Evidence map›Paper›PMID 36997644›Full record

ArticleNature chemical biology2023

Membrane phase separation drives responsive assembly of receptor signaling domains.

Sarah A Shelby, Ivan Castello-Serrano, Kathleen C Wisser, Ilya Levental, Sarah L Veatch

Abstract read
In one paragraph

Article in Nature chemical biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing 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

82 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
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  5. Review
  6. Spatial Deconstruction of the Plasma Membrane.Journal of the American Chemical Society · 2026
    Article
  7. Article
  8. Review
  9. Review
  10. Protein-enhanced small molecule disruptors of ordered membrane domains.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Sarah A ShelbyProgram in Biophysics, University of Michigan, Ann Arbor, MI, USA.
Ivan Castello-SerranoDepartment of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA, USA.ORCID 0000-0002-2307-6476
Kathleen C WisserProgram in Biophysics, University of Michigan, Ann Arbor, MI, USA.
Ilya LeventalDepartment of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA, USA.ORCID 0000-0002-1206-9545
Sarah L VeatchProgram in Biophysics, University of Michigan, Ann Arbor, MI, USA. sveatch@umich.edu.ORCID 0000-0002-9317-2308

Funding

The functional organization of mammalian membranes-Equipment SupplementR35GM134949 · NIGMS · UNIVERSITY OF VIRGINIA · PI Ilya Levental · 2020 to 2026
$3.8M
Ion channel regulation by heterogeneous membranesR01GM110052 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI VEATCH, SARAH L · 2014 to 2022
$2.9M
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 GM110052NIGMS NIH HHS R01 GM124072NIGMS NIH HHS R35 GM134949
6 · The paper itself

Abstract

Plasma membrane heterogeneity has been tied to a litany of cellular functions and is often explained by analogy to membrane phase separation; however, models based on phase separation alone fall short of describing the rich organization available within cell membranes. Here we present comprehensive experimental evidence motivating an updated model of plasma membrane heterogeneity in which membrane domains assemble in response to protein scaffolds. Quantitative super-resolution nanoscopy measurements in live B lymphocytes detect membrane domains that emerge upon clustering B cell receptors (BCRs). These domains enrich and retain membrane proteins based on their preference for the liquid-ordered phase. Unlike phase-separated membranes that consist of binary phases with defined compositions, membrane composition at BCR clusters is modulated through the protein constituents in clusters and the composition of the membrane overall. This tunable domain structure is detected through the variable sorting of membrane probes and impacts the magnitude of BCR activation.

Indexed as

Membrane MicrodomainsMembrane ProteinsCell MembraneMembrane Proteins

Identifiers

PMID36997644
PMCPMC10771812

What OpenQuestion holds

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Registered trials

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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.