title: Sid2p, a spindle pole body kinase that regulates the onset of cytokinesis.
abstract: The fission yeast Schizosaccharomyces pombe divides by medial fission through the use of an actomyosin contractile ring. Precisely at the end of anaphase, the ring begins to constrict and the septum forms. Proper coordination of cell division with mitosis is crucial to ensure proper segregation of chromosomes to daughter cells. The Sid2p kinase is one of several proteins that function as part of a novel signaling pathway required for initiation of medial ring constriction and septation. Here, we show that Sid2p is a component of the spindle pole body at all stages of the cell cycle and localizes transiently to the cell division site during medial ring constriction and septation. A medial ring and an intact microtubule cytoskeleton are required for the localization of Sid2p to the division site. We have established an in vitro assay for measuring Sid2p kinase activity, and found that Sid2p kinase activity peaks during medial ring constriction and septation. Both Sid2p localization to the division site and activity depend on the function of all of the other septation initiation genes: cdc7, cdc11, cdc14, sid1, spg1, and sid4. Thus, Sid2p, a component of the spindle pole body, by virtue of its transient localization to the division site, appears to determine the timing of ring constriction and septum delivery in response to activating signals from other Sid gene products.
authors.affiliation: Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA.
authors.forename: C A
authors.initials: CA
authors.lastname: Sparks
authors.forename: M
authors.initials: M
authors.lastname: Morphew
authors.forename: D
authors.initials: D
authors.lastname: McCollum
mesh_terms: D000199:Actins / Q000378:metabolism; D018797:Cell Cycle Proteins; D002455:Cell Division; D003599:Cytoskeleton / Q000378:metabolism; D004268:DNA-Binding Proteins; D004843:Epistasis, Genetic; D005656:Fungal Proteins / Q000235:genetics / Q000502:physiology; D005800:Genes, Fungal / Q000235:genetics / Q000502:physiology; D018816:Genes, cdc / Q000235:genetics / Q000502:physiology; D008870:Microtubules / Q000378:metabolism; D009154:Mutation; D011494:Protein Kinases / Q000235:genetics / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins; D012568:Schizosaccharomyces / Q000166:cytology* / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D029702:Schizosaccharomyces pombe Proteins; D015398:Signal Transduction; D008941:Spindle Apparatus / Q000378:metabolism*; D013696:Temperature; D013997:Time Factors
chemical_list: D000199:Actins; D018797:Cell Cycle Proteins; D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D011993:Recombinant Fusion Proteins; D029701:Saccharomyces cerevisiae Proteins; D029702:Schizosaccharomyces pombe Proteins; C499592:TAH11 protein, S cerevisiae; C406818:cdt1 protein, S pombe; D011494:Protein Kinases; C113816:Sid2 protein, S pombe; C085768:DBF2 protein, S cerevisiae; D017346:Protein Serine-Threonine Kinases