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(Received for publication, December 19, 1996, and in revised form, January 22, 1997)
From the Ceramide has been proposed as a second messenger
molecule implicated in a variety of biological processes. It has
recently been reported that ceramide activates stress-activated protein kinase (SAPK, also known as c-Jun NH2-terminal kinase
JNK), a subfamily member of mitogen-activated protein kinase
superfamily molecules and that the ceramide/SAPK/JNK signaling pathway
is required for stress-induced apoptosis. However, the molecular mechanism by which ceramide induces SAPK/JNK activation is unknown. Here we show that TAK1, a member of the mitogen-activated protein kinase kinase kinase family, is activated by treatment of cells with
agents and stresses that induce an increase in ceramide. Ceramide
itself stimulated the kinase activity of TAK1. Expression of a
constitutively active form of TAK1 resulted in activation of SAPK/JNK
and SEK1/MKK4, a direct activator of SAPK/JNK. Furthermore, expression
of a kinase-negative form of TAK1 interfered with the activation of
SAPK/JNK induced by ceramide. These results indicate that TAK1 may
function as a mediator of ceramide signaling to SAPK/JNK
activation.
Volume 272, Number 13,
Issue of March 28, 1997
pp. 8141-8144
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
COMMUNICATION:
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Department of Genetics and Molecular
Biology, Institute for Virus Research, Kyoto University, Sakyo-ku,
Kyoto 606-01, Japan, the § Department of Molecular Biology,
Faculty of Science, Nagoya University, Chikusa-ku, Nagoya 464-01, Japan
and the ¶ Faculty of Pharmaceutical Sciences, Hokkaido
University, Sapporo 060, Japan
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