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Vol. 10, Issue 5, 1495-1510, May 1999
,
Department of Biology, Queen's University, Kingston, Ontario K7L
3N6, Canada
The ssp1 gene encodes a protein kinase
involved in alteration of cell polarity in Schizosaccharomyces
pombe. ssp1 deletion causes stress sensitivity,
reminiscent of defects in the stress-activated MAP kinase, Spc1;
however, the two protein kinases do not act through the same pathway.
Ssp1 is localized mainly in the cytoplasm, but after a rise in external
osmolarity it is rapidly recruited to the plasma membrane,
preferentially to active growth zones and septa. Loss of Ssp1 function
inhibits actin relocalization during osmotic stress, in
cdc3 and cdc8 mutant backgrounds, and in
the presence of latrunculin A, implicating Ssp1 in promotion of actin
depolymerization. We propose a model in which Ssp1 can be activated
independently of Spc1 and can partially compensate for its loss. The
ssp1 deletion mutant exhibited monopolar actin distribution, but new end take-off (NETO) could be induced in these
cells by exposure to KCl or to latrunculin A pulse treatment. This
treatment induced NETO in cdc10 cells arrested in G1 but not in tea1 cells. This suggests that cells that contain
intact cell end markers are competent to undergo NETO throughout
interphase, and Ssp1 is involved in generating the NETO stimulus by
enlarging the actin monomer pool.
Corresponding author. E-mail address:
youngpg{at}biology.queensu.ca.
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