Evidence map›Paper›PMID 38605024›Full record

ArticleNature communications2024

Hydrophobic mismatch drives self-organization of designer proteins into synthetic membranes.

Justin A Peruzzi, Jan Steinkühler, Timothy Q Vu, Taylor F Gunnels, Vivian T Hu, Peilong Lu, David Baker, Neha P Kamat

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Membrane-Associated Biomolecules for Synthetic Cell Signalling.Chembiochem : a European journal of chemical biology · 2026
    Review
  2. Hydrophobic mismatch induces lipid sorting based on tail unsaturation.bioRxiv : the preprint server for biology · 2026
    Article
  3. The Evolution of Lipids from Solvents to Substrates.Annual review of biophysics · 2026
    Review
  4. Spatially regulated mRNA translation enables functional membrane protein integration in synthetic cells.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. CD24 Regulates the Formation of Ectosomes in B Lymphocytes.Journal of extracellular vesicles · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Functional Regulation of Aquaporin Dynamics by Lipid Bilayer Composition.bioRxiv : the preprint server for biology · 2023
    Article
  17. Engineering transmembrane signal transduction in synthetic membranes using two-component systems.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  18. Article
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

8 authors.

Justin A PeruzziDepartment of Chemical and Biological Engineering, Northwestern University, Evanston, IL, 60208, USA.ORCID http://orcid.org/0000-0003-3782-1382
Jan SteinkühlerCenter for Synthetic Biology, Northwestern University, Evanston, IL, 60208, USA.ORCID http://orcid.org/0000-0003-4226-7945
Timothy Q VuCenter for Synthetic Biology, Northwestern University, Evanston, IL, 60208, USA.
Taylor F GunnelsCenter for Synthetic Biology, Northwestern University, Evanston, IL, 60208, USA.ORCID http://orcid.org/0000-0002-2498-2630
Vivian T HuCenter for Synthetic Biology, Northwestern University, Evanston, IL, 60208, USA.ORCID http://orcid.org/0009-0001-5391-1049
Peilong LuKey Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou, Zhejiang, China.ORCID http://orcid.org/0000-0001-5894-9268
David BakerDepartment of Biochemistry, University of Washington, Seattle, WA, 98195, USA.ORCID http://orcid.org/0000-0001-7896-6217
Neha P KamatCenter for Synthetic Biology, Northwestern University, Evanston, IL, 60208, USA. nkamat@northwestern.edu.ORCID http://orcid.org/0000-0001-9362-6106

Funding

Developing Capacity to Evaluate Training Programs via Development of Human, Institutional and Social CapitalT32GM008449 · NIGMS · NORTHWESTERN UNIVERSITY · PI LEONARD, JOSHUA NATHANIEL · 1993 to 2023
$7.8M
NIGMS NIH HHS T32 GM008449
6 · The paper itself

Abstract

The organization of membrane proteins between and within membrane-bound compartments is critical to cellular function. Yet we lack approaches to regulate this organization in a range of membrane-based materials, such as engineered cells, exosomes, and liposomes. Uncovering and leveraging biophysical drivers of membrane protein organization to design membrane systems could greatly enhance the functionality of these materials. Towards this goal, we use de novo protein design, molecular dynamic simulations, and cell-free systems to explore how membrane-protein hydrophobic mismatch could be used to tune protein cotranslational integration and organization in synthetic lipid membranes. We find that membranes must deform to accommodate membrane-protein hydrophobic mismatch, which reduces the expression and co-translational insertion of membrane proteins into synthetic membranes. We use this principle to sort proteins both between and within membranes, thereby achieving one-pot assembly of vesicles with distinct functions and controlled split-protein assembly, respectively. Our results shed light on protein organization in biological membranes and provide a framework to design self-organizing membrane-based materials with applications such as artificial cells, biosensors, and therapeutic nanoparticles.

Indexed as

Artificial CellsMembrane ProteinsCell MembraneLipid BilayersLiposomesMembranesLipid BilayersLiposomesMembrane Proteins

Identifiers

PMID38605024
PMCPMC11009411

What OpenQuestion holds

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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.