TTDN1 is a Plk1-interacting protein involved in maintenance of cell cycle integrity |
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Authors: | Y Zhang Y Tian Q Chen D Chen Z Zhai H-B Shu |
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Institution: | (1) College of Life Sciences, Peking University, Beijing, 100871, China;(2) College of Life Sciences, Wuhan University, Wuhan, 430072, China |
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Abstract: | Polo-like kinase 1 (Plk1) is a highly conserved serine/threonine kinase that plays critical roles in many cell cycle events,
especially in mitosis. In the present study, we identified TTDN1 as a potential interacting partner of Plk1 in yeast two-hybrid
screens. Sequence analysis indicates that TTDN1 contains a consensus Plk1-binding motif at its C terminus. TTDN1 colocalizes
with Plk1 at the centrosome in mitosis and the midbody during cytokinesis. TTDN1 is phosphorylated by Cdk1 in mitosis, and
this is required for its interaction with Plk1. Site-directed mutagenesis indicates that TTDN1 is phosphorylated at multiple
residues, including Ser93 and Ser104. Mutation of Thr120 of TTDN1 abolishes its interaction with Plk1, suggesting phosphorylation
of Thr120 in the consensus Plk1-binding motif is required for its interaction with Plk1. Overexpression of TTDN1 or its knockdown
by siRNA causes multi-polar spindles and multiple nuclei, suggesting that TTDN1 plays a role in regulating mitosis and cytokinesis.
Received 27 November 2006; received after revision 4 January 2007; accepted 25 January 2007
Y. Zhang, Y. Tian: These authors contribute equally to this work. |
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Keywords: | Plk1 Cdk1 TTDN1 cell cycle phosphorylation |
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