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,
*
Division of Allergy, La Jolla Institute for Allergy and Immunology, San Diego, CA 92121;
Fred Hutchinson Cancer Research Center, Seattle, WA 98109; and
Department of Biochemistry, University of Washington, Seattle, WA 98195
Stimulation of the high affinity IgE receptor (Fc
RI) as well as
a variety of stresses induce activation of c-Jun N-terminal protein
kinases (JNKs) stress-activated protein kinases in mast cells. At least
three distinct signaling pathways leading to JNK activation have been
delineated based on the involvements of Bruton’s tyrosine kinase
(Btk), protein kinase C (PKC), and the JNK-activating cascades composed
of multiple protein kinases. The PKC-dependent pathway, which is
inhibited by a PKC inhibitor Ro31-8425 and can be activated by PMA,
functions as a major route in FcRI-stimulated mast cells derived
from btk gene knockout mice. On the other hand,
wild-type mouse-derived mast cells use both PKC-dependent and
PKC-independent pathways for JNK activation. A PKC-independent pathway
is regulated by Btk and SEK1 via the PAK
MEKK1SEK1JNK cascade,
and is sensitive to phosphatidylinositol 3-kinase inhibitors,
wortmannin and LY-294002, while the PKC-dependent pathway is affected
to a lesser extent by both wortmannin treatment and overexpression of
wild-type and dominant negative mutant SEK1 proteins. Another
PKC-independent pathway involves Btk and MKK7, a recently cloned direct
activator of JNK. Among the stresses tested, UV irradiation seems to
activate Btk and JNK via the PKC-independent
pathways.
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