Evidence map›Paper›PMID 38049424›Full record

ArticleNature communications2023

Transmembrane coupling of liquid-like protein condensates.

Yohan Lee, Sujin Park, Feng Yuan, Carl C Hayden, Liping Wang, Eileen M Lafer, Siyoung Q Choi, Jeanne C Stachowiak

Abstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Biomolecular Condensates Can Induce Local Membrane Potentials.Small (Weinheim an der Bergstrasse, Germany) · 2026
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Biomolecular Condensates can Induce Local Membrane Potentials.bioRxiv : the preprint server for biology · 2024
    Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. 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.

Yohan Lee *Department of Biomedical Engineering, The University of Texas at Austin, Austin, TX, USA.ORCID 0000-0002-0440-8092
Sujin Park *Department of Chemical and Biomolecular Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, Republic of Korea.ORCID 0000-0001-7819-5678
Feng YuanDepartment of Biomedical Engineering, The University of Texas at Austin, Austin, TX, USA.ORCID 0000-0002-6592-1578
Carl C HaydenDepartment of Biomedical Engineering, The University of Texas at Austin, Austin, TX, USA.
Liping WangDepartment of Biochemistry and Structural Biology, The University of Texas Health Science Center at San Antonio, San Antonio, TX, USA.
Eileen M LaferDepartment of Biochemistry and Structural Biology, The University of Texas Health Science Center at San Antonio, San Antonio, TX, USA.
Siyoung Q ChoiDepartment of Chemical and Biomolecular Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, Republic of Korea.
Jeanne C StachowiakDepartment of Biomedical Engineering, The University of Texas at Austin, Austin, TX, USA. jcstach@austin.utexas.edu.ORCID 0000-0003-2501-142X

Funding

Protein Networks as Synergistic Drivers of Membrane RemodelingR35GM139531 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI Jeanne Casstevens Stachowiak · 2021 to 2026
$4.0M
NIGMS NIH HHS R35 GM139531
6 · The paper itself

Abstract

Liquid-liquid phase separation of proteins occurs on both surfaces of cellular membranes during diverse physiological processes. In vitro reconstitution could provide insight into the mechanisms underlying these events. However, most existing reconstitution techniques provide access to only one membrane surface, making it difficult to probe transmembrane phenomena. To study protein phase separation simultaneously on both membrane surfaces, we developed an array of freestanding planar lipid membranes. Interestingly, we observed that liquid-like protein condensates on one side of the membrane colocalized with those on the other side, resulting in transmembrane coupling. Our results, based on lipid probe partitioning and mobility of lipids, suggest that protein condensates locally reorganize membrane lipids, a process which could be explained by multiple effects. These findings suggest a mechanism by which signals originating on one side of a biological membrane, triggered by protein phase separation, can be transferred to the opposite side.

Indexed as

LipidsProteinsCell MembraneLipidsProteins

Identifiers

PMID38049424
PMCPMC10696066

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.