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Phosphorylation of BAD at Ser‐128 during mitosis and paclitaxel‐induced apoptosis
Author(s) -
Berndtsson Maria,
Konishi Yoshiyuki,
Bonni Azad,
Hägg Maria,
Shoshan Maria,
Linder Stig,
Havelka Aleksandra Mandic
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.04.067
Subject(s) - phosphorylation , apoptosis , mitosis , microbiology and biotechnology , serine , cell cycle , paclitaxel , protein phosphorylation , chemistry , biology , biochemistry , cancer , genetics , protein kinase a
Phosphorylation of BCL‐2 family member BAD at different residues triggers different physiological effects, either inhibiting or promoting apoptosis. The recently identified phosphorylation site at Ser‐128 enhances the apoptotic activity of BAD. We here show that BAD becomes phosphorylated at Ser‐128 in the mitotic phase of the cell cycle in NIH3T3 cells. We also show that BAD‐S128 is phosphorylated in taxol‐treated mouse fibroblasts and MDA‐MB‐231 human breast cancer cells. However, expression of a phosphorylation‐defective dominant negative BAD mutant did not block taxol‐induced apoptosis. These data support the view that the phosphorylation of BAD Serine 128 exerts cell‐specific effects on apoptosis. Whereas the BAD Serine 128 phosphorylation induces apoptosis in neuronal cells, it does not appear to promote apoptosis in proliferating non‐neural cells during mitosis or upon exposure to the antineoplastic agent taxol.