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

TitlePodosome formation promotes plasma membrane invagination and integrin-β3 endocytosis on a viscous RGD-membrane
Authors
Issue Date2020
PublisherNature Research (part of Springer Nature): Fully open access journals. The Journal's web site is located at http://www.nature.com/commsbio
Citation
Communications Biology, 2020, v. 3, p. article no. 117 How to Cite?
AbstractIntegrin 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.
Persistent Identifierhttp://hdl.handle.net/10722/281688
ISSN
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorCao, F-
dc.contributor.authorZhou, Y-
dc.contributor.authorLiu, X-
dc.contributor.authorYu, C-H-
dc.date.accessioned2020-03-22T04:18:19Z-
dc.date.available2020-03-22T04:18:19Z-
dc.date.issued2020-
dc.identifier.citationCommunications Biology, 2020, v. 3, p. article no. 117-
dc.identifier.issn2399-3642-
dc.identifier.urihttp://hdl.handle.net/10722/281688-
dc.description.abstractIntegrin 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.-
dc.languageeng-
dc.publisherNature Research (part of Springer Nature): Fully open access journals. The Journal's web site is located at http://www.nature.com/commsbio-
dc.relation.ispartofCommunications Biology-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.titlePodosome formation promotes plasma membrane invagination and integrin-β3 endocytosis on a viscous RGD-membrane-
dc.typeArticle-
dc.identifier.emailYu, C-H: chyu1@hku.hk-
dc.identifier.authorityYu, C-H=rp01930-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1038/s42003-020-0843-2-
dc.identifier.scopuseid_2-s2.0-85081884333-
dc.identifier.hkuros309472-
dc.identifier.volume3-
dc.identifier.spagearticle no. 117-
dc.identifier.epagearticle no. 117-
dc.identifier.isiWOS:000521060500009-
dc.publisher.placeUnited Kingdom-
dc.identifier.issnl2399-3642-

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