Abstract:
:Bcl-xL, a close homolog of Bcl2, is an important regulator of apoptosis and is overexpressed in human cancer. Phosphorylation of Bcl-xL can be induced by microtubule-damaging drugs such as taxol or 2-methoxyestradiol (2-ME). By site-directed mutagenesis studies, we have identified that serine 62 is the necessary site for taxol- or 2-ME-induced Bcl-xL phosphorylation in prostate cancer cells. Further studies with the inhibitor of Jun kinase (JNK) and phosphorylation null mutant of Bcl-xL reveal the augmentative role of JNK-mediated Bcl-xL phosphorylation in apoptosis of prostate cancer cells. In summary, our studies suggest that the phosphorylation of Bcl-xL by stress response kinase signaling might oppose the anti-apoptotic function of Bcl-xL to permit prostate cancer cells to die by apoptosis.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Basu A,Haldar Sdoi
10.1016/s0014-5793(03)00131-5keywords:
subject
Has Abstractpub_date
2003-03-13 00:00:00pages
41-7issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579303001315journal_volume
538pub_type
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