Please use this identifier to cite or link to this item: https://doi.org/10.1038/ncomms9672
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dc.titleIntegrin-beta3 clusters recruit clathrin-mediated endocytic machinery in the absence of traction force
dc.contributor.authorYu, C.-H
dc.contributor.authorRafiq, N.B.M
dc.contributor.authorCao, F
dc.contributor.authorZhou, Y
dc.contributor.authorKrishnasamy, A
dc.contributor.authorBiswas, K.H
dc.contributor.authorRavasio, A
dc.contributor.authorChen, Z
dc.contributor.authorWang, Y.-H
dc.contributor.authorKawauchi, K
dc.contributor.authorJones, G.E
dc.contributor.authorSheetz, M.P
dc.date.accessioned2020-09-10T01:49:18Z
dc.date.available2020-09-10T01:49:18Z
dc.date.issued2015
dc.identifier.citationYu, C.-H, Rafiq, N.B.M, Cao, F, Zhou, Y, Krishnasamy, A, Biswas, K.H, Ravasio, A, Chen, Z, Wang, Y.-H, Kawauchi, K, Jones, G.E, Sheetz, M.P (2015). Integrin-beta3 clusters recruit clathrin-mediated endocytic machinery in the absence of traction force. Nature Communications 6 : 8672. ScholarBank@NUS Repository. https://doi.org/10.1038/ncomms9672
dc.identifier.issn20411723
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/175473
dc.description.abstractThe turnover of integrin receptors is critical for cell migration and adhesion dynamics. Here we find that force development at integrins regulates adaptor protein recruitment and endocytosis. Using mobile RGD (Arg-Gly-Asp) ligands on supported lipid membranes (RGD membranes) and rigid RGD ligands on glass (RGD-glass), we find that matrix force-dependent integrin signals block endocytosis. Dab2, an adaptor protein of clathrin-mediated endocytosis, is not recruited to activated integrin-beta3 clusters on RGD-glass; however, it is recruited to integrin-mediated adhesions on RGD membranes. Further, when force generation is inhibited on RGD-glass, Dab2 binds to integrin-beta3 clusters. Dab2 binding to integrin-beta3 excludes other adhesion-related adaptor proteins, such as talin. The clathrin-mediated endocytic machinery combines with Dab2 to facilitate the endocytosis of RGD-integrin-beta3 clusters. From these observations, we propose that loss of traction force on ligand-bound integrin-beta3 causes recruitment of Dab2/clathrin, resulting in endocytosis of integrins. © 2015 Macmillan Publishers Limited. All rights reserved.
dc.publisherNature Publishing Group
dc.sourceUnpaywall 20200831
dc.subjectadhesion
dc.subjectbiochemistry
dc.subjectcells and cell components
dc.subjectglass
dc.subjectligand
dc.subjectlipid
dc.subjectprotein
dc.subjectbeta3 integrin
dc.subjectclathrin
dc.subjectDab2 protein, mouse
dc.subjectprotein binding
dc.subjectvesicular transport adaptor protein
dc.subjectanimal
dc.subjectbiomechanics
dc.subjectcell motion
dc.subjectcells
dc.subjectchemistry
dc.subjectcytology
dc.subjectendocytosis
dc.subjectgenetics
dc.subjectHeLa cell line
dc.subjecthuman
dc.subjectmetabolism
dc.subjectmouse
dc.subjecttraction therapy
dc.subjectAdaptor Proteins, Vesicular Transport
dc.subjectAnimals
dc.subjectBiomechanical Phenomena
dc.subjectCell Movement
dc.subjectCells
dc.subjectClathrin
dc.subjectEndocytosis
dc.subjectHeLa Cells
dc.subjectHumans
dc.subjectIntegrin beta3
dc.subjectMice
dc.subjectProtein Binding
dc.subjectTraction
dc.typeArticle
dc.contributor.departmentMECHANOBIOLOGY INSTITUTE
dc.contributor.departmentBIOLOGY (NU)
dc.description.doi10.1038/ncomms9672
dc.description.sourcetitleNature Communications
dc.description.volume6
dc.description.page8672
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