Zcchc8 is a glycogen synthase kinase-3 substrate that interacts with RNA-binding proteins

Michael P. Gustafson, Markus Welcker, Harry C. Hwang, Bruce E. Clurman

Research output: Contribution to journalArticlepeer-review

18 Scopus citations


Phosphorylation of c-Myc on threonine 58 (T58) stimulates its degradation by the Fbw7-SCF ubiquitin ligase. We used a phosphorylation-specific antibody raised against the c-Myc T58 region to attempt to identify other proteins regulated by the Fbw7 pathway. We identified two predominant proteins recognized by this antibody. The first is Ebna1 binding protein 2, a nucleolar protein that, in contrast with a previous report, is likely responsible for the nucleolar staining exhibited by this antibody. The second is Zcchc8, a nuclear protein that is highly phosphorylated in cells treated with nocodazole. We show that Zcchc8 is directly phosphorylated by GSK-3 in vitro and that GSK-3 inhibition prevents Zcchc8 phosphorylation in vivo. Moreover, we found that Zcchc8 interacts with proteins involved in RNA processing/degradation. We suggest that Zcchc8 is a GSK-3 substrate with a role in RNA metabolism.

Original languageEnglish (US)
Pages (from-to)1359-1367
Number of pages9
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - Dec 23 2005


  • Ebna1 binding protein 2
  • GSK-3
  • Myc
  • RNA processing
  • Zcchc8

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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