Growth factors inactivate the cell death promoter BAD by phosphorylation of its BH3 domain on Ser155
XM Zhou, Y Liu, G Payne, RJ Lutz… - Journal of Biological …, 2000 - ASBMB
The Bcl-2 family protein BAD promotes apoptosis by binding through its BH3 domain to Bcl-x
L and related cell death suppressors. When BAD is phosphorylated on either Ser 112 or Ser
136, it forms a complex with 14-3-3 in the cytosol and no longer interacts with Bcl-x L at the
mitochondria. Here we show that phosphorylation of a distinct site Ser 155, which is at the
center of the BAD BH3 domain, directly suppressed the pro-apoptotic function of BAD by
eliminating its affinity for Bcl-x L. Protein kinase A functioned as a BAD Ser 155 kinase both …
L and related cell death suppressors. When BAD is phosphorylated on either Ser 112 or Ser
136, it forms a complex with 14-3-3 in the cytosol and no longer interacts with Bcl-x L at the
mitochondria. Here we show that phosphorylation of a distinct site Ser 155, which is at the
center of the BAD BH3 domain, directly suppressed the pro-apoptotic function of BAD by
eliminating its affinity for Bcl-x L. Protein kinase A functioned as a BAD Ser 155 kinase both …
