The Budding Yeast Cdc48Shp1 Complex Promotes Cell Cycle Progression by Positive Regulation of Protein Phosphatase 1 (Glc7)

• DOI: 10.1371/journal.pone.0056486
• Publication Date: 2013-02-13T22:07:00Z
• Authors: Stefanie Böhm; Alexander Buchberger
• Keywords: 0301 basic medicine; Saccharomyces cerevisiae Proteins; ddc:540; Science; Green Fluorescent Proteins; Mitosis; Cell Cycle Proteins; Saccharomyces cerevisiae; Protein Serine-Threonine Kinases; 03 medical and health sciences; Aurora Kinases; Valosin Containing Protein; Protein Phosphatase 1; Phosphorylation; Adenosine Triphosphatases; Cell Nucleus; Q; Cell Cycle; R; Intracellular Signaling Peptides and Proteins; Microscopy, Fluorescence; Multiprotein Complexes; Mutation; Medicine; Microtubule-Associated Proteins; Cell Division; Research Article; Protein Binding

The conserved, ubiquitin-selective AAA ATPase Cdc48 regulates numerous cellular processes including protein quality control, DNA repair and the cell cycle. function is tightly controlled by a multitude of cofactors mediating substrate specificity processing. UBX domain Shp1 bona fide substrate-recruiting cofactor in budding yeast S. cerevisiae. Even though has been proposed to be positive regulator Glc7, catalytic subunit phosphatase 1 cerevisiae, its functions complex with remain largely unknown. Here we show that deletion SHP1 gene results severe growth defects cycle delay at metaphase anaphase transition caused reduced Glc7 activity. Using an engineered binding-deficient variant Shp1, establish Cdc48Shp1 as critical mitotic We demonstrate shp1 mutants possess perturbed balance Ipl1 (Aurora B) kinase activities hyper-phosphorylation kinetochore Dam1, key Ipl1, defect shp1. also for first time physical interaction between vivo. Whereas loss does not significantly affect levels or localization, it causes binding activator Glc8 Glc7. Our data suggest controls activity regulating possibly further regulatory subunits.