title: Timely Closure of the Prospore Membrane Requires SPS1 and SPO77 in Saccharomyces cerevisiae.
abstract: During sporulation in Saccharomyces cerevisiae, a double lipid bilayer called the prospore membrane is formed de novo, growing around each meiotic nucleus and ultimately closing to create four new cells within the mother cell. Here we show that SPS1, which encodes a kinase belonging to the germinal center kinase III family, is involved in prospore membrane development and is required for prospore membrane closure. We find that SPS1 genetically interacts with SPO77 and see that loss of either gene disrupts prospore membrane closure in a similar fashion. Specifically, cells lacking SPS1 and SPO77 produce hyperelongated prospore membranes from which the leading edge protein complex is not removed from the prospore membrane in a timely fashion. The SPS1/SPO77 pathway is required for the proper phosphorylation and stability of Ssp1, a member of the leading edge protein complex that is removed and degraded when the prospore membrane closes. Genetic dissection of prospore membrane closure finds SPS1 and SPO77 act in parallel to a previously described pathway of prospore membrane closure that involves AMA1, an activator of the meiotic anaphase promoting complex.
authors.affiliation: Department of Biology, University of Massachusetts, Boston, Massachusetts 02125.
authors.forename: Scott M
authors.initials: SM
authors.lastname: Paulissen
authors.affiliation: Department of Biology, University of Massachusetts, Boston, Massachusetts 02125.
authors.forename: Christian J
authors.initials: CJ
authors.lastname: Slubowski
authors.affiliation: Department of Biology, University of Massachusetts, Boston, Massachusetts 02125.
authors.forename: Joseph M
authors.initials: JM
authors.lastname: Roesner
authors.affiliation: Department of Biology, University of Massachusetts, Boston, Massachusetts 02125 linda.huang@umb.edu.
authors.forename: Linda S
authors.identifier: 0000-0002-9033-4391
authors.initials: LS
authors.lastname: Huang
mesh_terms: D064173:Anaphase-Promoting Complex-Cyclosome / Q000235:genetics; D064199:Cdc20 Proteins / Q000235:genetics* / Q000378:metabolism; D018797:Cell Cycle Proteins / Q000235:genetics* / Q000378:metabolism; D002462:Cell Membrane / Q000235:genetics / Q000378:metabolism; D008540:Meiosis / Q000235:genetics; D046912:Multiprotein Complexes / Q000235:genetics / Q000378:metabolism; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000235:genetics* / Q000378:metabolism; D055550:Protein Stability; D021381:Protein Transport / Q000235:genetics; D059748:Proteolysis; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics* / Q000378:metabolism; D013172:Spores, Fungal / Q000235:genetics* / Q000378:metabolism
chemical_list: C577515:Ama1 protein, S cerevisiae; D064199:Cdc20 Proteins; D018797:Cell Cycle Proteins; D046912:Multiprotein Complexes; C000619231:SPO77 protein, S cerevisiae; C051095:SSP1 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D064173:Anaphase-Promoting Complex-Cyclosome; D017346:Protein Serine-Threonine Kinases; C505365:Sps1 protein, S cerevisiae
keywords: anaphase promoting complex; cytokinesis; germinal center kinase; meiotic exit; prospore membrane; sporulation