Evidence map›Paper›PMID 25321392›Full record

ArticleeLife2014

Phase transitions of multivalent proteins can promote clustering of membrane receptors.

Sudeep Banjade, Michael K Rosen

Open access · goldAbstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 331 papers.

0numbers the graph read from it
0cells of the map it votes in
331citing papers in PubMed
9.4field-weighted citation impact, top 1% 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

331 citing papers in PubMed, 621 citations in OpenAlex.

  1. Review
  2. LAT condensation gates PLCγ1 activation via bimodal LAT phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Review
  5. Review
  6. Patchy Membrane-Directed Multiphase Complex Coacervation.Journal of the American Chemical Society · 2026
    Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. Article
  13. Munc13 serves as a molecular filter for SNARE sorting and assembly in active zone condensates.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review

271 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

2 authors at 2 institutions in 1 country.

Sudeep BanjadeDepartment of Biophysics, Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, United States.
Michael K RosenDepartment of Biophysics, Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, United States.
Southwestern Medical Center · USThe University of Texas Southwestern Medical Center · US

Funding

STRUCTURAL STUDY OF RHO-GTPASE REGULATORS AND EFFECTORSR01GM056322 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI ROSEN, MICHAEL K · 1997 to 2019
$5.7M
Howard Hughes Medical InstituteNIGMS NIH HHS R01-GM56322
6 · The paper itself

Abstract

Clustering of proteins into micrometer-sized structures at membranes is observed in many signaling pathways. Most models of clustering are specific to particular systems, and relationships between physical properties of the clusters and their molecular components are not well understood. We report biochemical reconstitution on supported lipid bilayers of protein clusters containing the adhesion receptor Nephrin and its cytoplasmic partners, Nck and N-WASP. With Nephrin attached to the bilayer, multivalent interactions enable these proteins to polymerize on the membrane surface and undergo two-dimensional phase separation, producing micrometer-sized clusters. Dynamics and thermodynamics of the clusters are modulated by the valencies and affinities of the interacting species. In the presence of the Arp2/3 complex, the clusters assemble actin filaments, suggesting that clustering of regulatory factors could promote local actin assembly at membranes. Interactions between multivalent proteins could be a general mechanism for cytoplasmic adaptor proteins to organize membrane receptors into micrometer-scale signaling zones.

Indexed as

Phase TransitionActin-Related Protein 2-3 ComplexActinsAdaptor Proteins, Signal TransducingAmino Acid MotifsAmino Acid SequenceAnimalsCell MembraneCluster AnalysisLipid BilayersMembrane ProteinsMolecular Sequence DataOncogene ProteinsPeptidesPolymerizationProtein BindingActin-Related Protein 2-3 ComplexActinsAdaptor Proteins, Signal TransducingLipid BilayersMembrane ProteinsNck proteinnephrinOncogene ProteinsPeptidesReceptors, Cell SurfaceWiskott-Aldrich Syndrome Protein, Neuronalactin regulationbiophysicscell biologyhumanmembrane clusteringmultivalencyphase separationpolymerizationsignal transductionstructural biology

Identifiers

PMID25321392
PMCPMC4238058
OpenAlexW2172098255

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.