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The Orb CPEB protein regulates translation of localized mRNAs in  Drosophila  ovaries. While there are multiple hypo- and hyperphosphorylated Orb isoforms in wild type ovaries, most are missing in  orb F303  , which has an amino acid substitution in a buried region of the second RRM domain. Using a proteomics approach we identified a candidate Orb kinase, Casein Kinase 2 (CK2). In addition to being associated with Orb  in vivo , we show that  ck2  is required for  orb  functioning in  gurken  signaling and in the autoregulation of  orb  mRNA localization and translation. Supporting a role for  ck2  in Orb phosphorylation, we find that the phosphorylation pattern is altered when  ck2  activity is partially compromised. Finally, we show that the Orb hypophosphorylated isoforms are in slowly sedimenting complexes that contain the translational repressor Bruno, while the hyperphosphorylated isoforms assemble into large complexes that co-sediment with polysomes and contain the Wisp poly(A) polymerase.

The Functioning of the Drosophila CPEB Protein Orb Is Regulated by Phosphorylation and Requires Casein Kinase 2 Activity