Polo-like kinase 1 (Plk1) plays essential roles at multiple events during cell division, yet little is known about its physiological substrates. In a cDNA phage display screen using Plk1 C-terminal affinity columns, we identified NudC (nu clear d istribution gene C) as a Plk1 binding protein. Here, we characterize the interaction between Plk1 and NudC, show that Plk1 phosphorylates NudC at conserved S274 and S326 residues in vitro, and present evidence that NudC is also a substrate for Plk1 in vivo. Downregulation of NudC by RNA interference results in multiple mitotic defects, including multinucleation and cells arrested at the midbody stage, which are rescued by ectopic expression of wild-type NudC, but not by NudC with mutations in the Plk1 phosphorylation sites. These results suggest that Plk1 phosphorylation of NudC may influence cytokinesis.
|Number of pages||12|
|State||Published - Jul 1 2003|
Bibliographical noteFunding Information:
We thank Young-Joo Jang, Sheng Ma, Matthew Michael, Gideon Dreyfuss, Eleanor Erikson, Yang Shi, and Sue-hwa Lin for critical comments and discussion. This work was supported by National Institutes of Health Grant GM59172. R.L.E. is the John F. Drum American Cancer Society Research Professor.
ASJC Scopus subject areas
- Molecular Biology
- Biochemistry, Genetics and Molecular Biology (all)
- Developmental Biology
- Cell Biology