Evidence map›Paper›PMID 20966971›Full record

ReviewNature reviews. Molecular cell biology2010

The FERM domain: organizing the structure and function of FAK.

Margaret C Frame, Hitesh Patel, Bryan Serrels, Daniel Lietha, Michael J Eck

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Molecular cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 215 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
215citing papers in PubMed, 1 pooled it
–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

215 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Review
  3. Actin cytoskeletal dynamics in hepatic myofibroblasts and fibrosis.Nature reviews. Gastroenterology & hepatology · 2026
    Review
  4. The Impact of Zinc on T Cell Motility and the Immunological Synapse.International journal of molecular sciences · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Focal Adhesion Kinase Variants May Contribute to Risk of Human Myelomeningocele.medRxiv : the preprint server for health sciences · 2025
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Gas-powered extracellular vesicles promote bone regeneration.Extracellular vesicles and circulating nucleic acids · 2025
    Article
  18. Article
  19. Article
  20. The integrin adhesome and control of anti-tumour immunity.Biochemical Society transactions · 2024
    Review

155 more citing papers are in PubMed but not listed here.

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

5 authors.

Margaret C FrameEdinburgh Cancer Research UK Centre, Institute of Genetics and Molecular Medicine, Western General Hospital, Crewe Road South, Edinburgh EH4 2XR, UK. M.Frame@ed.ac.uk
Hitesh Patel
Bryan Serrels
Daniel Lietha
Michael J Eck

Funding

STRUCTURE OF INTEGRINS AND YWTD BETA PROPELLER DOMAINSP01HL048675 · NHLBI · IMMUNE DISEASE INSTITUTE, INC. · PI SPRINGER, TIMOTHY A · 1992 to 2009
$20.9M
Cancer Research UKNHLBI NIH HHS P01 HL048675Worldwide Cancer Research 09-0316
6 · The paper itself

Abstract

Focal adhesion kinase (FAK) is a scaffold and tyrosine kinase protein that binds to itself and cellular partners through its four-point-one, ezrin, radixin, moesin (FERM) domain. Recent structural work reveals that regulatory protein partners convert auto-inhibited FAK into its active state by binding to its FERM domain. Further, the identity of FAK FERM domain-interacting proteins yields clues as to how FAK coordinates diverse cellular responses, including cell adhesion, polarization, migration, survival and death, and suggests that FERM domains might mediate information transfer between the cell cortex and nucleus. Importantly, the FAK FERM domain might act as a paradigm for the actions of other FERM domain-containing proteins.

Indexed as

Protein Structure, TertiarySignal TransductionAnimalsCell NucleusCell Physiological PhenomenaCytoplasmFocal Adhesion Protein-Tyrosine KinasesHumansModels, MolecularProtein BindingFocal Adhesion Protein-Tyrosine Kinases

Identifiers

PMID20966971

What OpenQuestion holds

Textmetadata
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.