Evidence map›Paper›PMID 32170110›Full record

ArticleCommunications biology2020

Podosome formation promotes plasma membrane invagination and integrin-β3 endocytosis on a viscous RGD-membrane.

Fakun Cao, Yuhuan Zhou, Xiaoting Liu, Cheng-Han Yu

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2020. 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
3.1field-weighted citation impact, top 8% 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, 28 citations in OpenAlex.

  1. Article
  2. Review
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  6. BIN1 gene replacement reverses BIN1-related centronuclear myopathy.Molecular therapy : the journal of the American Society of Gene Therapy · 2025
    Article
  7. Kindlin Regulates Mechanosensitive Activation and Adhesion Assembly of Integrin beta6.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  8. Article
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  10. Article
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  13. Review
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  16. PI(3,4)PProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  17. Article
  18. Article
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

4 authors at 2 institutions in 1 country.

Fakun CaoSchool of Biomedical Sciences, Li Ka Shing Faculty of Medicine, University of Hong Kong, Hong Kong, China.ORCID http://orcid.org/0000-0003-0542-4374
Yuhuan ZhouSchool of Biomedical Sciences, Li Ka Shing Faculty of Medicine, University of Hong Kong, Hong Kong, China.
Xiaoting LiuSchool of Biomedical Sciences, Li Ka Shing Faculty of Medicine, University of Hong Kong, Hong Kong, China.
Cheng-Han YuSchool of Biomedical Sciences, Li Ka Shing Faculty of Medicine, University of Hong Kong, Hong Kong, China. chyu1@hku.hk.ORCID http://orcid.org/0000-0002-8821-8877
University of Hong Kong · HKHKU-Pasteur Research Pole · HK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Integrin receptors orchestrate cell adhesion and cytoskeletal reorganization. The endocytic mechanism of integrin-β3 receptor at the podosome remains unclear. Using viscous RGD-membrane as the model system, here we show that the formation of podosome-like adhesion promotes Dab2/clathrin-mediated endocytosis of integrin-β3. Integrin-β3 and RGD ligand are endocytosed from the podosome and sorted into the endosomal compartment. Inhibitions of podosome formation and knockdowns of Dab2 and clathrin reduce RGD endocytosis. F-actin assembly at the podosome core exhibits protrusive contact towards the substrate and results in plasma membrane invaginations at the podosome ring. BIN1 specifically associates with the region of invaginated membrane and recruits DNM2. During the podosome formation, BIN1 and DNM2 synchronously enrich at the podosome ring and trigger clathrin dissociation and RGD endocytosis. Knockdowns of BIN1 and DNM2 suppress RGD endocytosis. Thus, plasma membrane invagination caused by F-actin polymerization promotes BIN1-dependent DNM2 recruitment and facilitate integrin-β3 endocytosis at the podosome.

Indexed as

Membranes, ArtificialActinsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAnimalsCell AdhesionCell MembraneCells, CulturedClathrinDynamin IIEndocytosisFibroblastsGene Knockdown TechniquesHumansIntegrin beta3LigandsActinsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular Transportarginyl-glycyl-aspartic acidBin1 protein, ratClathrinDab2 protein, ratDynamin IIIntegrin beta3LigandsMembranes, ArtificialNerve Tissue ProteinsOligopeptidesTumor Suppressor Proteins

Identifiers

PMID32170110
PMCPMC7070051
OpenAlexW3012234471

What OpenQuestion holds

Textmetadata
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.