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  • MAPKK-independent activation of p38alpha mediated by TAB1-dependent autophosphorylation of p38alpha.

MAPKK-independent activation of p38alpha mediated by TAB1-dependent autophosphorylation of p38alpha.

Science (New York, N.Y.) (2002-02-16)
Baoxue Ge, Hermann Gram, Franco Di Padova, Betty Huang, Liguo New, Richard J Ulevitch, Ying Luo, Jiahuai Han
ZUSAMMENFASSUNG

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 p38alpha MAPK that does not involve the prototypic kinase cascade. Rather it depends on interaction of p38alpha with TAB1 [transforming growth factor-beta-activated protein kinase 1 (TAK1)-binding protein 1] leading to autophosphorylation and activation of p38alpha. We detected formation of a TRAF6-TAB1-p38alpha complex and showed stimulus-specific TAB1-dependent and TAB1-independent p38alpha activation. These findings suggest that alternative activation pathways contribute to the biological responses of p38alpha to various stimuli.

MATERIALIEN
Produktnummer
Marke
Produktbeschreibung

Sigma-Aldrich
p38α, active, GST tagged human, PRECISIO® Kinase, recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution