Evidence map›Paper›PMID 30455180›Full record

ArticleThe Journal of general physiology2018

Ion channels can be allosterically regulated by membrane domains near a de-mixing critical point.

Ofer Kimchi, Sarah L Veatch, Benjamin B Machta

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2018. 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
0.8field-weighted citation impact, top 29% 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, 27 citations in OpenAlex.

  1. Protein-enhanced small molecule disruptors of ordered membrane domains.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  15. The plasma membrane as an adaptable fluid mosaic.Biochimica et biophysica acta. Biomembranes · 2023
    Review
  16. Article
  17. Critical Phenomena in Plasma Membrane Organization and Function.Annual review of physical chemistry · 2021
    Review
  18. Defining how multiple lipid species interact with inward rectifier potassium (Kir2) channels.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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

3 authors at 3 institutions in 1 country.

Ofer KimchiDepartment of Physics, Princeton University, Princeton, NJ.
Sarah L VeatchDepartment of Biophysics, University of Michigan, Ann Arbor, MI.
Benjamin B MachtaDepartment of Physics, Princeton University, Princeton, NJ benjamin.machta@yale.edu.ORCID 0000-0001-9065-614X
Harvard University · USPrinceton University · USUniversity of Michigan · US

Funding

MOLECULAR BIOPHYSICS TRAINING GRANTT32GM008313 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI MURTHY, VENKATESH N · 1989 to 2023
$14.6M
Ion channel regulation by heterogeneous membranesR01GM110052 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI VEATCH, SARAH L · 2014 to 2022
$2.9M
NIGMS NIH HHS R01 GM110052NIGMS NIH HHS T32 GM008313
6 · The paper itself

Abstract

Ion channels are embedded in the plasma membrane, a compositionally diverse two-dimensional liquid that has the potential to exert profound influence on their function. Recent experiments suggest that this membrane is poised close to an Ising critical point, below which cell-derived plasma membrane vesicles phase separate into coexisting liquid phases. Related critical points have long been the focus of study in simplified physical systems, but their potential roles in biological function have been underexplored. Here we apply both exact and stochastic techniques to the lattice Ising model to study several ramifications of proximity to criticality for idealized lattice channels, whose function is coupled through boundary interactions to critical fluctuations of membrane composition. Because of diverging susceptibilities of system properties to thermodynamic parameters near a critical point, such a lattice channel's activity becomes strongly influenced by perturbations that affect the critical temperature of the underlying Ising model. In addition, its kinetics acquire a range of time scales from its surrounding membrane, naturally leading to non-Markovian dynamics. Our model may help to unify existing experimental results relating the effects of small-molecule perturbations on membrane properties and ion channel function. We also suggest ways in which the role of this mechanism in regulating real ion channels and other membrane-bound proteins could be tested in the future.

Indexed as

Models, ChemicalAlgorithmsAllosteric RegulationComputer SimulationIon ChannelsKineticsIon Channels

Identifiers

PMID30455180
PMCPMC6279359
OpenAlexW2901159170

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.