Abstract
Ski is a negative regulator of the transforming growth factor-β and other signalling pathways. The absence of SKI in mouse fibroblasts leads to chromosome segregation defects and genomic instability, suggesting a role for Ski during mitosis. At this stage, Ski is phosphorylated but to date little is known about the kinases involved in this process. Here, we show that Aurora A kinase is able to phosphorylate Ski in vitro. In vivo, Aurora A and Ski co-localized at the centrosomes and co-immunoprecipitated. Conversely, a C-terminal truncation mutant of Ski (SkiΔ491-728) lacking a coiled-coil domain, displayed decreased centrosomal localization. This mutant no longer co-immunoprecipitated with Aurora-A in vivo, but was still phosphorylated in vitro, indicating that the Ski-Aurora A interaction takes place at the centrosomes. These data identify Ski as a novel target of Aurora A and contribute to an understanding of the role of these proteins in the mitotic process.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 539-543 |
| Number of pages | 5 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 409 |
| Issue number | 3 |
| DOIs | |
| State | Published - Jun 10 2011 |
| Externally published | Yes |
Fingerprint
Keywords
- Aurora A
- Ski
- Ski phosphorylation
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Cell Biology
- Molecular Biology
Cite this
Identification of Ski as a target for Aurora A kinase. / Mosquera, Jocelyn; Armisen, Ricardo; Zhao, Hongling; Rojas, Diego A.; Maldonado, Edio; Tapia, Julio C.; Colombo, Alicia; Hayman, Michael J.; Marcelain, Katherine.
In: Biochemical and Biophysical Research Communications, Vol. 409, No. 3, 10.06.2011, p. 539-543.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Identification of Ski as a target for Aurora A kinase
AU - Mosquera, Jocelyn
AU - Armisen, Ricardo
AU - Zhao, Hongling
AU - Rojas, Diego A.
AU - Maldonado, Edio
AU - Tapia, Julio C.
AU - Colombo, Alicia
AU - Hayman, Michael J.
AU - Marcelain, Katherine
PY - 2011/6/10
Y1 - 2011/6/10
N2 - Ski is a negative regulator of the transforming growth factor-β and other signalling pathways. The absence of SKI in mouse fibroblasts leads to chromosome segregation defects and genomic instability, suggesting a role for Ski during mitosis. At this stage, Ski is phosphorylated but to date little is known about the kinases involved in this process. Here, we show that Aurora A kinase is able to phosphorylate Ski in vitro. In vivo, Aurora A and Ski co-localized at the centrosomes and co-immunoprecipitated. Conversely, a C-terminal truncation mutant of Ski (SkiΔ491-728) lacking a coiled-coil domain, displayed decreased centrosomal localization. This mutant no longer co-immunoprecipitated with Aurora-A in vivo, but was still phosphorylated in vitro, indicating that the Ski-Aurora A interaction takes place at the centrosomes. These data identify Ski as a novel target of Aurora A and contribute to an understanding of the role of these proteins in the mitotic process.
AB - Ski is a negative regulator of the transforming growth factor-β and other signalling pathways. The absence of SKI in mouse fibroblasts leads to chromosome segregation defects and genomic instability, suggesting a role for Ski during mitosis. At this stage, Ski is phosphorylated but to date little is known about the kinases involved in this process. Here, we show that Aurora A kinase is able to phosphorylate Ski in vitro. In vivo, Aurora A and Ski co-localized at the centrosomes and co-immunoprecipitated. Conversely, a C-terminal truncation mutant of Ski (SkiΔ491-728) lacking a coiled-coil domain, displayed decreased centrosomal localization. This mutant no longer co-immunoprecipitated with Aurora-A in vivo, but was still phosphorylated in vitro, indicating that the Ski-Aurora A interaction takes place at the centrosomes. These data identify Ski as a novel target of Aurora A and contribute to an understanding of the role of these proteins in the mitotic process.
KW - Aurora A
KW - Ski
KW - Ski phosphorylation
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U2 - 10.1016/j.bbrc.2011.05.040
DO - 10.1016/j.bbrc.2011.05.040
M3 - Article
VL - 409
SP - 539
EP - 543
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -