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Volume 272, Number 3,
Issue of January 17, 1997
pp. 1904-1909
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Cytoskeleton Reorganization Induces the Urokinase-type
Plasminogen Activator Gene via the Ras/Extracellular
Signal-regulated Kinase (ERK) Signaling Pathway
(Received for publication, June 11, 1996, and in revised form, September 23, 1996)
José Pedro
Irigoyen
,
Daniel
Besser
and
Yoshikuni
Nagamine
From the Friedrich Miescher Institute, P.O. Box 2543, CH-4002
Basel, Switzerland
Urokinase-type plasminogen activator (uPA)
expression is induced upon cytoskeletal reorganization (CSR) by a
mechanism independent of protein kinase C and cAMP protein kinase in
nontransformed renal epithelial (LLC-PK1) cells. This
CSR-dependent uPA gene activation is mediated by an
AP-1-recognizing element located 2 kilobases upstream of the
transcription initiation site. The phosphorylation of c-Jun, a
component of AP-1, is induced by CSR, which seems to increase both the
activity and stability of c-Jun (Lee, J. S., von der Ahe, D., Kiefer,
B., and Nagamine, Y. (1993) Nucleic Acids Res. 21, 3365-3372). It has been shown that c-Jun is phosphorylated by members
of the mitogen-activated protein kinase family, i.e. ERKs
and JNKs. ERKs are activated through a growth factor-coupled
Ras/Raf-dependent signaling pathway, while JNKs are
activated through a stress-induced signaling pathway. Although CSR
induces both ERK-2 and JNK activity, JNK does not seem to be involved
in the uPA gene induction because UV irradiation, which activates JNK
as efficiently as CSR, does not activate the uPA promoter. Further
analysis showed the involvement of SOS, Ras, and Raf-1 in the pathway
induced by CSR. Our results suggest that cells sense changes in cell
morphology using the cytoskeleton as a sensor and respond by activating
the ERK-involving signaling pathway from within the cell.

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Copyright © 1997 by the American Society for Biochemistry and Molecular Biology.
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