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J Biol Chem, Vol. 274, Issue 51, 36035-36038, December 17, 1999
, and
From the Department of Immunology, The Scripps Research Institute,
La Jolla, California 92037 and the Big mitogen-activated protein (MAP) kinase
(BMK1), also known as ERK5, is a member of the MAP kinase family whose
cellular activity is elevated in response to growth factors, oxidative stress, and hyperosmolar conditions. Previous studies have identified MEK5 as a cellular kinase directly regulating BMK1 activity; however, signaling molecules that directly regulate MEK5 activity have not yet
been defined. Through utilization of a yeast two-hybrid screen, we have
identified MEKK3 as a molecule that physically interacts with MEK5.
This interaction appears to take place in mammalian cells as evidenced
by the fact that cellular MEK5 and MEKK3 co-immunoprecipitate. In
addition, we show that a dominant active form of MEKK3 stimulates BMK1
activity through MEK5. Moreover, we demonstrate that MEKK3 activity is
required for growth factor mediated cellular activation of endogenous
BMK1. Taken together, these results identify MEKK3 as a kinase that
regulates the activity of MEK5 and BMK1 during growth factor-induced
cellular stimulation.
Department of
Microbiology and Immunology, Aichi Medical University, Nagakute, Aichi
480-1195, Japan
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