Timely Closure of the Prospore Membrane Requires SPS1 and SPO77 in Saccharomyces cerevisiae

• Published in: Genetics (Austin) Vol. 203; no. 3; pp. 1203 - 1216
• Main Authors: Paulissen, Scott M, Slubowski, Christian J, Roesner, Joseph M, Huang, Linda S
• Format: Journal Article
• Language: English
• Published: United States Genetics Society of America 01.07.2016
• Subjects: Anaphase-Promoting Complex-Cyclosome - genetics; Cdc20 Proteins - genetics; Cdc20 Proteins - metabolism; Cell cycle; Cell Cycle Proteins - genetics; Cell Cycle Proteins - metabolism; Cell division; Cell Membrane - genetics; Cell Membrane - metabolism; Insects; Investigations; Localization; Meiosis - genetics; Membranes; Multiprotein Complexes - genetics; Multiprotein Complexes - metabolism; Phosphorylation; Protein Stability; Protein Transport - genetics; Protein-Serine-Threonine Kinases - genetics; Protein-Serine-Threonine Kinases - metabolism; Proteins; Proteolysis; Saccharomyces cerevisiae; Saccharomyces cerevisiae - genetics; Saccharomyces cerevisiae - metabolism; Saccharomyces cerevisiae Proteins - genetics; Saccharomyces cerevisiae Proteins - metabolism; Spores, Fungal - genetics; Spores, Fungal - metabolism; Yeast; anaphase promoting complex; prospore membrane; meiotic exit; germinal center kinase; cytokinesis; sporulation
• ISSN: 1943-2631; 0016-6731; 1943-2631
• DOI: 10.1534/genetics.115.183939

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.