Timely Closure of the Prospore Membrane Requires SPS1 and SPO77 in Saccharomyces cerevisiae.
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.
['Paulissen|Scott M|SM|', 'Slubowski|Christian J|CJ|', 'Roesner|Joseph M|JM|', 'Huang|Linda S|LS|0000-0002-9033-4391']
D064173:Anaphase-Promoting Complex-Cyclosome D064199:Cdc20 Proteins D018797:Cell Cycle Proteins D002462:Cell Membrane D008540:Meiosis D046912:Multiprotein Complexes D010766:Phosphorylation D017346:Protein Serine-Threonine Kinases D055550:Protein Stability D021381:Protein Transport D059748:Proteolysis D012441:Saccharomyces cerevisiae D029701:Saccharomyces cerevisiae Proteins D013172:Spores, Fungal
prospore membrane sporulation germinal center kinase anaphase promoting complex cytokinesis meiotic exit