Phosphorylation of the septin cdc3 in g1 by the cdc28 kinase is essential for efficient septin ring disassembly.

摘要: The septins constitute a family of filament-forming proteins ubiquitous in eukaryotic species. We demonstrate here that the Saccharomyces cerevisiae septin, Cdc3, is substrate cell cycle regulatory cyclin-dependent kinase (Cdk), Cdc28. Two serines near C-terminus Cdc3 are phosphorylated Cdc28-dependent manner. Analysis mutant allele cannot be at these sites revealed an effect Cdc28 phosphorylation time budding. Immunofluorescence analysis wild-type and indicated prevention impairs disassembly old septin ring, which inherited mitosis but usually disappears immediately prior to assembly new ring. Furthermore, immuno-fluorescence ring dynamics G1 cyclin (Cln) suggests function required for efficient disassembly. Thus, by end may facilitate initiation promoting obsolete from previous cycle.