Please use this identifier to cite or link to this item: https://doi.org/10.1242/bio.016428
Title: Association between tensin 1 and p130Cas at focal adhesions links actin inward flux to cell migration
Authors: Zhao Z.
Tan S.H. 
Machiyama H.
Kawauchi K.
Araki K.
Hirata H.
Sawada Y. 
Keywords: actin
cellular apoptosis susceptibility protein
Crk associated substrate protein
paxillin
protein SH2
SH2PTB protein
tensin
tensin 1
unclassified drug
actin filament
Article
cell migration
cell motility
cell transport
controlled study
cytoskeleton
focal adhesion
HEK293 cell line
human
human cell
immunofluorescence
in vitro study
nonhuman
photoactivation
protein binding
protein expression
protein localization
protein motif
protein phosphorylation
protein protein interaction
Issue Date: 2016
Citation: Zhao Z., Tan S.H., Machiyama H., Kawauchi K., Araki K., Hirata H., Sawada Y. (2016). Association between tensin 1 and p130Cas at focal adhesions links actin inward flux to cell migration. Biology Open 5 (4) : 499-506. ScholarBank@NUS Repository. https://doi.org/10.1242/bio.016428
Abstract: Cell migration is a highly dynamic process that plays pivotal roles in both physiological and pathological processes. We have previously reported that p130Cas supports cell migration through the binding to Src as well as phosphorylation-dependent association with actin retrograde flow at focal adhesions. However, it remains elusive how phosphorylated Cas interacts with actin cytoskeletons. We observe that the actin-binding protein, tensin 1, co-localizes with Cas, but not with its phosphorylation-defective mutant, at focal adhesions in leading regions of migrating cells. While a truncation mutant of tensin 1 that lacks the phosphotyrosine-binding PTB and SH2 domains (tensin 1-SH2PTB) poorly co-localizes or co-immunoprecitates with Cas, bacterially expressed recombinant tensin 1-SH2PTB protein binds to Cas in vitro in a Cas phosphorylation-dependent manner. Furthermore, exogenous expression of tensin 1-SH2PTB, which is devoid of the actin-interacting motifs, interferes with the Cas-driven cell migration, slows down the inward flux of Cas molecules, and impedes the displacement of Cas molecules from focal adhesions. Taken together, our results show that tensin 1 links inwardly moving actin cytoskeletons to phosphorylated Cas at focal adhesions, thereby driving cell migration. © 2016. Published by The Company of Biologists Ltd |.
Source Title: Biology Open
URI: https://scholarbank.nus.edu.sg/handle/10635/174017
ISSN: 20466390
DOI: 10.1242/bio.016428
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