Ubiquitylation and degradation of serum-inducible kinase by hVPS18, a RING-H2 type ubiquitin ligase

Satomi Yogosawa, Shigetsugu Hatakeyama, Keiichi I. Nakayama, Hiroyuki Miyoshi, Shinichi Kohsaka, Chihiro Akazawa

Research output: Contribution to journalArticlepeer-review

25 Citations (Scopus)

Abstract

Serum-inducible kinase (SNK) is a member of polo-like kinases that serve as regulators of multiple events during cell division. Rapid changes in the activity and abundance of SNK were reported after the serum stimulation and after the activation of synaptic transmission in the brain. Yet the detailed mechanisms that control the level of SNK protein have not been fully elucidated. In this report, we show that the RING-H2 domain of hVPS18 (human vacuolar pro-tein sorting 18) has a genuine ubiquitin ligase (E3) activity. Using the yeast two-hybrid screening, we identify SNK as a candidate substrate of hVPS18. The half-life of SNK is increased in HeLa cells that down-regulated hVPS18 by lentivirus-mediated small hairpin RNA interference. Furthermore, the delayed entry into S phase is observed in HeLa cells overexpressing h VPS18. These results suggest that hVPS18 may play an important role in regulation of SNK activity through its ubiquitin ligase.

Original languageEnglish
Pages (from-to)41619-41627
Number of pages9
JournalJournal of Biological Chemistry
Volume280
Issue number50
DOIs
Publication statusPublished - Dec 16 2005

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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