Evidence map›Paper›PMID 22332778›Full record

ArticleThe journal of physical chemistry. B2012

The membrane environment can promote or suppress bistability in cell signaling networks.

Steven M Abel, Jeroen P Roose, Jay T Groves, Arthur Weiss, Arup K Chakraborty

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 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 20% 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, 46 citations in OpenAlex.

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  6. Diffusive search and trajectories on tubular networks: a propagator approach.The European physical journal. E, Soft matter · 2021
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  18. Stochastic transitions in a bistable reaction system on the membrane.Journal of the Royal Society, Interface · 2013
    Article
  19. 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

5 authors at 3 institutions in 1 country.

Steven M AbelDepartment of Chemical Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
Jeroen P Roose
Jay T Groves
Arthur Weiss
Arup K Chakraborty
Massachusetts Institute of Technology · USUniversity of California, San Francisco · USHoward Hughes Medical Institute · US

Funding

Understand the metabolic fitness of naïve T cellsP01AI091580 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI ARTHUR Robert SALOMON · 2011 to 2026
$31.1M
NIH Director's Pioneer AwardDP1OD001022 · OD · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI CHAKRABORTY, ARUP K. · 2006 to 2010
$4.1M
Howard Hughes Medical InstituteNIAID NIH HHS 1P01AI091580-01NIAID NIH HHS P01 AI091580NIH HHS DP1 OD001022
6 · The paper itself

Abstract

Many key biochemical reactions that mediate signal transduction in cells occur at the cell membrane, yet how the two-dimensional membrane environment influences the collective behavior of signaling networks is poorly understood. We study models of two topologically different signaling pathways that exhibit bistability, examining the effects of reduced protein mobility and increased concentration at the membrane, as well as effects due to differences in spatiotemporal correlations between the membrane environment and three-dimensional cytoplasm. The two model networks represent the distributive enzymatic modification of a protein at multiple sites and the positive feedback-mediated activation of a protein. In both cases, we find that confining proteins to a membrane-like environment can markedly alter the emergent dynamics. For the distributive protein modification network, increased concentration promotes bistability through enhanced protein-protein binding, while lower mobility and membrane-enhanced spatiotemporal correlations suppress bistability. For the positive feedback-mediated activation network, confinement to a membrane environment enhances protein activation, which can induce bistability or stabilize a monostable, active state. Importantly, the influence of the membrane environment on signaling dynamics can be qualitatively different for signaling modules with different network topologies.

Indexed as

Cell MembraneEnzyme ActivationEnzymesMembrane ProteinsProtein BindingProtein StabilitySignal TransductionEnzymesMembrane Proteins

Identifiers

PMID22332778
PMCPMC3321252
OpenAlexW1983378124

What OpenQuestion holds

Textmetadata
LicenceTDM
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.