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

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

Research output: Contribution to journalArticle

16 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)1359-1367
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume338
Issue number3
DOIs
StatePublished - Dec 23 2005
Externally publishedYes

Fingerprint

Glycogen Synthase Kinase 3
Phosphorylation
RNA-Binding Proteins
Threonine
Nuclear Proteins
Antibodies
SKP Cullin F-Box Protein Ligases
Substrates
RNA
Nocodazole
Degradation
Proteins
RNA Stability
Metabolism
Carrier Proteins
Staining and Labeling
Processing

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Zcchc8 is a glycogen synthase kinase-3 substrate that interacts with RNA-binding proteins. / Gustafson, Michael; Welcker, Markus; Hwang, Harry C.; Clurman, Bruce E.

In: Biochemical and Biophysical Research Communications, Vol. 338, No. 3, 23.12.2005, p. 1359-1367.

Research output: Contribution to journalArticle

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AU - Welcker, Markus

AU - Hwang, Harry C.

AU - Clurman, Bruce E.

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AB - 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.

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