Polo-like kinase 1-mediated phosphorylation of the GTP-binding protein Ran is important for bipolar spindle formation
Copyright policy )Polo-like kinase 1-mediated phosphorylation of the GTP-binding protein Ran is important for bipolar spindle formation
Polo-like kinase functions are essential for the establishment of a normal bipolar mitotic spindle, although precisely how Plk1 regulates the spindle is uncertain. In this study, we report that the small GTP/GDP-binding protein Ran is associated with Plk1. Plk1 is capable of phosphorylating co-immunoprecipitated Ran in vitro on serine-135 and Ran is phosphorylated in vivo at the same site during mitosis when Plk1 is normally activated. Cell cultures over-expressing a Ran S135D mutant have significantly higher numbers of abnormal mitotic cells than those over-expressing either wild-type or S135A Ran. The abnormalities in S135D mutant cells are similar to cells over-expressing Plk1. Our data suggests that Ran is a physiological substrate of Plk1 and that Plk1 regulates the spindle organization partially through its phosphorylation on Ran.
- National Institute of Health Pakistan
- Science Applications International Corporation (United States) United States
- National Institute on Aging United States
- National Institutes of Health United States
Binding Sites, Mitosis, Cell Cycle Proteins, Protein Serine-Threonine Kinases, Cell Line, Polo-Like Kinase 1, Dogs, ran GTP-Binding Protein, Cell Line, Tumor, Proto-Oncogene Proteins, Mutation, Serine, Animals, Humans, Guanosine Triphosphate, Phosphorylation, Protein Binding
Binding Sites, Mitosis, Cell Cycle Proteins, Protein Serine-Threonine Kinases, Cell Line, Polo-Like Kinase 1, Dogs, ran GTP-Binding Protein, Cell Line, Tumor, Proto-Oncogene Proteins, Mutation, Serine, Animals, Humans, Guanosine Triphosphate, Phosphorylation, Protein Binding
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