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Article: Podosome formation promotes plasma membrane invagination and integrin-β3 endocytosis on a viscous RGD-membrane
Title | Podosome formation promotes plasma membrane invagination and integrin-β3 endocytosis on a viscous RGD-membrane |
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Authors | |
Issue Date | 2020 |
Publisher | Nature 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? |
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. |
Persistent Identifier | http://hdl.handle.net/10722/281688 |
ISSN | 2023 Impact Factor: 5.2 2023 SCImago Journal Rankings: 2.090 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Cao, F | - |
dc.contributor.author | Zhou, Y | - |
dc.contributor.author | Liu, X | - |
dc.contributor.author | Yu, C-H | - |
dc.date.accessioned | 2020-03-22T04:18:19Z | - |
dc.date.available | 2020-03-22T04:18:19Z | - |
dc.date.issued | 2020 | - |
dc.identifier.citation | Communications Biology, 2020, v. 3, p. article no. 117 | - |
dc.identifier.issn | 2399-3642 | - |
dc.identifier.uri | http://hdl.handle.net/10722/281688 | - |
dc.description.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. | - |
dc.language | eng | - |
dc.publisher | Nature Research (part of Springer Nature): Fully open access journals. The Journal's web site is located at http://www.nature.com/commsbio | - |
dc.relation.ispartof | Communications Biology | - |
dc.rights | This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License. | - |
dc.title | Podosome formation promotes plasma membrane invagination and integrin-β3 endocytosis on a viscous RGD-membrane | - |
dc.type | Article | - |
dc.identifier.email | Yu, C-H: chyu1@hku.hk | - |
dc.identifier.authority | Yu, C-H=rp01930 | - |
dc.description.nature | published_or_final_version | - |
dc.identifier.doi | 10.1038/s42003-020-0843-2 | - |
dc.identifier.scopus | eid_2-s2.0-85081884333 | - |
dc.identifier.hkuros | 309472 | - |
dc.identifier.volume | 3 | - |
dc.identifier.spage | article no. 117 | - |
dc.identifier.epage | article no. 117 | - |
dc.identifier.isi | WOS:000521060500009 | - |
dc.publisher.place | United Kingdom | - |
dc.identifier.issnl | 2399-3642 | - |