View : 58 Download: 0

Specific tyrosine phosphorylation of focal adhesion kinase mediated by Fer tyrosine kinase in suspended hepatocytes

Title
Specific tyrosine phosphorylation of focal adhesion kinase mediated by Fer tyrosine kinase in suspended hepatocytes
Authors
Oh M.-A.Choi S.Lee M.J.Choi M.-C.Lee S.-A.Ko W.Cance W.G.Oh E.-S.Buday L.Kim S.-H.Lee J.W.
Ewha Authors
오억수
SCOPUS Author ID
오억수scopus
Issue Date
2009
Journal Title
Biochimica et Biophysica Acta - Molecular Cell Research
ISSN
0167-4889JCR Link
Citation
vol. 1793, no. 5, pp. 781 - 791
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
Cell adhesion to the extracellular matrix (ECM) can activate signaling via focal adhesion kinase (FAK) leading to dynamic regulation of cellular morphology. Mechanistic basis for the lack of effective intracellular signaling by non-attached epithelial cells is poorly understood. To examine whether signaling in suspended cells is regulated by Fer cytoplasmic tyrosine kinase, we investigated the effect of ectopic Fer expression on signaling in suspended or adherent hepatocytes. We found that ectopic Fer expression in Huh7 hepatocytes in suspension or on non-permissive poly-lysine caused significant phosphorylation of FAK Tyr577, Tyr861, or Tyr925, but not Tyr397 or Tyr576. Fer-mediated FAK phosphorylation in suspended cells was independent of c-Src activity or growth factor stimulation, but dependent of cortactin expression. Consistent with these results, complex formation between FAK, Fer, and cortactin was observed in suspended cells. The Fer-mediated effect correlated with multiple membrane protrusions, even on poly-lysine. Together, these observations suggest that Fer may allow a bypass of anchorage-dependency for intracellular signal transduction in hepatocytes. © 2009 Elsevier B.V. All rights reserved.
DOI
10.1016/j.bbamcr.2009.01.015
Appears in Collections:
자연과학대학 > 생명과학전공 > Journal papers
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML


qrcode

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

BROWSE