The functioning of the drosophila CPEB protein orb is regulated by phosphorylation and requires casein kinase 2 activity

Li Chin Wong, Alexandre Costa, Ian McLeod, Ali Sarkeshik, John Yates, Saw Kyin, David Perlman, Paul Schedl

Research output: Contribution to journalArticlepeer-review

18 Scopus citations

Abstract

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.

Original languageEnglish (US)
Article numbere24355
JournalPloS one
Volume6
Issue number9
DOIs
StatePublished - Sep 19 2011

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)
  • General

Fingerprint Dive into the research topics of 'The functioning of the drosophila CPEB protein orb is regulated by phosphorylation and requires casein kinase 2 activity'. Together they form a unique fingerprint.

Cite this