Evidence map›Paper›PMID 21339294›Full record

ArticleThe Journal of biological chemistry2011

Rif-mDia1 interaction is involved in filopodium formation independent of Cdc42 and Rac effectors.

Wah Ing Goh, Thankiah Sudhaharan, Kim Buay Lim, Kai Ping Sem, Chew Ling Lau, Sohail Ahmed

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
–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

27 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Fast-cycling Rho GTPases.Small GTPases · 2020
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Rhof promotes murine marginal zone B cell development.Nagoya journal of medical science · 2014
    Article
  14. Three-dimensional aspects of matrix assembly by cells in the developing cornea.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  15. Article
  16. Article
  17. NG2 regulates directional migration of oligodendrocyte precursor cells via Rho GTPases and polarity complex proteins.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
    Article
  18. Article
  19. Article
  20. Rho GTPases in platelet function.Journal of thrombosis and haemostasis : JTH · 2013
    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

6 authors.

Wah Ing GohInstitute of Medical Biology, 8A Biomedical Grove, Immunos, Singapore 138648.
Thankiah Sudhaharan
Kim Buay Lim
Kai Ping Sem
Chew Ling Lau
Sohail Ahmed

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Filopodia are cellular protrusions important for axon guidance, embryonic development, and wound healing. The Rho GTPase Cdc42 is the best studied inducer of filopodium formation, and several of its effectors and their interacting partners have been linked to the process. These include IRSp53, N-WASP, Mena, and Eps8. The Rho GTPase, Rif, also drives filopodium formation. The signaling pathway by which Rif induces filopodia is poorly understood, with mDia2 being the only protein implicated to date. It is thus not clear how distinct the Rif-driven pathway for filopodium formation is from the one mediated by Cdc42. In this study, we characterize the dynamics of Rif-induced filopodia by time lapse imaging of live neuronal cells and show that Rif drives filopodium formation via an independent pathway that does not involve the Cdc42 effectors N-WASP and IRSp53, the IRSp53 binding partner Mena, or the Rac effectors WAVE1 and WAVE2. Rif formed filopodia in the absence of N-WASP or Mena and when IRSp53, WAVE1, or WAVE2 was knocked down by RNAi. Rif-mediated filopodial protrusion was instead reduced by silencing mDia1 expression or overexpressing a dominant negative mutant of mDia1. mDia1 on its own was able to form filopodia. Data from acceptor photobleaching FRET studies of protein-protein interaction demonstrate that Rif interacts directly with mDia1 in filopodia but not with mDia2. Taken together, these results suggest a novel pathway for filopodia formation via Rif and mDia1.

Indexed as

AnimalsCarrier Proteinscdc42 GTP-Binding ProteinCell Line, TumorCytoskeletal ProteinsForminsGene Knockdown TechniquesMiceMicrofilament ProteinsMutationNerve Tissue ProteinsNeuronsProto-Oncogene Proteins c-aktPseudopodiaSignal TransductionWiskott-Aldrich Syndrome Protein FamilyBaiap2 protein, mouseCarrier Proteinscdc42 GTP-Binding ProteinCytoskeletal ProteinsDiap1 protein, mouseEnah protein, mouseForminsMicrofilament ProteinsNerve Tissue ProteinsProto-Oncogene Proteins c-aktWasf2 protein, mouseWasl protein, mouseWiskott-Aldrich Syndrome Protein FamilyWiskott-Aldrich Syndrome Protein, Neuronal

Identifiers

PMID21339294
PMCPMC3075712

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.