Evidence map›Paper›PMID 29694870›Full record

ArticleBiophysical journal2018

Protein Partitioning into Ordered Membrane Domains: Insights from Simulations.

Xubo Lin, Alemayehu A Gorfe, Ilya Levental

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.4field-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

35 citing papers in PubMed, 72 citations in OpenAlex.

  1. Hydrophobic mismatch induces lipid sorting based on tail unsaturation.bioRxiv : the preprint server for biology · 2026
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  13. DHHC17 Is a New Regulator of AMPK Signaling.Molecular and cellular biology · 2022
    Article
  14. Review
  15. Review
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  18. Article
  19. Review
  20. Regulatory effects of post-translational modifications on zDHHCThe Journal of biological chemistry · 2020
    Review
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 2 institutions in 2 countries.

Xubo LinDepartment of Integrative Biology and Pharmacology, McGovern Medical School, The University of Texas Health Science Center at Houston, Houston, Texas; School of Biological Science and Medical Engineering, Beihang University, Beijing, China; Beijing Advanced Innovation Center for Biomedical Engineering, Beihang University, Beijing, China.
Alemayehu A GorfeDepartment of Integrative Biology and Pharmacology, McGovern Medical School, The University of Texas Health Science Center at Houston, Houston, Texas. Electronic address: alemayehu.g.abebe@uth.tmc.edu.
Ilya LeventalDepartment of Integrative Biology and Pharmacology, McGovern Medical School, The University of Texas Health Science Center at Houston, Houston, Texas. Electronic address: ilya.levental@uth.tmc.edu.
The University of Texas Health Science Center at Houston · USBeihang University · CN

Funding

Lipidomic, biophysical, and functional differentiation of Mesenchymal Stem Cell membranesR01GM114282 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI LEVENTAL, ILYA · 2015 to 2019
$1.7M
Nanoclusters of Lipid-anchored Proteins in Membranes: How and where they appearR01GM100078 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI GORFE, ALEMAYEHU A. · 2012 to 2016
$1.4M
Structural determinants and functional consequences of protein partitioning to ordered membrane microdomains.R01GM124072 · NIGMS · UNIVERSITY OF VIRGINIA · PI LEVENTAL, ILYA · 2017 to 2019
$961k
NIGMS NIH HHS R01 GM100078NIGMS NIH HHS R01 GM114282NIGMS NIH HHS R01 GM124072
6 · The paper itself

Abstract

Cellular membranes are laterally organized into domains of distinct structures and compositions by the differential interaction affinities between various membrane lipids and proteins. A prominent example of such structures are lipid rafts, which are ordered, tightly packed domains that have been widely implicated in cellular processes. The functionality of raft domains is driven by their selective recruitment of specific membrane proteins to regulate their interactions and functions; however, there have been few general insights into the factors that determine the partitioning of membrane proteins between coexisting liquid domains. In this work, we used extensive coarse-grained and atomistic molecular dynamics simulations, potential of mean force calculations, and conceptual models to describe the partitioning dynamics and energetics of a model transmembrane domain from the linker of activation of T cells. We find that partitioning between domains is determined by an interplay between protein-lipid interactions and differential lipid packing between raft and nonraft domains. Specifically, we show that partitioning into ordered domains is promoted by preferential interactions between peptides and ordered lipids, mediated in large part by modification of the peptides by saturated fatty acids (i.e., palmitoylation). Ordered phase affinity is also promoted by elastic effects, specifically hydrophobic matching between the membrane and the peptide. Conversely, ordered domain partitioning is disfavored by the tight molecular packing of the lipids therein. The balance of these dominant drivers determines partitioning. In the case of the wild-type linker of activation of T cells transmembrane domain, these factors combine to yield enrichment of the peptide at L

Indexed as

Molecular Dynamics SimulationAdaptor Proteins, Signal TransducingAmino Acid SequenceHydrophobic and Hydrophilic InteractionsMembrane MicrodomainsProtein DomainsAdaptor Proteins, Signal Transducing

Identifiers

PMID29694870
PMCPMC5937199
OpenAlexW2801994775

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.