Evidence map›Paper›PMID 37078342›Full record

ArticleJournal of cell science2023

ConFERMing the role of talin in integrin activation and mechanosignaling.

Michael Bachmann, Baihao Su, Rolle Rahikainen, Vesa P Hytönen, Jinhua Wu, Bernhard Wehrle-Haller

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

11 citing papers in PubMed, 13 citations in OpenAlex.

  1. The Impact of Zinc on T Cell Motility and the Immunological Synapse.International journal of molecular sciences · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Skeletogenic Expression of Integrin Alpha, Talin and Npnt Genes and Npnt Role in Sea Urchin Skeletogenesis.Journal of experimental zoology. Part B, Molecular and developmental evolution · 2026
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. 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

6 authors at 2 institutions in 2 countries.

Michael BachmannDepartment of Cell Physiology and Metabolism, Centre Médical Universitaire, 1211 Geneva 4, Switzerland.ORCID 0000-0001-9450-3458
Baihao SuMolecular Therapeutics Program, Fox Chase Cancer Center, 333 Cottman Ave, Philadelphia, PA 19111, USA.
Rolle RahikainenFaculty of Medicine and Health Technology, Arvo Ylpön katu 34, Tampere University, FI-33520 Tampere, Finland.ORCID 0000-0003-1265-862X
Vesa P HytönenFaculty of Medicine and Health Technology, Arvo Ylpön katu 34, Tampere University, FI-33520 Tampere, Finland.ORCID 0000-0002-9357-1480
Jinhua WuMolecular Therapeutics Program, Fox Chase Cancer Center, 333 Cottman Ave, Philadelphia, PA 19111, USA.ORCID 0000-0001-5913-0633
Bernhard Wehrle-HallerDepartment of Cell Physiology and Metabolism, Centre Médical Universitaire, 1211 Geneva 4, Switzerland.ORCID 0000-0002-1159-1147
Fox Chase Cancer Center · USTampere University · FI

Funding

Novel Regulatory Mechanisms Underlying Inside-out Integrin ActivationR35GM119560 · NIGMS · RESEARCH INST OF FOX CHASE CAN CTR · PI Jinhua Wu · 2016 to 2026
$5.0M
NIGMS NIH HHS R35 GM119560
6 · The paper itself

Abstract

Talin (herein referring to the talin-1 form), is a cytoskeletal adapter protein that binds integrin receptors and F-actin, and is a key factor in the formation and regulation of integrin-dependent cell-matrix adhesions. Talin forms the mechanical link between the cytoplasmic domain of integrins and the actin cytoskeleton. Through this linkage, talin is at the origin of mechanosignaling occurring at the plasma membrane-cytoskeleton interface. Despite its central position, talin is not able to fulfill its tasks alone, but requires help from kindlin and paxillin to detect and transform the mechanical tension along the integrin-talin-F-actin axis into intracellular signaling. The talin head forms a classical FERM domain, which is required to bind and regulate the conformation of the integrin receptor, as well as to induce intracellular force sensing. The FERM domain allows the strategic positioning of protein-protein and protein-lipid interfaces, including the membrane-binding and integrin affinity-regulating F1 loop, as well as the interaction with lipid-anchored Rap1 (Rap1a and Rap1b in mammals) GTPase. Here, we summarize the structural and regulatory features of talin and explain how it regulates cell adhesion and force transmission, as well as intracellular signaling at integrin-containing cell-matrix attachment sites.

Indexed as

ActinsTalinAnimalsCell AdhesionCytoskeletal ProteinsIntegrinsLipidsMammalsActinsCytoskeletal ProteinsIntegrinsLipidsTalinActinAdhesionKindlinPaxillinPIP2Rap1RIAMSignalingVinculin

Identifiers

PMID37078342
PMCPMC10198623
OpenAlexW4366598696

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.