Evidence map›Paper›PMID 23959172›Full record

ArticleCellular and molecular life sciences : CMLS2013

Swiprosin-1 modulates actin dynamics by regulating the F-actin accessibility to cofilin.

Yun Hyun Huh, So Hee Kim, Kyoung-Hwun Chung, Sena Oh, Min-Sung Kwon, Hyun-Woo Choi, Sangmyung Rhee, Je-Hwang Ryu, Zee Yong Park, Chang-Duk Jun and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2013. 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
2.3field-weighted citation impact, top 14% 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, 41 citations in OpenAlex.

  1. Article
  2. Pharmaceuticals (Basel, Switzerland) · 2024
    Article
  3. Article
  4. Article
  5. Getting cells into shape by calcium-dependent actin cross-linking proteins.Frontiers in cell and developmental biology · 2023
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. EFhd2 Affects Tau Liquid-Liquid Phase Separation.Frontiers in neuroscience · 2019
    Article
  12. Article
  13. Article
  14. Observational
  15. Article
  16. Article
  17. Structural implications of CaScientific reports · 2016
    Article
  18. Review
  19. Article
  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

11 authors at 3 institutions in 1 country.

Yun Hyun Huh
So Hee Kim
Kyoung-Hwun Chung
Sena Oh
Min-Sung Kwon
Hyun-Woo Choi
Sangmyung Rhee
Je-Hwang Ryu
Zee Yong Park
Chang-Duk Jun
Woo Keun Song
Gwangju Institute of Science and Technology · KRChonnam National University · KRChung-Ang University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Membrane protrusions, like lamellipodia, and cell movement are dependent on actin dynamics, which are regulated by a variety of actin-binding proteins acting cooperatively to reorganize actin filaments. Here, we provide evidence that Swiprosin-1, a newly identified actin-binding protein, modulates lamellipodial dynamics by regulating the accessibility of F-actin to cofilin. Overexpression of Swiprosin-1 increased lamellipodia formation in B16F10 melanoma cells, whereas knockdown of Swiprosin-1 inhibited EGF-induced lamellipodia formation, and led to a loss of actin stress fibers at the leading edges of cells but not in the cell cortex. Swiprosin-1 strongly facilitated the formation of entangled or clustered F-actin, which remodeled the structural organization of actin filaments making them in accessible to cofilin. EGF-induced phosphorylation of Swiprosin-1 at Ser183, a phosphorylation site newly identified using mass spectrometry, effectively inhibited clustering of actin filaments and permitted cofilin access to F-actin, resulting in actin depolymerization. Cells over expressing a Swiprosin-1 phosphorylation-mimicking mutant or a phosphorylation-deficient mutant exhibited irregular membrane dynamics during the protrusion and retraction cycles of lamellipodia. Taken together, these findings suggest that dynamic exchange of Swiprosin-1 phosphorylation and dephosphorylation is a novel mechanism that regulates actin dynamics by modulating the pattern of cofilin activity at the leading edges of cells.

Indexed as

Actin Depolymerizing FactorsActinsAdaptor Proteins, Signal TransducingAnimalsCalcium-Binding ProteinsCell MembraneEpidermal Growth FactorHumansMiceMicrofilament ProteinsPhosphorylationSerineSignal TransductionTumor Cells, CulturedActin Depolymerizing FactorsActinsAdaptor Proteins, Signal TransducingCalcium-Binding ProteinsEFHD2 protein, humanEFHD2 protein, mouseEpidermal Growth FactorMicrofilament ProteinsSerine

Identifiers

PMID23959172
PMCPMC3830201
OpenAlexW2004043477

What OpenQuestion holds

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LicenceCC BY
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.