Evidence map›Paper›PMID 29505559›Full record

ArticlePLoS computational biology2018

Cytosolic proteins can exploit membrane localization to trigger functional assembly.

Osman N Yogurtcu, Margaret E Johnson

Open access · goldAbstract read
In one paragraph

Article in PLoS computational biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.9field-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

37 citing papers in PubMed, 64 citations in OpenAlex.

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  10. Intrinsically disordered region amplifies membrane remodeling to augment selective ER-phagy.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
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  16. Modeling membrane reshaping driven by dynamic protein assemblies.Current opinion in structural biology · 2023
    Review
  17. Autoregulation of HBritish journal of cancer · 2022
    Article
  18. 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

2 authors at 1 institution in 1 country.

Osman N YogurtcuDepartment of Biophysics, Johns Hopkins University, Baltimore, MD, United States of America.ORCID 0000-0003-4987-3753
Margaret E JohnsonDepartment of Biophysics, Johns Hopkins University, Baltimore, MD, United States of America.ORCID 0000-0001-9881-291X
Johns Hopkins University · US

Funding

Modeling the nucleation of clathrin coated vesicles at the cell membraneR00GM098371 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI JOHNSON, MARGARET ELLEN · 2013 to 2015
$743k
NIGMS NIH HHS R00 GM098371
6 · The paper itself

Abstract

Cell division, endocytosis, and viral budding would not function without the localization and assembly of protein complexes on membranes. What is poorly appreciated, however, is that by localizing to membranes, proteins search in a reduced space that effectively drives up concentration. Here we derive an accurate and practical analytical theory to quantify the significance of this dimensionality reduction in regulating protein assembly on membranes. We define a simple metric, an effective equilibrium constant, that allows for quantitative comparison of protein-protein interactions with and without membrane present. To test the importance of membrane localization for driving protein assembly, we collected the protein-protein and protein-lipid affinities, protein and lipid concentrations, and volume-to-surface-area ratios for 46 interactions between 37 membrane-targeting proteins in human and yeast cells. We find that many of the protein-protein interactions between pairs of proteins involved in clathrin-mediated endocytosis in human and yeast cells can experience enormous increases in effective protein-protein affinity (10-1000 fold) due to membrane localization. Localization of binding partners thus triggers robust protein complexation, suggesting that it can play an important role in controlling the timing of endocytic protein coat formation. Our analysis shows that several other proteins involved in membrane remodeling at various organelles have similar potential to exploit localization. The theory highlights the master role of phosphoinositide lipid concentration, the volume-to-surface-area ratio, and the ratio of 3D to 2D equilibrium constants in triggering (or preventing) constitutive assembly on membranes. Our simple model provides a novel quantitative framework for interpreting or designing in vitro experiments of protein complexation influenced by membrane binding.

Indexed as

Cell MembraneComputer SimulationCytoplasmCytosolDiffusionEndocytosisMembrane ProteinsModels, BiologicalMultiprotein ComplexesProtein BindingMembrane ProteinsMultiprotein Complexes

Identifiers

PMID29505559
PMCPMC5854442
OpenAlexW2951202896

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.