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Fig. 8. Model for how reversible AKAP95-PKA interaction (mediated by RII{alpha} phosphorylation) controls chromatin structure during mitosis. During interphase, AKAP95 and PKA-RII{alpha} localize to distinct compartments, separated by the nuclear envelope. At mitosis entry, AKAP95 associates with condensing chromatin. RII{alpha} is phosphorylated by the CDK1-cyclin-B complex. RII{alpha} phosphorylation turns on a molecular switch promoting RII{alpha} anchoring to AKAP95 and maintenance of condensed chromosomes during mitosis. (Although anchoring of RII{alpha} to AKAP95 has been demonstrated, anchoring of the catalytic subunit of PKA is only suggested.) Throughout mitosis, anchoring of phosphorylated RII{alpha} to chromatin-bound AKAP95 is required to prevent PCD. At mitosis exit, dephosphorylation of RII{alpha} by a threonine phosphatase induces RII{alpha} dissociation from chromatin-bound AKAP95. This relieves inhibition of chromatin decondensation, allowing chromosome decondensation as the nuclear envelope reassembles.