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J Biol Chem, Vol. 274, Issue 19, 13133-13138, May 7, 1999
-induced c-Jun N-terminal Kinase Signaling
Cascade
,,
From the The c-Jun N-terminal kinase (JNK) signaling
pathway is involved in transforming growth factor Department of Microbiology and Immunology,
Baylor College of Medicine, Houston, Texas 77030 and
§ Amgen, Inc., Boulder, Colorado 80301
(TGF-)
signaling in a variety of cell systems. We report here that
hematopoietic progenitor kinase 1 (HPK1), a novel Ste20-like protein
serine/threonine kinase, serves as an upstream mediator for the
TGF--activated JNK1 cascade in 293T cells. TGF- treatment
resulted in a time-dependent activation of HPK1, which was
accompanied by similar kinetics of JNK1 activation. The activation of
JNK1 by TGF- was abrogated by a kinase-defective HPK1 mutant but not
by a kinase-defective mutant of kinase homologous to Ste20/Sps1. This
result indicates that HPK1 is specifically required for TGF--induced
activation of JNK1. We also found that TGF--induced JNK1 activation
was blocked by a kinase-defective mutant of TGF--activated kinase 1 (TAK1). In addition, interaction between HPK1 and TAK1 was observed in
transient transfection assays, and this interaction was enhanced by
TGF- treatment. Both stress-activated protein kinase/extracellular
signal-regulated kinase kinase (SEK) and mitogen-activated protein
kinase kinase 7 (MKK7) are immediate upstream activators of JNK1.
Although SEK and MKK7 acted downstream of TAK1, only a kinase-defective
SEK mutant blocked TGF--induced activation of JNK1, indicating that
the TGF- signal is relayed solely through SEK, but not MKK7,
in vivo. Furthermore, TGF--induced activating protein 1 activation was blocked by a HPK1 mutant, as well as by TAK1 and
SEK mutants. Taken together, these studies establish a potential
cascade of TGF--activated interacting kinases beginning with HPK1, a
Ste20 homolog, and ending in JNK1 activation: HPK1 
TAK1 SEK JNK1.
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