Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.celrep.2013.10.040
Title: Integrin-matrix clusters form podosome-like adhesions in the absence of traction forces
Authors: Yu, C.-H.
Rafiq, N.
Krishnasamy, A.
Hartman, K.
Jones, G.
Bershadsky, A.
Sheetz, M. 
Issue Date: 12-Dec-2013
Source: Yu, C.-H., Rafiq, N., Krishnasamy, A., Hartman, K., Jones, G., Bershadsky, A., Sheetz, M. (2013-12-12). Integrin-matrix clusters form podosome-like adhesions in the absence of traction forces. Cell Reports 5 (5) : 1456-1468. ScholarBank@NUS Repository. https://doi.org/10.1016/j.celrep.2013.10.040
Abstract: Matrix-activated integrins can form different adhesion structures. We report that nontransformed fibroblasts develop podosome-like adhesions when spread on fluid Arg-Gly-Asp peptide (RGD)-lipid surfaces, whereas they habitually form focal adhesions on rigid RGD glass surfaces. Similar to classic macrophage podosomes, the podosome-like adhesions are protrusive and characterized by doughnut-shaped RGD rings that surround characteristic core components including F-actin, N-WASP, and Arp2/Arp3. Furthermore, there are 18 podosome markers in these adhesions, though they lack matrix metalloproteinases that characterize invadopodia and podosomes of Src-transformed cells. When nontransformed cells develop force on integrin-RGD clusters by pulling RGD lipids to prefabricated rigid barriers (metal lines spaced by 1-2μm), these podosomes fail to form and instead form focal adhesions. The formation of podosomes on fluid surfaces is mediated by local activation of phosphoinositide 3-kinase (PI3K) and the production of phosphatidylinositol-(3,4,5)-triphosphate (PIP3) in a FAK/PYK2-dependent manner. Enrichment of PIP3 precedes N-WASP activation and the recruitment of RhoA-GAP ARAP3. We propose that adhesion structures can be modulated by traction force development and that production of PIP3 stimulates podosome formation and subsequent RhoA downregulation in the absence of traction force.
Source Title: Cell Reports
URI: http://scholarbank.nus.edu.sg/handle/10635/100946
ISSN: 22111247
DOI: 10.1016/j.celrep.2013.10.040
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

49
checked on Apr 2, 2018

WEB OF SCIENCETM
Citations

48
checked on Apr 2, 2018

Page view(s)

28
checked on Mar 11, 2018

Google ScholarTM

Check

Altmetric


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