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Biochem Biophys Res Commun. 2005 Dec 23;338(3):1359-67. Epub 2005 Oct 25.

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

Author information

1
Division of Human Biology, Fred Hutchinson Cancer Research Center, Seattle, WA 98109, USA.

Abstract

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.

PMID:
16263084
DOI:
10.1016/j.bbrc.2005.10.090
[Indexed for MEDLINE]

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