Evidence map›Paper›PMID 33458919›Full record

ArticleCell proliferation2021

Formin homology domains of Daam1 bind to Fascin and collaboratively promote pseudopodia formation and cell migration in breast cancer.

Leiyu Hao, Yan Liu, Xinqian Yu, Yuerong Zhu, Yichao Zhu

Open access · goldAbstract read
In one paragraph

Article in Cell proliferation, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

18 citing papers in PubMed, 23 citations in OpenAlex.

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  10. The prognostic value of DAAM2 in lower grade glioma, liver cancer, and breast cancer.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2023
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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 at 3 institutions in 1 country.

Leiyu HaoDepartment of Physiology, Nanjing Medical University, Nanjing, China.
Yan LiuDepartment of Physiology, Nanjing Medical University, Nanjing, China.
Xinqian YuDepartment of Physiology, Nanjing Medical University, Nanjing, China.
Yuerong ZhuQinhuai District, Nanjing Jinling Hospital, Nanjing, China.
Yichao ZhuDepartment of Physiology, Nanjing Medical University, Nanjing, China.ORCID https://orcid.org/0000-0003-3499-8510
Hebei Yiling Hospital · CNNanjing Medical University · CNNanjing General Hospital of Nanjing Military Command · CN

Funding

National Natural Science Foundation of China 82073194Natural Science Foundation of Jiangsu Province BK20181367State Key Laboratory of Reproductive Medicine SKLRM-K202003
6 · The paper itself

Abstract

objectivesCancer cell migration to secondary organs remains an essential cause of death among breast cancer (BrCa) patients. Cell motility mainly relies on actin dynamics. Our previous reports verified that dishevelled-associated activator of morphogenesis 1 (Daam1) regulates invadopodia extension and BrCa cell motility. However, how Daam1 is involved in actin filament assembly and promotes pseudopodia formation in BrCa cells remains unclear. MATERIALS AND

methodsOne hundred human BrCa samples were collected at Women's Hospital of Nanjing Medical University. Immunohistochemistry (IHC) was used to examine Daam1 and Fascin expression. Wound healing and Boyden chamber assays were used to explore cell migration and pseudopodia extension of BrCa cells. Co-IP/pull down and Western blotting were performed to study the physical interaction between Daam1 and Fascin. Immunofluorescence assays were performed to observe whether Daam1 and Fascin were colocalized and mediated actin filament assembly.

resultsFascin was upregulated in BrCa tissues compared with that in paracarcinoma tissues. The downregulation of Fascin caused a decline in pseudopodia formation and cell motility. Moreover, we found that Daam1 interacted with Fascin via formin homology (FH) domains, especially the FH2 domain. Immunofluorescence assays showed that Daam1 and Fascin partially colocalized to actin filaments, and the knockdown of Daam1 or Fascin failed to colocalize to short and curved actin filaments.

conclusionsDaam1 specifically binds to Fascin via FH domains and cooperatively facilitates pseudopodia formation and cell migration by promoting actin filament assembly in BrCa.

Indexed as

Actin CytoskeletonAdaptor Proteins, Signal TransducingBreast NeoplasmsCell MovementForminsHumansPseudopodiarho GTP-Binding ProteinsAdaptor Proteins, Signal TransducingForminsrho GTP-Binding Proteins

Identifiers

PMID33458919
PMCPMC7941230
OpenAlexW3121774625

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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.