Mitogen activated protein kinases (MAPKs) are critical components of several signal transduction pathways that convert extracellular stimuli into cellular responses. Four groups of MAPKs (ERKs, JNKs, p38, and ERK5) have been identified in mammalian cells. MAPK pathways contain a 3-kinase cascade consisting of a MAPK, a MAP/ERK kinase (MEK), and a MEK kinase (MEKK). MEKK phosphorylation of MEKs leads to activation and subsequent MEK-mediated phosphorylation of both Thr and Tyr residues at the Thr-X-Tyr dual phosphorylation motif of MAPKs. TAO1 was isolated from a rat cDNA library using the sequence from yeast Ste20p kinase. Sequence analysis shows that TAO1 contains an N-terminal Ser/Thr protein kinase domain, an acidic domain, and two serine-rich domains. The catalytic domain of TAO1 is 40% identical to the p21-activated kinases, PAK1 and PAK2, and 33% identical to MEKK1. TAO1 expression is highest in brain, but it is also detected in heart and lung. TAO1 can activate MEK3, MEK4, and MEK6 from the stress-responsive MAPK pathway, but not MEK1 or 2 from the classical MAPK pathway. Thus, TAO1 may be an important MEKK in the p38-containing stress-responsive MAPK pathway.
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