Evidence map›Paper›PMID 25060237›Full record

ArticleNature communications2014

Multi-protein assemblies underlie the mesoscale organization of the plasma membrane.

Sinem K Saka, Alf Honigmann, Christian Eggeling, Stefan W Hell, Thorsten Lang, Silvio O Rizzoli

Abstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.

0numbers the graph read from it
0cells of the map it votes in
97citing 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

97 citing papers in PubMed.

  1. Spatial Deconstruction of the Plasma Membrane.Journal of the American Chemical Society · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. CD9-association with PIPFEBS open bio · 2025
    Article
  7. Article
  8. Higher-order transient membrane protein structures.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Cluster parameter-based DBSCAN maps for image characterization.Computational and structural biotechnology journal · 2025
    Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Role of the membrane anchor in the regulation of Lck activity.The Journal of biological chemistry · 2022
    Article
  18. Review
  19. Article
  20. Article

37 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.

Sinem K Saka1] Department of Neuro- and Sensory Physiology, University of Göttingen Medical Centre, and Centre for Nanoscale Microscopy and Molecular Physiology of the Brain (CNMPB), 37075 Göttingen, Germany [2] International Max Planck Research School Molecular Biology, 37077 Göttingen, Germany.
Alf HonigmannDepartment of Nanobiophotonics, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
Christian EggelingMRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, Oxford OX3 9DS, UK.
Stefan W HellDepartment of Nanobiophotonics, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
Thorsten LangDepartment of Membrane Biochemistry, Life and Medical Sciences (LIMES) Institute, University of Bonn, 53115 Bonn, Germany.
Silvio O RizzoliDepartment of Neuro- and Sensory Physiology, University of Göttingen Medical Centre, and Centre for Nanoscale Microscopy and Molecular Physiology of the Brain (CNMPB), 37075 Göttingen, Germany.

Funding

Medical Research Council MC_UU_12010/9Medical Research Council MR/K01577X/1
6 · The paper itself

Abstract

Most proteins have uneven distributions in the plasma membrane. Broadly speaking, this may be caused by mechanisms specific to each protein, or may be a consequence of a general pattern that affects the distribution of all membrane proteins. The latter hypothesis has been difficult to test in the past. Here, we introduce several approaches based on click chemistry, through which we study the distribution of membrane proteins in living cells, as well as in membrane sheets. We found that the plasma membrane proteins form multi-protein assemblies that are long lived (minutes), and in which protein diffusion is restricted. The formation of the assemblies is dependent on cholesterol. They are separated and anchored by the actin cytoskeleton. Specific proteins are preferentially located in different regions of the assemblies, from their cores to their edges. We conclude that the assemblies constitute a basic mesoscale feature of the membrane, which affects the patterning of most membrane proteins, and possibly also their activity.

Indexed as

ActinsAnimalsCell FusionCell MembraneChlorocebus aethiopsCholesterolClick ChemistryCOS CellsCytoskeletonFluorescence Recovery After PhotobleachingMembrane ProteinsMultiprotein ComplexesPC12 CellsRatsActinsCholesterolMembrane ProteinsMultiprotein Complexes

Identifiers

PMID25060237
PMCPMC4124874

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.