Ras can affect its nanoclustering response and thus allosterically effector recruitment and downstream signaling. We postulate that cancer- and developmental disease-linked mutations that are associated with the Ras membrane conformation may exhibit so far unrecognized Ras nanoclustering and therefore signaling alterations.

Indexed as

Models, BiologicalProtein MultimerizationSignal TransductionAnimalsCell LineCell MembraneCricetinaeGalectin 1MiceMice, KnockoutNeoplasmsOncogene Protein p21(ras)Protein Structure, Secondaryraf KinasesGalectin 1Oncogene Protein p21(ras)raf KinasesCancerFluorescence Correlation SpectroscopyFluorescence-lifetime Microscopy Imaging (FLIM)Fluorescence Recovery after Photobleaching (FRAP)Fluorescence Resonance Energy Transfer (FRET)MembraneNanoclusterRasSignalingStimulated Emission Depletion (STED)

Identifiers

PMID24569991
PMCPMC3975003
OpenAlexW2030863049

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.