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- W3040942600 abstract "5417 Previously we had shown that BAD plays a critical role in apoptosis of MCF-7 breast CA cells (MBC, 15:3266,2004). Recently we have observed that BAD is a regulator of cell proliferation in the MCF-7 cell line (AACR 2004 Abs# 4824). App 20% of endogenous BAD is localized in the nucleus. Phosphorylated (p) BAD (S136) can also be observed in the nucleus where as both S136 and S112 pBAD is localized in the nuclear fraction upon over expression of wild type (wt) BAD. Over expressed wtBAD inhibited E2 induced proliferation fraction (PF) but dual phosphorylation site mutant (S136A/S112A (dmBAD)) did not. Removal of endogenous BAD by specific siRNA appeared to increase PF following E2 treatment. Endogenous cyclin D1 (CD1) was also increased by siRNA for BAD. WtBAD but not dmBAD inhibited serum or E2 stimulated CD1 synthesis. Using CRE and AP-1 mutants of the CD1 reporter we found that BAD inhibits expression of CD1 mainly through the CRE element, whereas dmBAD was ineffective. This inhibition appears to be mediated by the ability of wtBAD but not dmBAD to interact with c-jun. BAD appears to inhibit phospho c-jun formation by inhibiting Erk as well as JNK. Thus we demonstrate a novel role for BAD in cell cycle regulation which is dependent on phosphorylation of S112/136 residues but not on BAD/BCL2 interaction. (supported by NIH)" @default.
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- W3040942600 date "2005-05-01" @default.
- W3040942600 modified "2023-09-26" @default.
- W3040942600 title "Phospho BAD decreases breast cancer cell proliferation by inhibiting c-jun activation of the CRE in cyclin D1" @default.
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