The focal adhesion targeting domain of p130Cas confers a mechanosensing function

Bradbury, Peta M., Turner, Kylie, Mitchell, Camilla, Griffin, Kaitlyn R., Middlemiss, Shiloh, Lau, Loretta, Dagg, Rebecca, Taran, Elena, Cooper-White, Justin, Fabry, Ben and O'Neill, Geraldine M. (2017) The focal adhesion targeting domain of p130Cas confers a mechanosensing function. Journal of Cell Science, 130 7: 1263-1273. doi:10.1242/jcs.192930

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Author Bradbury, Peta M.
Turner, Kylie
Mitchell, Camilla
Griffin, Kaitlyn R.
Middlemiss, Shiloh
Lau, Loretta
Dagg, Rebecca
Taran, Elena
Cooper-White, Justin
Fabry, Ben
O'Neill, Geraldine M.
Title The focal adhesion targeting domain of p130Cas confers a mechanosensing function
Journal name Journal of Cell Science   Check publisher's open access policy
ISSN 1477-9137
0021-9533
Publication date 2017-04-01
Sub-type Article (original research)
DOI 10.1242/jcs.192930
Open Access Status File (Publisher version)
Volume 130
Issue 7
Start page 1263
End page 1273
Total pages 11
Place of publication Cambridge, United Kingdom
Publisher Company of Biologists
Collection year 2018
Language eng
Abstract Members of the Cas family of focal adhesion proteins contain a highly conserved C-terminal focal adhesion targeting (FAT) domain. To determine the role of the FAT domain in these proteins, we compared wild-type exogenous NEDD9 with a hybrid construct in which the NEDD9 FAT domain had been exchanged for the p130Cas (also known as BCAR1) FAT domain. Fluorescence recovery after photobleaching (FRAP) revealed significantly slowed exchange of the fusion protein at focal adhesions and significantly slower twodimensional migration. No differences were detected in cell stiffness as measured using atomic force microscopy (AFM) and in cell adhesion forces measured with a magnetic tweezer device. Thus, the slowed migration was not due to changes in cell stiffness or adhesion strength. Analysis of cell migration on surfaces of increasing rigidity revealed a striking reduction of cell motility in cells expressing the p130Cas FAT domain. The p130Cas FAT domain induced rigiditydependent phosphorylation of tyrosine residues within NEDD9. This in turn reduced post-translational cleavage of NEDD9, which we show inhibits NEDD9-induced migration. Collectively, our data therefore suggest that the p130Cas FAT domain uniquely confers a mechanosensing function.
Keyword Cell migration
FAT
Focal adhesion
Mechanosensing
NEDD9
P130Cas
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: HERDC Pre-Audit
Australian Institute for Bioengineering and Nanotechnology Publications
 
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