Evidence map›Paper›PMID 24366544›Full record

ArticleMolecular and cellular biology2014

Signal integration by lipid-mediated spatial cross talk between Ras nanoclusters.

Yong Zhou, Hong Liang, Travis Rodkey, Nicholas Ariotti, Robert G Parton, John F Hancock

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

89 citing papers in PubMed, 137 citations in OpenAlex.

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  9. Loss of lipid asymmetry facilitates plasma membrane blebbing by decreasing membrane lipid packing.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  20. RAS GTPases and Interleaflet Coupling in the Plasma Membrane.Cold Spring Harbor perspectives in biology · 2023
    Review

29 more citing papers are in PubMed but not listed here.

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

6 authors at 2 institutions in 2 countries.

Yong ZhouDepartment of Integrative Biology and Pharmacology, University of Texas Health Science Center, Houston, Texas, USA.
Hong Liang
Travis Rodkey
Nicholas Ariotti
Robert G Parton
John F Hancock
The University of Texas Health Science Center at Houston · USUniversity of Queensland · AU

Funding

Structure and Function of Plasma membrane NanodomainsR01GM066717 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI HANCOCK, JOHN F · 2003 to 2012
$2.4M
NIGMS NIH HHS GM066717NIGMS NIH HHS R01 GM066717
6 · The paper itself

Abstract

Lipid-anchored Ras GTPases form transient, spatially segregated nanoclusters on the plasma membrane that are essential for high-fidelity signal transmission. The lipid composition of Ras nanoclusters, however, has not previously been investigated. High-resolution spatial mapping shows that different Ras nanoclusters have distinct lipid compositions, indicating that Ras proteins engage in isoform-selective lipid sorting and accounting for different signal outputs from different Ras isoforms. Phosphatidylserine is a common constituent of all Ras nanoclusters but is only an obligate structural component of K-Ras nanoclusters. Segregation of K-Ras and H-Ras into spatially and compositionally distinct lipid assemblies is exquisitely sensitive to plasma membrane phosphatidylserine levels. Phosphatidylserine spatial organization is also modified by Ras nanocluster formation. In consequence, Ras nanoclusters engage in remote lipid-mediated communication, whereby activated H-Ras disrupts the assembly and operation of spatially segregated K-Ras nanoclusters. Computational modeling and experimentation reveal that complex effects of caveolin and cortical actin on Ras nanoclustering are similarly mediated through regulation of phosphatidylserine spatiotemporal dynamics. We conclude that phosphatidylserine maintains the lateral segregation of diverse lipid-based assemblies on the plasma membrane and that lateral connectivity between spatially remote lipid assemblies offers important previously unexplored opportunities for signal integration and signal processing.

Indexed as

AnimalsCell LineCell MembraneCHO CellsCricetulusGenes, rasMembrane LipidsPhosphatidylserinesras ProteinsSignal TransductionMembrane LipidsPhosphatidylserinesras Proteins

Identifiers

PMID24366544
PMCPMC4023829
OpenAlexW1968075591

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.