Evidence map›Paper›PMID 28304276›Full record

ArticleeLife2017

Scaffold-mediated gating of Cdc42 signalling flux.

Péter Rapali, Romain Mitteau, Craig Braun, Aurèlie Massoni-Laporte, Caner Ünlü, Laure Bataille, Floriane Saint Arramon, Steven P Gygi, Derek McCusker

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

28 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Sortase A-Mediated Farnesylation of Cdc42ACS synthetic biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Protein scaffolds: A tool for multi-enzyme assembly.Biotechnology reports (Amsterdam, Netherlands) · 2021
    Review
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  12. Article
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  14. Article
  15. Review
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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

9 authors at 2 institutions in 2 countries.

Péter RapaliUniversity of Bordeaux, CNRS, European Institute of Chemistry and Biology, IBGC, UMR 5095, Pessac, France.
Romain MitteauUniversity of Bordeaux, CNRS, European Institute of Chemistry and Biology, IBGC, UMR 5095, Pessac, France.
Craig BraunDepartment of Cell Biology, Harvard Medical School, Boston, United States.
Aurèlie Massoni-LaporteUniversity of Bordeaux, CNRS, European Institute of Chemistry and Biology, IBGC, UMR 5095, Pessac, France.
Caner ÜnlüUniversity of Bordeaux, CNRS, European Institute of Chemistry and Biology, IBGC, UMR 5095, Pessac, France.ORCID 0000-0002-0612-3111
Laure BatailleUniversity of Bordeaux, CNRS, European Institute of Chemistry and Biology, IBGC, UMR 5095, Pessac, France.
Floriane Saint ArramonUniversity of Bordeaux, CNRS, European Institute of Chemistry and Biology, IBGC, UMR 5095, Pessac, France.
Steven P GygiDepartment of Cell Biology, Harvard Medical School, Boston, United States.
Derek McCuskerUniversity of Bordeaux, CNRS, European Institute of Chemistry and Biology, IBGC, UMR 5095, Pessac, France.ORCID 0000-0003-1455-1711
Centre National de la Recherche Scientifique · FRHarvard University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Scaffold proteins modulate signalling pathway activity spatially and temporally. In budding yeast, the scaffold Bem1 contributes to polarity axis establishment by regulating the GTPase Cdc42. Although different models have been proposed for Bem1 function, there is little direct evidence for an underlying mechanism. Here, we find that Bem1 directly augments the guanine exchange factor (GEF) activity of Cdc24. Bem1 also increases GEF phosphorylation by the p21-activated kinase (PAK), Cla4. Phosphorylation abrogates the scaffold-dependent stimulation of GEF activity, rendering Cdc24 insensitive to additional Bem1. Thus, Bem1 stimulates GEF activity in a reversible fashion, contributing to signalling flux through Cdc42. The contribution of Bem1 to GTPase dynamics was borne-out by in vivo imaging: active Cdc42 was enriched at the cell pole in hypophosphorylated cdc24 mutants, while hyperphosphorylated cdc24 mutants that were resistant to scaffold stimulation displayed a deficit in active Cdc42 at the pole. These findings illustrate the self-regulatory properties that scaffold proteins confer on signalling pathways.

Indexed as

Adaptor Proteins, Signal Transducingcdc42 GTP-Binding Protein, Saccharomyces cerevisiaeChloride ChannelsGuanosine TriphosphateIntravital MicroscopyMicroscopySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionAdaptor Proteins, Signal TransducingBEM1 protein, S cerevisiaecdc42 GTP-Binding Protein, Saccharomyces cerevisiaeChloride ChannelsGEF1 protein, S cerevisiaeGuanosine TriphosphateSaccharomyces cerevisiae Proteinscell biologycell polarityRho GTPaseS. cerevisiaesignaling

Identifiers

PMID28304276
PMCPMC5386590
OpenAlexW2597144747

What OpenQuestion holds

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Registered trials

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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.