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A more recent version of this article appeared on August 1, 2003
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Submitted on October 31, 2002
Revised on February 3, 2003
Accepted on February 19, 2003
-radiation- and okadaic acid induced- apoptosis
1 Department of Anatomy and Cell Biology, Medical faculty, University of Bergen, Årstadveien 19, N-5009 Bergen
2 Section of Molecular Hematology, Department of Internal Medicine, Haukeland University Hospital, N-5021 Bergen, Norway
* Corresponding author. E-mail address: stein.doskeland{at}iac.uib.no.
Protein phosphatase directed toxins like okadaic acid (OA) are general apoptosis inducers. We show that a protein ("inhibitor of radiation and OA induced apoptosis": Irod/Ian5), belonging to the family of immune associated nucleotide binding proteins, protected Jurkat T-cells against OA- and 
-radiation- induced apoptosis. Unlike previously described anti-apoptotic proteins Irod/Ian5 did not protect against anti-Fas, TNF-
, staurosporine, UV-light, or a number of chemotherapeutic drugs. Irod antagonized a calmodulin-dependent protein kinase II-dependent step upstream of activation of caspase 3. Irod has predicted GTP-binding, coiled-coil and membrane binding domains. Irod localized to the centrosomal/Golgi/ER compartment. Deletion of either the C-terminal membrane binding domain or the N-terminal GTP-binding domain did not affect the anti-apoptotic function of Irod, nor the centrosomal localization. The middle part of Irod, containing the coiled-coil domain, was therefore responsible for centrosomal anchoring and resistance towards death. Being widely expressed and able to protect also non-immune cells, the function of Irod may not be limited to the immune system. The function and localization of Irod indicate that the centrosome and calmodulin-dependent protein kinase II may have important roles in apoptosis signaling.
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