Evidence map›Paper›PMID 37011205›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2023

Phase transition of tensin-1 during the focal adhesion disassembly and cell division.

Yuh-Ru Julie Lee, Soichiro Yamada, Su Hao Lo

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

14 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. The role and regulation of integrins in cell migration and invasion.Nature reviews. Molecular cell biology · 2025
    Review
  10. Somatic BrafAngiogenesis · 2024
    Article
  11. Article
  12. ULK/Atg1: phasing in and out of autophagy.Trends in biochemical sciences · 2024
    Review
  13. Review
  14. Tensins in Kidney Function and Diseases.Life (Basel, Switzerland) · 2023
    Review
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

3 authors at 1 institution in 1 country.

Yuh-Ru Julie LeeDepartment of Plant Biology, University of California, Davis, CA 95616.ORCID 0000-0001-7450-6395
Soichiro YamadaDepartment of Biomedical Engineering, University of California, Davis, CA 95616.ORCID 0000-0001-6413-0814
Su Hao LoDepartment of Biochemistry and Molecular Medicine, University of California, Davis, CA 95817.ORCID 0000-0002-2675-9387
University of California, Davis · US

Funding

Staff InvestigatorsP30CA093373 · NCI · UNIVERSITY OF CALIFORNIA DAVIS · PI Laura Marcu · 2002 to 2026
$84.9M
Molecular basis of force-sensing by the keratin networkR01GM148706 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI Soichiro Yamada · 2023 to 2026
$1.7M
NCI NIH HHS P30 CA093373NIGMS NIH HHS R01 GM148706
6 · The paper itself

Abstract

Biomolecular condensates are nonmembranous structures that are mainly formed through liquid-liquid phase separation. Tensins are focal adhesion (FA) proteins linking the actin cytoskeleton to integrin receptors. Here, we report that GFP-tagged tensin-1 (TNS1) proteins phase-separate to form biomolecular condensates in cells. Live-cell imaging showed that new TNS1 condensates are budding from the disassembling ends of FAs, and the presence of these condensates is cell cycle dependent. TNS1 condensates dissolve immediately prior to mitosis and rapidly reappear while postmitotic daughter cells establish new FAs. TNS1 condensates contain selected FA proteins and signaling molecules such as pT308Akt but not pS473Akt, suggesting previously unknown roles of TNS1 condensates in disassembling FAs, as the storage of core FA components and the signaling intermediates.

Indexed as

Focal AdhesionsSignal TransductionCell AdhesionCell DivisionProteinsTensinsProteinsTensinsbiomolecular condensatecell divisionfocal adhesiontensinTNS1

Identifiers

PMID37011205
PMCPMC10104483
OpenAlexW4362520777

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.