The role of Plo1 kinase in mitotic commitment and septation in Schizosaccharomyces pombe

Tanaka, Kayoko; Petersen, Janni; Maclver, Fiona; Mulvihill, Daniel P.; Glover, David M.; Hagan, Iain M.
March 2001
EMBO Journal;3/15/2001, Vol. 20 Issue 6, p1259
Academic Journal
Plo1-associated casein kinase activity peaked during mitosis before septation. Phosphatase treatment abolished this activity. Mitotic Plo1 activation had a requirement for prior activation of M-phase promoting factor (MPF), suggesting that Plo1 does not act as a mitotic trigger kinase to initiate MPF activation during mitotic commitment. A link between Plo1 and the septum initiating network (SIN) has been suggested by the inability of plo1? cells to septate and the prolific septation following plo1+ overexpression. Interphase activation of Spg1, the G protein that modulates SIN activity, induced septation but did not stimulate Plo1-associated kinase activity. Conversely, SIN inactivation did not affect the mitotic stimulation of Plo1-associated kinase activity. plo1.ts4 cells formed a misshapen actin ring, but rarely septated at 36°C. Forced activation of Spg1 enabled plo1.ts4 mutant cells, but not cells with defects in the SIN component Sid2, to convert the actin ring to a septum. The ability of plo1+ overexpression to induce septation was severely compromised by SIN inactivation. We propose that Plo1 acts before the SIN to control septation.


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