IMR Press / FBS / Volume 4 / Issue 2 / DOI: 10.2741/S290

Frontiers in Bioscience-Scholar (FBS) is published by IMR Press from Volume 13 Issue 1 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on as a courtesy and upon agreement with Frontiers in Bioscience.

14-3-3zeta cooperates with phosphorylated Plk1 and is required for correct cytokinesis
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1 Department of Biochemistry and Molecular Biology, Anhui Medical University, Hefei 230032, China
2 Department of Anaesthesiology, the First Affiliated Hospital of Anhui Medical University, Hefei 230032, China
3 Key Laboratory of Gene Resource Utilization for Genetic Diseases of Educational Ministry and Anhui Province, Anhui Medical University, Hefei 230032, China
4 Anhui Provincial Key Laboratory for Cellular Dynamics and Chemical Biology, Hefei 230027, China
5 Department of Microbiology and Parasitology, Anhui Provincial Key Laboratory of Genomic Research, Anhui Medical University, Hefei 230032, China
6 Department of Oncology, Anhui Provincial Hospital, Hefei 230001, China

*Author to whom correspondence should be addressed.

Academic Editor: Xueji Zhang

Front. Biosci. (Schol Ed) 2012, 4(2), 639–650;
Published: 1 January 2012
(This article belongs to the Special Issue Biosensors and their applications)

Proteins of the 14-3-3 family are functionally conserved in eukaryotic kingdom which participates in diversified and critical cellular processes. However, the exact roles of these proteins in mitotic regulation has remained elusive. Polo-like kinase 1 (Plk1) is a serine/threonine protein kinase that plays multiple critical functions such as centrosome maturation, mitotic chromosome segregation, cytokinesis, and the DNA damage response. Here we show that 14-3-3zeta interacts and cooperates with Plk1 in mitotic progress. 14-3-3zeta is associated with the spindle at metaphase and concentrated in the midbody during cytokinesis. Using yeast two hybrid assay, we found a functional connection between 14-3-3zeta and Plk1. We demonstrate that phosphorylation of Plk1 at S330 and S597 promotes its interaction with 14-3-3zeta. Importantly, 14-3-3zeta cooperates with Plk1 in ensuring successful cytokinesis. We conclude that mitotic phosphorylation of Plk1 promotes interaction with 14-3-3zeta and this interaction is required for faithful cytokinesis. Taken together with the results of previous studies, our results suggest 14-3-3 family emerges as a novel player in mitotic regulation: cooperation with Plk1 to ensure a faithful cytokinesis.

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