Evidence map›Paper›PMID 29089556›Full record

ArticleNature communications2017

Structural determinants and functional consequences of protein affinity for membrane rafts.

Joseph H Lorent, Blanca Diaz-Rohrer, Xubo Lin, Kevin Spring, Alemayehu A Gorfe, Kandice R Levental, Ilya Levental

Erratum issuedAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 175 papers.

0numbers the graph read from it
0cells of the map it votes in
175citing papers in PubMed
–field-weighted citation impact
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

175 citing papers in PubMed.

  1. Review
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  8. Apical and basolateral plasma membranes in epithelial cells have distinct lipidomes and biophysical properties.Proceedings of the National Academy of Sciences of the United States of America · 2026
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115 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Joseph H LorentMcGovern Medical School, University of Texas Health Science Center, Houston MSB 4.202A, 6431 Fannin St, Houston, TX, 77096, USA.
Blanca Diaz-RohrerMcGovern Medical School, University of Texas Health Science Center, Houston MSB 4.202A, 6431 Fannin St, Houston, TX, 77096, USA.
Xubo LinMcGovern Medical School, University of Texas Health Science Center, Houston MSB 4.202A, 6431 Fannin St, Houston, TX, 77096, USA.ORCID http://orcid.org/0000-0002-4417-3582
Kevin SpringMcGovern Medical School, University of Texas Health Science Center, Houston MSB 4.202A, 6431 Fannin St, Houston, TX, 77096, USA.
Alemayehu A GorfeMcGovern Medical School, University of Texas Health Science Center, Houston MSB 4.202A, 6431 Fannin St, Houston, TX, 77096, USA.
Kandice R LeventalMcGovern Medical School, University of Texas Health Science Center, Houston MSB 4.202A, 6431 Fannin St, Houston, TX, 77096, USA.
Ilya LeventalMcGovern Medical School, University of Texas Health Science Center, Houston MSB 4.202A, 6431 Fannin St, Houston, TX, 77096, USA. ilya.levental@uth.tmc.edu.ORCID http://orcid.org/0000-0002-1206-9545

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

Eukaryotic plasma membranes are compartmentalized into functional lateral domains, including lipid-driven membrane rafts. Rafts are involved in most plasma membrane functions by selective recruitment and retention of specific proteins. However, the structural determinants of transmembrane protein partitioning to raft domains are not fully understood. Hypothesizing that protein transmembrane domains (TMDs) determine raft association, here we directly quantify raft affinity for dozens of TMDs. We identify three physical features that independently affect raft partitioning, namely TMD surface area, length, and palmitoylation. We rationalize these findings into a mechanistic, physical model that predicts raft affinity from the protein sequence. Application of these concepts to the human proteome reveals that plasma membrane proteins have higher raft affinity than those of intracellular membranes, consistent with raft-mediated plasma membrane sorting. Overall, our experimental observations and physical model establish general rules for raft partitioning of TMDs and support the central role of rafts in membrane traffic.

Indexed as

Amino Acid SequenceAnimalsCell LineHumansMembrane MicrodomainsMembrane ProteinsModels, BiologicalProtein BindingProtein DomainsProteomeRatsMembrane ProteinsProteome

Identifiers

PMID29089556
PMCPMC5663905

What OpenQuestion holds

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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.