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HER2/Neu (ErbB2) signaling to Rac1-Pak1 is temporally and spatially modulated by transforming growth factor beta

Authors
Wang, Shizhen EmilyShin, IncheolWu, Frederick Y.Friedman, David B.Arteaga, Carlos L.
Issue Date
Oct-2006
Publisher
AMER ASSOC CANCER RESEARCH
Citation
CANCER RESEARCH, v.66, no.19, pp.9591 - 9600
Indexed
SCIE
SCOPUS
Journal Title
CANCER RESEARCH
Volume
66
Number
19
Start Page
9591
End Page
9600
URI
https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/180899
DOI
10.1158/0008-5472.CAN-06-2071
ISSN
0008-5472
Abstract
In HER2 (ErbB2)-overexpressing cells, transforming growth factor beta (TGF-beta), via activation of phosphoinositide-3 kinase (PI3K), recruits actin and actinin to HER2, which then colocalizes with Vav2, activated Rac1, and Pak1 at cell protrusions. This results in prolonged Rac1. activation, enhanced motility and invasiveness, Bad phosphorylation, uncoupling of Bad/Bcl-2, and enhanced cell survival. The recruitment of the HER2/Vav2/Rac1/Pak1/actin/actinin complex to lamellipodia was abrogated by actinin siRNAs, dominant-negative (dn) p85, gefitinib, and dn-Rac1 or dnPak1, suggesting that the reciprocal interplay of PI3K, HER2 kinase, and Rac GTPases with the actin cytoskeleton is necessary for TGF-beta action in oncogene-overexpressing cells. Thus, by recruiting the actin skeleton, TGF-beta "cross-links" this signaling complex at cell lamellipodia; this prolongs Rac1 activation and increases metastatic properties and survival of HER2-overexpressing cells.
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