Reaction: ATP + a protein = ADP + a phosphoprotein
Other name(s): Cdc5; Cdc5p; Plk; PLK; Plk1; Plo1; POLO kinase; polo serine-threonine kinase; polo-like kinase; polo-like kinase 1; serine/threonine-specific Drosophila kinase polo; STK21
Systematic name: ATP:protein phosphotransferase (spindle-pole-dependent)
Comments: The enzyme associates with the spindle pole during mitosis and is thought to play an important role in the dynamic function of the mitotic spindle during chromosome segregation. The human form of the enzyme, Plk1, does not phosphorylate histone H1, enolase and phosvitin but it can phosphorylate myelin basic protein and microtubule-associated protein MAP-2, although to a lesser extent than casein [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 149433-93-2
References:
1. Llamazares, S., Moreira, A., Tavares, A., Girdham, C., Spruce, B.A., Gonzalez, C., Karess, R.E., Glover, D.M. and Sunkel, C.E. polo encodes a protein kinase homolog required for mitosis in Drosophila. Genes Dev. 5 (1991) 2153-2165. [PMID: 1660828]
2. Golsteyn, R.M., Mundt, K.E., Fry, A.M. and Nigg, E.A. Cell cycle regulation of the activity and subcellular localization of Plk1, a human protein kinase implicated in mitotic spindle function. J. Cell Biol. 129 (1995) 1617-1628. [PMID: 7790358]
3. Mulvihill, D.P. and Hyams, J.S. Cytokinetic actomyosin ring formation and septation in fission yeast are dependent on the full recruitment of the polo-like kinase Plo1 to the spindle pole body and a functional spindle assembly checkpoint. J. Cell. Sci. 115 (2002) 3575-3586. [PMID: 12186944]
4. Ohkura, H. Phosphorylation: polo kinase joins an elite club. Curr. Biol. 13 (2003) R912-R914. [PMID: 14654016]