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MAPKK-Independent Activation of p38 Mediated by TAB1-Dependent Autophosphorylation of p38
Baoxue Ge,1Hermann Gram,2Franco Di Padova,2Betty Huang,3Liguo New,1Richard J. Ulevitch,1Ying Luo,34Jiahuai Han1*
Phosphorylation of mitogen-activated protein kinases
(MAPKs) on specific tyrosine and threonine sites by MAP kinase kinases(MAPKKs) is thought to be the sole activation mechanism. Here,we
report an unexpected activation mechanism for p38 MAPK thatdoes not
involve the prototypic kinase cascade. Rather it dependson interaction
of p38 with TAB1 [transforming growth factor--activatedprotein kinase 1 (TAK1)-binding protein 1] leading to
autophosphorylationand activation of p38. We detected formation of
a TRAF6-TAB1-p38complex and showed stimulus-specific TAB1-dependent
and TAB1-independentp38 activation. These findings suggest that
alternative activationpathways contribute to the biological responses
of p38 to variousstimuli.
1 Department of Immunology, The Scripps
Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
2 Novartis Pharma AG, CH-4002, Basel,
Switzerland.
3 Rigel, Inc., South San Francisco, CA
94080, USA.
4 Shanghai Genomics, Inc., Shanghai,
China.
*
To whom correspondence should be addressed. E-mail:
jhan{at}scripps.edu
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277, 47444-47450
|Abstract »|Full Text »|PDF »
Fyn and p38 Signaling Are Both Required for Maximal Hypertonic Activation of the Osmotic Response Element-binding Protein/Tonicity-responsive Enhancer-binding Protein (OREBP/TonEBP).
B. C. B. Ko, A. K. M. Lam, A. Kapus, L. Fan, S. K. Chung, and S. S. M. Chung (2002)
J. Biol. Chem.
277, 46085-46092
|Abstract »|Full Text »|PDF »
Transforming Growth Factor-beta Stimulates Parathyroid Hormone-related Protein and Osteolytic Metastases via Smad and Mitogen-activated Protein Kinase Signaling Pathways.
S.-M. Kakonen, K. S. Selander, J. M. Chirgwin, J. J. Yin, S. Burns, W. A. Rankin, B. G. Grubbs, M. Dallas, Y. Cui, and T. A. Guise (2002)
J. Biol. Chem.
277, 24571-24578
|Abstract »|Full Text »|PDF »
Mediated by TAB1-Dependent Autophosphorylation of p38
MAPK that does not
involve the prototypic kinase cascade. Rather it depends on interaction
of p38
-activated protein kinase 1 (TAK1)-binding protein 1] leading to
autophosphorylation and activation of p38
