Journal
MOLECULAR CELL
Volume 19, Issue 3, Pages 321-332Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2005.06.024
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- NCI NIH HHS [CA21765-25, CA075162] Funding Source: Medline
- NIGMS NIH HHS [GM044088-13] Funding Source: Medline
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FADD is essential for death receptor (DR)-induced apoptosis. However, it is also critical for cell cycle progression and proliferation, activities that are regulated by phosphorylation of its C-terminal Ser194, which has also been implicated in sensitizing cancer cells to chemotherapeutic drugs and in regulating FADD's intracellular localization. We now demonstrate that casein kinase l alpha (CKI alpha) phosphorylates FADD at Ser194 both in vitro and in vivo. FADD-CKI alpha association regulates the subcellular localization of FADD, and phosphorylated FADD was found to colocalize with CKI alpha on the spindle poles in metaphase. Inhibition of CKI alpha diminished FADD phosphorylation, prevented the ability of Taxol to arrest cells in mitosis, and blocked mitogen-induced proliferation of mouse splenocytes. In contrast, a low level of cycling splenocytes from mice expressing FADD with a mutated phosphorylation site was insensitive to CKI inhibition. These data suggest that phosphorylation of FADD by CKI is a crucial event during mitosis.
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