Evidence map›Paper›PMID 19759398›Full record

ArticleThe Journal of biological chemistry2009

Dynamic interaction of amphiphysin with N-WASP regulates actin assembly.

Hiroshi Yamada, Sergi Padilla-Parra, Sun-Joo Park, Toshiki Itoh, Mathilde Chaineau, Ilaria Monaldi, Ottavio Cremona, Fabio Benfenati, Pietro De Camilli, Maïté Coppey-Moisan and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.7field-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

40 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Bend it like BIN1: how a membrane-curving adaptor protein shapes cardiac physiology.American journal of physiology. Heart and circulatory physiology · 2025
    Review
  3. Article
  4. Article
  5. RACK1 promotesiScience · 2023
    Article
  6. Mechanisms and Regulation of Cardiac CaInternational journal of molecular sciences · 2021
    Review
  7. Review
  8. SIV-Mediated Synaptic Dysfunction Is Associated with an Increase in Synapsin Site 1 Phosphorylation and Impaired PP2A Activity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2019
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Amphiphysin 2 (BIN1) in physiology and diseases.Journal of molecular medicine (Berlin, Germany) · 2014
    Review
  20. 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

13 authors at 8 institutions in 5 countries.

Hiroshi YamadaDepartment of Neuroscience, Okayama University Graduate School of Medicine, Dentistry, and Pharmaceutical Sciences, 2-5-1 Shikata-cho, Kita-ku, Okayama 700-8558, Japan.
Sergi Padilla-Parra
Sun-Joo Park
Toshiki Itoh
Mathilde Chaineau
Ilaria Monaldi
Ottavio Cremona
Fabio Benfenati
Pietro De Camilli
Maïté Coppey-Moisan
Marc Tramier
Thierry Galli
Kohji Takei
Université Paris Cité · FRItalian Institute of Technology · ITKobe University · JPOkayama University · JPCentre National de la Recherche Scientifique · FRHoward Hughes Medical Institute · USSorbonne Université · FRVita-Salute San Raffaele University · IT

Funding

Telethon GGP09134
6 · The paper itself

Abstract

Amphiphysin 1, an endocytic adaptor concentrated at synapses that couples clathrin-mediated endocytosis to dynamin-dependent fission, was also shown to have a regulatory role in actin dynamics. Here, we report that amphiphysin 1 interacts with N-WASP and stimulates N-WASP- and Arp2/3-dependent actin polymerization. Both the Src homology 3 and the N-BAR domains are required for this stimulation. Acidic liposome-triggered, N-WASP-dependent actin polymerization is strongly impaired in brain cytosol of amphiphysin 1 knock-out mice. FRET-FLIM analysis of Sertoli cells, where endogenously expressed amphiphysin 1 co-localizes with N-WASP in peripheral ruffles, confirmed the association between the two proteins in vivo. This association undergoes regulation and is enhanced by stimulating phosphatidylserine receptors on the cell surface with phosphatidylserine-containing liposomes that trigger ruffle formation. These results indicate that actin regulation is a key function of amphiphysin 1 and that such function cooperates with the endocytic adaptor role and membrane shaping/curvature sensing properties of the protein during the endocytic reaction.

Indexed as

Gene Expression RegulationActinsAnimalsBrainCell MembraneCytosolEndocytosisFluorescence Resonance Energy TransferLiposomesMaleMiceMice, KnockoutNerve Tissue ProteinsRatsReceptors, Cell SurfaceSertoli CellsActinsamphiphysinLiposomesNerve Tissue Proteinsphosphatidylserine receptorReceptors, Cell SurfaceWiskott-Aldrich Syndrome Protein, Neuronal

Identifiers

PMID19759398
PMCPMC2797194
OpenAlexW2085061590

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.