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Ubiquitin ligase Ufd2 is required for efficient degradation of Mps1 kinase.

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.

Pubmed ID: 22045814

Authors

  • 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

Journal

The Journal of biological chemistry

Publication Data

December 23, 2011

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM 078085
  • Agency: NIGMS NIH HHS, Id: R01 GM077311

Mesh Terms

  • Anaphase-Promoting Complex-Cyclosome
  • Animals
  • Bone Marrow Cells
  • Candida albicans
  • Cell Cycle Proteins
  • Cell Line, Tumor
  • Gene Expression Regulation, Fungal
  • Humans
  • Lectins
  • Male
  • Mice
  • Mitosis
  • Protein-Serine-Threonine Kinases
  • Protein-Tyrosine Kinases
  • Proteolysis
  • Saccharomyces cerevisiae Proteins
  • Ubiquitin
  • Ubiquitin-Conjugating Enzymes
  • Ubiquitin-Protein Ligase Complexes
  • Ubiquitin-Protein Ligases