S. Haldar et al., INACTIVATION OF BCL-2 BY PHOSPHORYLATION, Proceedings of the National Academy of Sciences of the United Statesof America, 92(10), 1995, pp. 4507-4511
The antiapoptosis potential of Bcl-2 protein is well established, but
the mechanism of Bcl-2 action is still poorly understood. Using the ph
osphatase inhibitor okadaic acid or the chemotherapeutic drug taxol, w
e found that Bcl-2 was phosphorylated in lymphoid cells. Phospho amino
acid analysis revealed that Bcl-2 was phosphorylated on serine. Under
similar conditions, okadaic acid or taxol treatment led to the induct
ion of apoptosis in these cells. Thus, phosphorylation of Bcl-2 seems
to inhibit its ability to interfere with apoptosis. In addition, phosp
horylated Bcl-2 can no longer prevent lipid peroxidation as required t
o protect cells from apoptosis.