Evidence map›Paper›PMID 24914801›Full record

ReviewSmall GTPases2014

Formins as effector proteins of Rho GTPases.

Sonja Kühn, Matthias Geyer

Open access · bronzeAbstract readReview
In one paragraph

Review in Small GTPases, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 160 papers.

0numbers the graph read from it
0cells of the map it votes in
160citing papers in PubMed
10.0field-weighted citation impact, top 1% 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

160 citing papers in PubMed, 281 citations in OpenAlex.

  1. Article
  2. Alterations of actin in aging.Journal of cell science · 2026
    Review
  3. Article
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  7. Review
  8. Article
  9. Current Evidence on the Involvement of RAGE-Diaph1 Signaling in the Pathology and Treatment of Neurodegenerative Diseases-An Overview.Pathophysiology : the official journal of the International Society for Pathophysiology · 2025
    Review
  10. Article
  11. Review
  12. Article
  13. Article
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  15. The role of actin cytoskeleton component Arp2/3 in inflammatory response.Frontiers in cell and developmental biology · 2025
    Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

100 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

2 authors at 2 institutions in 3 countries.

Sonja KühnCenter of Advanced European Studies and Research (caesar); Group Physical Biochemistry; Bonn, Germany.
Matthias GeyerCenter of Advanced European Studies and Research (caesar); Group Physical Biochemistry; Bonn, Germany.
Center of Advanced European Studies and Research · DELaboratoire d'Enzymologie et Biochimie Structurales · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Formin proteins were recognized as effectors of Rho GTPases some 15 years ago. They contribute to different cellular actin cytoskeleton structures by their ability to polymerize straight actin filaments at the barbed end. While not all formins necessarily interact with Rho GTPases, a subgroup of mammalian formins, termed Diaphanous-related formins or DRFs, were shown to be activated by small GTPases of the Rho superfamily. DRFs are autoinhibited in the resting state by an N- to C-terminal interaction that renders the central actin polymerization domain inactive. Upon the interaction with a GTP-bound Rho, Rac, or Cdc42 GTPase, the C-terminal autoregulation domain is displaced from its N-terminal recognition site and the formin becomes active to polymerize actin filaments. In this review we discuss the current knowledge on the structure, activation, and function of formin-GTPase interactions for the mammalian formin families Dia, Daam, FMNL, and FHOD. We describe both direct and indirect interactions of formins with GTPases, which lead to formin activation and cytoskeletal rearrangements. The multifaceted function of formins as effector proteins of Rho GTPases thus reflects the diversity of the actin cytoskeleton in cells.

Indexed as

Actin CytoskeletonAnimalsBinding SitesCarrier ProteinsFetal ProteinsForminsHumansIntracellular Signaling Peptides and ProteinsMicrofilament ProteinsNuclear ProteinsProtein Structure, Tertiaryrho GTP-Binding ProteinsCarrier ProteinsDaam1 protein, mouseDiap1 protein, mouseFetal ProteinsFHOD1 protein, mouseFmnl1 protein, mouseForminsIntracellular Signaling Peptides and ProteinsMicrofilament ProteinsNuclear Proteinsrho GTP-Binding ProteinsCdc42Daam1Daam2FHOD1FHOD3filopodiaFMNL1FMNL2FMNL3forminlamellipodiummDia1mDia2mDia3RacRhoROCKstress fiber

Identifiers

PMID24914801
PMCPMC4111664
OpenAlexW2002335132

What Socratic holds

Textmetadata
LicenceCC BY-NC
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 Socratic graph.