Ubiquitin ligase Ufd2 is required for efficient degradation of Mps1 kinase

Chang Liu, Dewald Van Dyk, Vitnary Choe, Jing Yan, Shubhra Majumder, Michael Costanzo, Xin Bao, Charles Boone, Keke Huo, Mark Winey, Harold Fisk, Brenda Andrews, Hai Rao

Research output: Contribution to journalArticle

15 Scopus citations

Abstract

Ufd2 is a U-box-containing ubiquitylation enzyme that promotes ubiquitin chain assembly on substrates. The physiological function of Ufd2 remains poorly understood. Here, we show that ubiquitylation and degradation of the cell cycle kinase Mps1, a known target of the anaphase-promoting complex E3, require Ufd2 enzyme. Yeast cells lacking UFD2 exhibit altered chromosome stability and several spindle-related phenotypes, expanding the biological function of Ufd2. We demonstrate that Ufd2-mediated Mps1 degradation is conserved in humans. Our results underscore the significance of Ufd2 in proteolysis and further suggest that Ufd2-like enzymes regulate far more substrates than previously envisioned.

Original languageEnglish (US)
Pages (from-to)43660-43667
Number of pages8
JournalJournal of Biological Chemistry
Volume286
Issue number51
DOIs
StatePublished - Dec 23 2011
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Liu, C., Van Dyk, D., Choe, V., Yan, J., Majumder, S., Costanzo, M., Bao, X., Boone, C., Huo, K., Winey, M., Fisk, H., Andrews, B., & Rao, H. (2011). Ubiquitin ligase Ufd2 is required for efficient degradation of Mps1 kinase. Journal of Biological Chemistry, 286(51), 43660-43667. https://doi.org/10.1074/jbc.M111.286229