Evidence map›Paper›PMID 33288722›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Crystal structure of the FERM-folded talin head reveals the determinants for integrin binding.

Pingfeng Zhang, Latifeh Azizi, Sampo Kukkurainen, Tong Gao, Mo Baikoghli, Marie-Claude Jacquier, Yijuan Sun, Juha A E Määttä, R Holland Cheng, Bernhard Wehrle-Haller and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

26 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. 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
  4. Article
  5. Article
  6. Biochemical and structural bases for talin ABSs-F-actin interactions.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Observational
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. Review
  19. Article
  20. The MeshCODE to scale-visualising synaptic binary information.Frontiers in cellular neuroscience · 2022
    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

12 authors at 4 institutions in 3 countries.

Pingfeng ZhangMolecular Therapeutics Program, Fox Chase Cancer Center, Philadelphia, PA 19111.ORCID 0000-0001-5985-4914
Latifeh AziziFaculty of Medicine and Health Technology, Tampere University, FI-33520 Tampere, Finland.
Sampo KukkurainenFaculty of Medicine and Health Technology, Tampere University, FI-33520 Tampere, Finland.
Tong GaoMolecular Therapeutics Program, Fox Chase Cancer Center, Philadelphia, PA 19111.
Mo BaikoghliDepartment of Molecular and Cellular Biology, University of California, Davis, CA 95616.ORCID 0000-0002-5786-602X
Marie-Claude JacquierDepartment of Cell Physiology and Metabolism, Centre Médical Universitaire, University of Geneva, 1211 Geneva 4, Switzerland.
Yijuan SunMolecular Therapeutics Program, Fox Chase Cancer Center, Philadelphia, PA 19111.
Juha A E MäättäFaculty of Medicine and Health Technology, Tampere University, FI-33520 Tampere, Finland.ORCID 0000-0003-3885-6149
R Holland ChengDepartment of Molecular and Cellular Biology, University of California, Davis, CA 95616.ORCID 0000-0002-2068-7271
Bernhard Wehrle-HallerDepartment of Cell Physiology and Metabolism, Centre Médical Universitaire, University of Geneva, 1211 Geneva 4, Switzerland Bernhard.Wehrle-Haller@unige.ch vesa.hytonen@tuni.fi Jinhua.wu@fccc.edu.ORCID 0000-0002-1159-1147
Vesa P HytönenFaculty of Medicine and Health Technology, Tampere University, FI-33520 Tampere, Finland; Bernhard.Wehrle-Haller@unige.ch vesa.hytonen@tuni.fi Jinhua.wu@fccc.edu.ORCID 0000-0002-9357-1480
Jinhua WuMolecular Therapeutics Program, Fox Chase Cancer Center, Philadelphia, PA 19111; Bernhard.Wehrle-Haller@unige.ch vesa.hytonen@tuni.fi Jinhua.wu@fccc.edu.ORCID 0000-0001-5913-0633
Fox Chase Cancer Center · USTampere University · FIUniversity of California, Davis · USUniversity of Geneva · CH

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
The rodent eye as a non-invasive window for understanding cancer nanotherapeuticsU01CA198880 · NCI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI LAM, KIT S · 2015 to 2019
$2.9M
Cell-specific nanocarrier with endocytic and endosomolytic activities for therapeutic genome editingUG3TR002866 · NCATS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI CHENG, R.HOLLAND, LAM, KIT S · 2019 to 2021
$2.3M
Spatiotemporal Gene Regulation and KSHV ReplicationR01CA225266 · NCI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI IZUMIYA, YOSHIHIRO · 2018 to 2022
$1.8M
Genetically Encoded Small Illuminants for 4D nucleome imagingU01EB021230 · NIBIB · UNIVERSITY OF CALIFORNIA AT DAVIS · PI CHENG, R.HOLLAND, IZUMIYA, YOSHIHIRO · 2015 to 2017
$990k
NCATS NIH HHS UG3 TR002866NCI NIH HHS R01 CA225266NCI NIH HHS U01 CA198880NIBIB NIH HHS U01 EB021230NIGMS NIH HHS R35 GM119560
6 · The paper itself

Abstract

Binding of the intracellular adapter proteins talin and its cofactor, kindlin, to the integrin receptors induces integrin activation and clustering. These processes are essential for cell adhesion, migration, and organ development. Although the talin head, the integrin-binding segment in talin, possesses a typical FERM-domain sequence, a truncated form has been crystallized in an unexpected, elongated form. This form, however, lacks a C-terminal fragment and possesses reduced β3-integrin binding. Here, we present a crystal structure of a full-length talin head in complex with the β3-integrin tail. The structure reveals a compact FERM-like conformation and a tightly associated N-P-L-Y motif of β3-integrin. A critical C-terminal poly-lysine motif mediates FERM interdomain contacts and assures the tight association with the β3-integrin cytoplasmic segment. Removal of the poly-lysine motif or disrupting the FERM-folded configuration of the talin head significantly impairs integrin activation and clustering. Therefore, structural characterization of the FERM-folded active talin head provides fundamental understanding of the regulatory mechanism of integrin function.

Indexed as

Amino Acid MotifsAnimalsBinding SitesHumansIntegrin beta3LeucineMiceMicroscopy, Electron, TransmissionModels, MolecularMutagenesisPolylysineProtein DomainsProtein FoldingTalinIntegrin beta3LeucinePolylysineTalinTln1 protein, mousecell adhesionFERM domainintegrinNPxY motiftalin

Identifiers

PMID33288722
PMCPMC7768682
OpenAlexW3112618987

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.