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Vol. 12, No. 21, pp. 3369-3381, November 1, 1998
1 Laboratory of Gene Regulation and Signal Transduction,
Department of Pharmacology, University of California San Diego, La
Jolla, California 92093-0636 USA;
2 Department of Immunology,
The University of Texas, M.D. Anderson Cancer Center, Houston, Texas
77030 USA;
3 Signal Pharmaceuticals,
San Diego, California 92121 USA
MAP kinase (MAPK) cascades are composed of a MAPK, MAPK kinase
(MAPKK), and a MAPKK kinase (MAPKKK). Despite the existence of numerous
components and ample opportunities for crosstalk, most MAPKs are
specifically and distinctly activated. We investigated the basis for
specific activation of the JNK subgroup of MAPKs. The specificity of
JNK activation is determined by the MAPKK JNKK1, which interacts with
the MAPKKK MEKK1 and JNK through its amino-terminal extension. Inactive
JNKK1 mutants can disrupt JNK activation by MEKK1 or tumor necrosis
factor (TNF) in intact cells only if they contain an intact
amino-terminal extension. Mutations in this region interfere with the
ability of JNKK1 to respond to TNF but do not affect its activation by
physical stressors. As JNK and MEKK1 compete for binding to JNKK1 and
activation of JNKK1 prevents its binding to MEKK1, activation of this
module is likely to occur through sequential MEKK1:JNKK1 and JNKK1:JNK
interactions. These results underscore a role for the amino-terminal
extension of MAPKKs in determination of response specificity.
[Key Words: JNKK1; MEKK1; MAP kinase; interaction; specificity]
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