Please use this identifier to cite or link to this item: https://doi.org/10.1038/ncomms9672
Title: Integrin-beta3 clusters recruit clathrin-mediated endocytic machinery in the absence of traction force
Authors: Yu, 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 
Keywords: adhesion
biochemistry
cells and cell components
glass
ligand
lipid
protein
beta3 integrin
clathrin
Dab2 protein, mouse
protein binding
vesicular transport adaptor protein
animal
biomechanics
cell motion
cells
chemistry
cytology
endocytosis
genetics
HeLa cell line
human
metabolism
mouse
traction therapy
Adaptor Proteins, Vesicular Transport
Animals
Biomechanical Phenomena
Cell Movement
Cells
Clathrin
Endocytosis
HeLa Cells
Humans
Integrin beta3
Mice
Protein Binding
Traction
Issue Date: 2015
Publisher: Nature Publishing Group
Citation: Yu, 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
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. © 2015 Macmillan Publishers Limited. All rights reserved.
Source Title: Nature Communications
URI: https://scholarbank.nus.edu.sg/handle/10635/175473
ISSN: 20411723
DOI: 10.1038/ncomms9672
Appears in Collections:Staff Publications
Elements

Show full item record
Files in This Item:
File Description SizeFormatAccess SettingsVersion 
10_1038_ncomms9672.pdf2.73 MBAdobe PDF

OPEN

NoneView/Download

SCOPUSTM   
Citations

51
checked on Jun 29, 2022

WEB OF SCIENCETM
Citations

45
checked on Oct 8, 2021

Page view(s)

156
checked on Jun 23, 2022

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.