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Vol. 14, Issue 2, 529-544, February 2003
1 (TGF-)-induced Apoptosis of
Prostate Cancer Cells Involves Smad7-dependent Activation of p38 by
TGF--activated Kinase 1 and Mitogen-activated Protein Kinase
Kinase 3
*Ludwig Institute for Cancer Research, Biomedical Centre,
75124 Uppsala, Sweden; The inhibitory Smad7, a direct target gene for transforming growth
factor-Department of Genetics
and Pathology, Rudbeck Laboratory, Uppsala University, 75185 Uppsala,
Sweden; and §Division of Cellular Biochemistry,
Netherlands Cancer Institute, 1066CX Amsterdam, The Netherlands
(TGF-), mediates TGF-1-induced apoptosis in several
cell types. Herein, we report that apoptosis of human prostate
cancer PC-3U cells induced by TGF-1 or Smad7 overexpression is
caused by a specific activation of the p38 mitogen-activated protein kinase pathway in a TGF--activated kinase 1 (TAK1)-
and mitogen-activated protein kinase kinase 3 (MKK3)-dependent manner. Expression of dominant negative p38, dominant negative MKK3, or incubation with the p38 selective inhibitor
[4-(4-fluorophenyl)-2-(4-methylsulfinylphenyl)-5-(4-pyridyl)1H-imidazole], prevented TGF-1-induced apoptosis. The expression of Smad7 was required for TGF--induced activation of MKK3 and p38 kinases, and
endogenous Smad7 was found to interact with phosphorylated p38 in a
ligand-dependent manner. Ectopic expression of wild-type TAK1 promoted
TGF-1-induced phosphorylation of p38 and apoptosis, whereas
dominant negative TAK1 reduced TGF-1-induced phosphorylation of p38
and apoptosis. Endogenous Smad7 was found to interact with TAK1, and
TAK1, MKK3, and p38 were coimmunoprecipitated with Smad7 in transiently
transfected COS1 cells. Moreover, ectopically expressed Smad7 enhanced
the coimmunoprecipitation of HA-MKK3 and Flag-p38, supporting the
notion that Smad7 may act as a scaffolding protein and facilitate TAK1-
and MKK3-mediated activation of p38.
Corresponding author. E-mail address:
marene.landstrom{at}licr.uu.se.
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