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Mol. Cell. Biol., 06 1997, 3408-3417, Vol 17, No. 6
KS Lee and RL Erikson
Plk is a mammalian serine/threonine protein kinase whose activity peaks at
the onset of M phase. It is closely related to other mammalian kinases,
Snk, Fnk, and Prk, as well as to Xenopus laevis Plx1, Drosophila
melanogaster polo, Schizosaccharomyces pombe Plo1, and Saccharomyces
cerevisiae Cdc5. The M phase of the cell cycle is a highly coordinated
process which insures the equipartition of genetic and cellular materials
during cell division. To enable understanding of the function of Plk during
M phase progression, various Plk mutants were generated and expressed in
Sf9 cells and budding yeast. In vitro kinase assays with Plk
immunoprecipitates prepared from Sf9 cells indicate that Glu206 and Thr210
play equally important roles for Plk activity and that replacement of
Thr210 with a negatively charged residue elevates Plk specific activity.
Ectopic expression of wild-type Plk (Plk WT) complements the cell division
defect associated with the cdc5-1 mutation in S. cerevisiae. The degree of
complementation correlates closely with the Plk activity measured in vitro,
as it is enhanced by a mutationally activated Plk, T210D, but is not
observed with the inactive forms K82M, D194N, and D194R. In a CDC5
wild-type background, expression of Plk WT or T210D, but not of inactive
forms, induced a sharp accumulation of cells in G1. Consistent with
elevated Plk activity, this phenomenon was enhanced by the C-terminally
deleted forms WT deltaC and T210D deltaC. Expression of T210D also induced
a class of cells with unusually elongated buds which developed multiple
septal structures. This was not observed with the C-terminally deleted form
T210D deltaC, however. It appears that the C terminus of Plk is not
required for the observed cell cycle influence but may be important for
polarized cell growth and septal structure formation.
Copyright © 1997, American Society for Microbiology
Plk is a functional homolog of Saccharomyces cerevisiae Cdc5, and elevated Plk activity induces multiple septation structures
Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138, USA. kslee@hubio2.harvard.edu
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