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 language | English (US) |
|---|---|
| Pages (from-to) | 43660-43667 |
| Number of pages | 8 |
| Journal | Journal of Biological Chemistry |
| Volume | 286 |
| Issue number | 51 |
| DOIs | |
| State | Published - Dec 23 2011 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology
Cite this
Ubiquitin ligase Ufd2 is required for efficient degradation of Mps1 kinase. / Liu, Chang; Van Dyk, Dewald; Choe, Vitnary; Yan, Jing; Majumder, Shubhra; Costanzo, Michael; Bao, Xin; Boone, Charles; Huo, Keke; Winey, Mark; Fisk, Harold; Andrews, Brenda; Rao, Hai.
In: Journal of Biological Chemistry, Vol. 286, No. 51, 23.12.2011, p. 43660-43667.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Ubiquitin ligase Ufd2 is required for efficient degradation of Mps1 kinase
AU - Liu, Chang
AU - Van Dyk, Dewald
AU - Choe, Vitnary
AU - Yan, Jing
AU - Majumder, Shubhra
AU - Costanzo, Michael
AU - Bao, Xin
AU - Boone, Charles
AU - Huo, Keke
AU - Winey, Mark
AU - Fisk, Harold
AU - Andrews, Brenda
AU - Rao, Hai
PY - 2011/12/23
Y1 - 2011/12/23
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=83755162358&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=83755162358&partnerID=8YFLogxK
U2 - 10.1074/jbc.M111.286229
DO - 10.1074/jbc.M111.286229
M3 - Article
C2 - 22045814
AN - SCOPUS:83755162358
VL - 286
SP - 43660
EP - 43667
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 51
ER -