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Phosphorylation by protein kinase CK2: A signaling switch for the caspase-inhibiting protein ARC

Official URL:https://doi.org/10.1016/S1097-2765(02)00600-7
PubMed:View item in PubMed
Creators Name:Li, P.F. and Li, J.C. and Mueller, E.C. and Otto, A. and Dietz, R. and von Harsdorf, R.
Journal Title:Molecular Cell
Journal Abbreviation:Mol Cell
Page Range:247-258
Date:August 2002
Keywords:Apoptosis, Casein Kinase II, Caspase 8, Caspase 9, Caspases, Cell Line, Cytoplasm, Cytoskeletal Proteins, Immediate-Early Proteins, Mitochondria, Skeletal Muscle, Myocardium, Nerve Tissue Proteins, Phosphorylation, Phosphotyrosine, Protein Binding, Protein Transport, Protein-Serine-Threonine Kinases, Wistar Rats, Signal Transduction, Time Factors, Animals, Rats
Abstract:Caspases play a central role in apoptosis, but their activity is under the control of caspase-inhibiting proteins. A characteristic of caspase-inhibiting proteins is direct caspase binding. It is yet unknown how the localization of caspase-inhibiting proteins is regulated and whether there are upstream signals controlling their function. Here we report that the function of ARC is regulated by protein kinase CK2. ARC at threonine 149 is phosphorylated by CK2. This phosphorylation targets ARC to mitochondria. ARC is able to bind to caspase-8 only when it is localized to mitochondria but not to the cytoplasm. Our results reveal a molecular mechanism by which a caspase-inhibiting protein requires phosphorylation in order to prevent apoptosis.
Publisher:Cell Press (U.S.A.)
Item Type:Article

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