Recruitment of phosphoinositide 3-kinase defines a positive contribution of tyrosine kinase signaling to E-cadherin function

Pang, Jian-Hong, Kraemer, Astrid, Stehbens, Samantha J., Frame, Margaret C. and Yap, Alpha S. (2005) Recruitment of phosphoinositide 3-kinase defines a positive contribution of tyrosine kinase signaling to E-cadherin function. The Journal of Biological Chemistry., 280 4: 3043-3050. doi:10.1074/jbc.M412148200

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Author Pang, Jian-Hong
Kraemer, Astrid
Stehbens, Samantha J.
Frame, Margaret C.
Yap, Alpha S.
Title Recruitment of phosphoinositide 3-kinase defines a positive contribution of tyrosine kinase signaling to E-cadherin function
Journal name The Journal of Biological Chemistry.   Check publisher's open access policy
ISSN 0021-9258
1083-351X
Publication date 2005-01-28
Year available 2004
Sub-type Article (original research)
DOI 10.1074/jbc.M412148200
Open Access Status File (Publisher version)
Volume 280
Issue 4
Start page 3043
End page 3050
Total pages 8
Place of publication Bethesda, MD, United States
Publisher American Society for Biochemistry and Molecular Biology
Language eng
Subject 11 Medical and Health Sciences
1101 Medical Biochemistry and Metabolomics
Abstract Classical cadherin adhesion molecules can function as adhesion-activated cell-signaling receptors. One key target for cadherin signaling is the lipid kinase phosphoinositide (PI) 3-kinase, which is recruited to cell-cell contacts and activated by E-cadherin. In this study, we sought to identify upstream factors necessary for E-cadherin to activate PI 3-kinase signaling. We found that inhibition of tyrosine kinase signaling blocked recruitment of PI 3-kinase to E-cadherin contacts and abolished the ability of E-cadherin to activate PI 3-kinase signaling. Tyrosine kinase inhibitors further perturbed several parameters of cadherin function, including cell adhesion and the ability of cells to productively extend nascent cadherin-adhesive contacts. Notably, the functional effects of tyrosine kinase blockade were rescued by expression of a constitutively active form of PI 3-kinase that restores PI 3-kinase signaling. Finally, using dominant negative Src mutants and Src-null cells, we identified Src as one key upstream kinase in the E-cadherin/PI 3-kinase-signaling pathway. Taken together, our findings indicate that tyrosine kinase activity, notably Src signaling, can contribute positively to cadherin function by supporting E-cadherin signaling to PI 3-kinase.
Keyword Phosphoinositide (PI) 3-kinase
E-cadherin
Tyrosine kinase inhibitors
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ
Additional Notes Published online on 19 November 2004

 
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Created: Fri, 13 Feb 2009, 00:14:56 EST by Ms Lynette Adams on behalf of Institute for Molecular Bioscience