Polo-like kinases: a team that plays throughout mitosis
- David M. Glover1,3,
- Iain M. Hagan2, and
- Álvaro A.M. Tavares1
- 1CRC Cell Cycle Genetics Group, Department of Anatomy and Physiology, Medical Sciences Institute, University of Dundee, Dundee DD1 4HN, UK; 2School of Biological Sciences, University of Manchester, Manchester M13 9PT, UK
This extract was created in the absence of an abstract.
When the first mutant allele of the Drosophila genepolo was first characterized over 10 years ago, attention focused on the defects that centrosome behavior exhibited at various stages of development (Sunkel and Glover 1988). The subsequent realization that the serine-threonine kinase it encodes is highly conserved from yeasts to humans has provoked a flurry of investigation into the function of the enzyme. A role for the polo-like kinases (plks) in regulating centrosome behavior has been borne out in several organisms, and the enzymes have attracted further attention recently with the realization that they regulate multiple stages of mitotic progression. In this article we review the current status of our understanding of the functions of plks from the time of commitment to M phase in the activation of Cdc25, through the activation of the anaphase promoting complex (APC), to the regulation of late mitotic events essential for cytokinesis. We discuss how to reconcile the sometimes apparently disparate observations made upon plk function in different organisms.
The team members
The plks are recognizable as a team because in addition to a highly conserved amino-terminal catalytic domain, their carboxyl termini contain three conserved regions, the polo boxes (for review, see Glover et al. 1996; Lane and Nigg 1997). Whereas in the yeasts andDrosophila only a single plk gene has been identified to date (Llamazares et al. 1991; Kitada et al. 1993; Ohkura et al. 1995), the higher vertebrates have multiple plk genes of which Plk1 is most similar to Drosophila polo. Two other plks, Snk and Fnk, have been described in mouse, as well as their human counterparts, hSnk and Prk [Clay et al. 1993; Lake and Jelinek 1993; Hamanaka et al. 1994; Holtrich et al. 1994; Golsteyn et al. 1994; Li et al. …
