Preparing your results

Our searching services are busy right now. Your search will reload in five seconds.

X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

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

http://www.ncbi.nlm.nih.gov/pubmed/22045814

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 RIS Download

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

Research resources used in this publication

None found

Research tools detected in this publication

None found

Data used in this publication

None found

Associated grants

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

BioGRID (Data, Interactions)

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.