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Papers In Press, published online ahead of print February 6, 2004
Pediatrics, National Jewish Medical and Research Center, Denver, CO 80206
Corresponding Author: Shyra.Gardai{at}UCHSC.edu
Although important for apoptosis, the mechanism of Bax regulation is poorly understood. This report demonstrates that phosphorylation of serine184 regulates Bax activity. The phosphorylation required PI3K/Akt activation and appeared to be mediated by Akt itself. In the serine phosphorylated form Bax was detected in the cytoplasm, could not be immunoprecipitated with the activation specific antibody 6A7, and promoted heterodimerization with Mcl-1, Bcl-xl and A1. Apoptotic neutrophils possessed reduced levels of serine phosphorylated Bax correlating with an increase in activated Bax as well as an increase in the amount of Bax found translocated to the mitochondria. We suggest that Bax is regulated by phosphorylation of serine184 in an Akt dependent manner and that phosphorylation inhibits Bax effects on the mitochondria by maintaining the protein in the cytoplasm, heterodimerized with anti-apoptotic Bcl-2 family members.
J. Biol. Chem, 10.1074/jbc.M400063200
Submitted on January 5, 2004
Revised on February 3, 2004
Accepted on February 6, 2004
Phosphorylation of Bax serine 184 by Akt regulates its activity and apoptosis in neutrophils
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