Integrin-beta3 clusters recruit clathrin-mediated endocytic machinery in the absence of traction force

Cheng-han Yu (), Nisha Bte Mohd Rafiq, Fakun Cao, Yuhuan Zhou, Anitha Krishnasamy, Kabir Hassan Biswas, Andrea Ravasio, Zhongwen Chen, Yu-Hsiu Wang, Keiko Kawauchi, Gareth E. Jones and Michael P. Sheetz ()
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Cheng-han Yu: School of Biomedical Sciences, Li Ka Shing Faculty of Medicine, The University of Hong Kong
Nisha Bte Mohd Rafiq: Mechanobiology Institute, National University of Singapore
Fakun Cao: School of Biomedical Sciences, Li Ka Shing Faculty of Medicine, The University of Hong Kong
Yuhuan Zhou: School of Biomedical Sciences, Li Ka Shing Faculty of Medicine, The University of Hong Kong
Anitha Krishnasamy: Mechanobiology Institute, National University of Singapore
Kabir Hassan Biswas: Mechanobiology Institute, National University of Singapore
Andrea Ravasio: Mechanobiology Institute, National University of Singapore
Zhongwen Chen: Mechanobiology Institute, National University of Singapore
Yu-Hsiu Wang: Mechanobiology Institute, National University of Singapore
Keiko Kawauchi: Mechanobiology Institute, National University of Singapore
Gareth E. Jones: King's College London
Michael P. Sheetz: Mechanobiology Institute, National University of Singapore

Nature Communications, 2015, vol. 6, issue 1, 1-12

Abstract: Abstract The 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.

Date: 2015
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DOI: 10.1038/ncomms9672

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