Inactivation of Bcl-2 by phosphorylation
TLDR
Using the phosphatase inhibitor okadaic acid or the chemotherapeutic drug taxol, it is found that Bcl-2 was phosphorylated in lymphoid cells, which seems to inhibit its ability to interfere with apoptosis.Abstract:
The antiapoptosis potential of Bcl-2 protein is well established, but the mechanism of Bcl-2 action is still poorly understood. Using the phosphatase inhibitor okadaic acid or the chemotherapeutic drug taxol, we 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 induction of apoptosis in these cells. Thus, phosphorylation of Bcl-2 seems to inhibit its ability to interfere with apoptosis. In addition, phosphorylated Bcl-2 can no longer prevent lipid peroxidation as required to protect cells from apoptosis.read more
Citations
More filters
Journal ArticleDOI
BCL-2 family members and the mitochondria in apoptosis
TL;DR: As the BCL-2 family members reside upstream of irreversible cellular damage and focus much of their efforts at the level of mitochondria, they play a pivotal role in deciding whether a cell will live or die, and it is argued that the amphipathic a-helical BH3 domain serves as a critical death domain in the pro-apoptotic members.
Journal ArticleDOI
Serine Phosphorylation of Death Agonist BAD in Response to Survival Factor Results in Binding to 14-3-3 Not BCL-XL
TL;DR: The rapid phosphorylation of BAD following IL-3 connects a proximal survival signal with the BCL-2 family, modulating this checkpoint for apoptosis and enhanced BAD's death-promoting activity.
Journal ArticleDOI
Movement of Bax from the Cytosol to Mitochondria during Apoptosis
TL;DR: In cells undergoing apoptosis, an early, dramatic change occurs in the intracellular localization of Bax, and this redistribution of soluble Bax to organelle-bound GFP–Bax appears important for Bx to promote cell death.
Journal ArticleDOI
Apoptosis in cancer
Scott W. Lowe,Athena W. Lin +1 more
TL;DR: An intense research effort is uncovering the underlying mechanisms of apoptosis such that, in the next decade, one envisions that this information will produce new strategies to exploit apoptosis for therapeutic benefit.
Journal ArticleDOI
Requirement of JNK for Stress- Induced Activation of the Cytochrome c-Mediated Death Pathway
Cathy Tournier,Patricia M. Hess,Derek D. Yang,Jie Xu,Tod K. Turner,Anjaruwee S. Nimnual,Dafna Bar-Sagi,Stephen N. Jones,Richard A. Flavell,Roger J. Davis +9 more
TL;DR: It is shown here that JNK is required for UV-induced apoptosis in primary murine embryonic fibroblasts, and data indicate that mitochondria are influenced by proapoptotic signal transduction through the JNK pathway.