Evidence map›Paper›PMID 25453114›Full record

ReviewJournal of cell science2014

Nanoclustering as a dominant feature of plasma membrane organization.

Maria F Garcia-Parajo, Alessandra Cambi, Juan A Torreno-Pina, Nancy Thompson, Ken Jacobson

Open access · bronzeAbstract readReview
In one paragraph

Review in Journal of cell science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 152 papers.

0numbers the graph read from it
0cells of the map it votes in
152citing papers in PubMed
9.3field-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

152 citing papers in PubMed, 294 citations in OpenAlex.

  1. Article
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  5. Spatial Deconstruction of the Plasma Membrane.Journal of the American Chemical Society · 2026
    Article
  6. Review
  7. Article
  8. Article
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  10. Cholesterol, PtdIns(4,5)PbioRxiv : the preprint server for biology · 2026
    Article
  11. Article
  12. Phosphatidylinositol 4,5-bisphosphate mediates Arl4D self-interaction to promote Pak1 signaling.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
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  19. Review
  20. Higher-order transient membrane protein structures.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article

92 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

5 authors at 3 institutions in 3 countries.

Maria F Garcia-ParajoICFO-Institut de Ciencies Fotoniques, Mediterranean Technology Park, 08860 Castelldefels (Barcelona), Spain ICREA-Institució Catalana de Recerca i Estudis Avançats, 08010 Barcelona, Spain maria.garcia-parajo@icfo.es frap@med.unc.edu.
Alessandra CambiNanobiophysics, MIRA Institute for Biomedical Technology and Technical Medicine and MESA+ Institute for Nanotechnology, University of Twente, 7522 NB Enschede, The Netherlands Department of Tumor Immunology, Radboud Institute for Molecular Life Sciences, Radboud University Medical Center, 6500 HB Nijmegen, The Netherlands.
Juan A Torreno-PinaICFO-Institut de Ciencies Fotoniques, Mediterranean Technology Park, 08860 Castelldefels (Barcelona), Spain.
Nancy ThompsonDepartment of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-3290, USA.
Ken JacobsonDepartment of Cell Biology and Physiology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7090, USA Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA maria.garcia-parajo@icfo.es frap@med.unc.edu.
Institute of Photonic Sciences · ESUniversity of North Carolina at Chapel Hill · USUniversity of Twente · NL

Funding

Structure and dynamics of membrane microdomains used for viral entry and egressR01GM041402 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI JACOBSON, KENNETH A · 1989 to 2016
$4.8M
NIGMS NIH HHS R01 GM041402
6 · The paper itself

Abstract

Early studies have revealed that some mammalian plasma membrane proteins exist in small nanoclusters. The advent of super-resolution microscopy has corroborated and extended this picture, and led to the suggestion that many, if not most, membrane proteins are clustered at the plasma membrane at nanoscale lengths. In this Commentary, we present selected examples of glycosylphosphatidyl-anchored proteins, Ras family members and several immune receptors that provide evidence for nanoclustering. We advocate the view that nanoclustering is an important part of the hierarchical organization of proteins in the plasma membrane. According to this emerging picture, nanoclusters can be organized on the mesoscale to form microdomains that are capable of supporting cell adhesion, pathogen binding and immune cell-cell recognition amongst other functions. Yet, a number of outstanding issues concerning nanoclusters remain open, including the details of their molecular composition, biogenesis, size, stability, function and regulation. Notions about these details are put forth and suggestions are made about nanocluster function and why this general feature of protein nanoclustering appears to be so prevalent.

Indexed as

NanoparticlesAnimalsCell MembraneHumansMembrane LipidsMembrane MicrodomainsMembrane ProteinsMicroscopyProtein Aggregatesras ProteinsReceptors, ImmunologicMembrane LipidsMembrane ProteinsProtein Aggregatesras ProteinsReceptors, ImmunologicPlasma membraneProtein nanoclusteringSuper-resolution microscopy

Identifiers

PMID25453114
PMCPMC4260763
OpenAlexW2157246740

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.