Evidence map›Paper›PMID 18538663›Full record

ArticleMolecular cell2008

Regulation of cell signaling dynamics by the protein kinase-scaffold Ste5.

Nan Hao, Sujata Nayak, Marcelo Behar, Ryan H Shanks, Michal J Nagiec, Beverly Errede, Jeffrey Hasty, Timothy C Elston, Henrik G Dohlman

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

77 citing papers in PubMed, 125 citations in OpenAlex.

  1. Variable thresholds for phosphorylation targets of the ERK signaling pathway.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Design patterns of biological cells.BioEssays : news and reviews in molecular, cellular and developmental biology · 2024
    Review
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  20. Testing the limits of gradient sensing.PLoS computational biology · 2017
    Article

17 more citing papers are in PubMed but not listed here.

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 1 country.

Nan HaoDepartment of Pharmacology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Sujata Nayak
Marcelo Behar
Ryan H Shanks
Michal J Nagiec
Beverly Errede
Jeffrey Hasty
Timothy C Elston
Henrik G Dohlman
University of North Carolina at Chapel Hill · USUniversity of California, San Diego · US

Funding

CARDIOVASCULAR SURGERY/BIOENGINEERING TRAININGT32HL007089 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CHIEN, SHU · 1985 to 2009
$9.3M
Modeling Feedback Regulation of Cell SignalingR01GM073180 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI DOHLMAN, HENRIK G. · 2005 to 2012
$2.6M
MAP kinase regulation of cell-fate transitions in yeastR01GM084071 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ELSTON, TIMOTHY C, ERREDE, BEVERLY · 2009 to 2012
$1.4M
NHLBI NIH HHS T32 HL007089NIGMS NIH HHS R01 GM073180
6 · The paper itself

Abstract

Cell differentiation requires the ability to detect and respond appropriately to a variety of extracellular signals. Here we investigate a differentiation switch induced by changes in the concentration of a single stimulus. Yeast cells exposed to high doses of mating pheromone undergo cell division arrest. Cells at intermediate doses become elongated and divide in the direction of a pheromone gradient (chemotropic growth). Either of the pheromone-responsive MAP kinases, Fus3 and Kss1, promotes cell elongation, but only Fus3 promotes chemotropic growth. Whereas Kss1 is activated rapidly and with a graded dose-response profile, Fus3 is activated slowly and exhibits a steeper dose-response relationship (ultrasensitivity). Fus3 activity requires the scaffold protein Ste5; when binding to Ste5 is abrogated, Fus3 behaves like Kss1, and the cells no longer respond to a gradient or mate efficiently with distant partners. We propose that scaffold proteins serve to modulate the temporal and dose-response behavior of the MAP kinase.

Indexed as

MAP Kinase Signaling SystemAdaptor Proteins, Signal TransducingCell DifferentiationEnzyme ActivationMitogen-Activated Protein KinasesPheromonesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdaptor Proteins, Signal TransducingFUS3 protein, S cerevisiaeKSS1 protein, S cerevisiaeMitogen-Activated Protein KinasesPheromonesSaccharomyces cerevisiae ProteinsSTE5 protein, S cerevisiae

Identifiers

PMID18538663
PMCPMC2518723
OpenAlexW2141999425

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.