FAS-associated factor 1 interacts with protein kinase CK2 in vivo upon apoptosis induction

We show here that in several different cell lines protein kinase CK2 and Fa s-associated factor 1 (FAF1) exist together in a complex which is stable to high monovalent salt concentration. The CK2/FAF1 complex formation is sign ificantly increased after induction of apoptosis with various DNA damaging agents. Interestingly this effect is only seen in cell lines with an embryo nic origin and not when cells have entered a differentiated state. It is fu rther shown that the CK2 specific phosphorylation sites in the FAF1 molecul e, i.e. serines 289 and 291 influence this complex formation. Mutation of t he CK2 phosphorylation sites in the FAF1 molecule to alanine leads to a 1.5 to 2.0-fold higher association between CK2 and FAF1. Since the CK2 activit y did not increase concomitantly with the complex formation we conclude tha t the FAF1 becomes 'locked' to the CK2 enzyme so that a normal enzyme catal ysis does not take place anymore. Subcellular localization experiments invo lving CK2 subunits and FAF1 show a co-localization of both CK2 subunits and FAF1 in the peri-nuclear cytoplasm. The majority of CK2 subunits is found in the nucleus. FAF1 is also found in the nucleoli. The results obtained fu rther support the view that protein kinase CK2 plays an important role in c ertain steps of apoptosis.