The Greatwall-Endosulfine switch accelerates autophagic flux during the cell divisions leading to G1 arrest and quiescence in fission yeast

In fission yeast cell cycle exit, autophagy, G1 arrest and entry into quiescence are coordinated by the activity of the protein phosphatase PP2A/B55 through the Greatwall-Endosulfine switch. In order to study the role of this pathway in the transcriptional changes that occur during entry into quiescence, RNA was extracted from wild-type cells and from four mutant strains at three time points. We performed a comparative gene expression profiling analysis of RNA-seq data between wild type cells growing in minimal medium (MM) and the mutants igo1∆, ppk18∆ cek1∆ and nmt1:GFP:ppk18+ and in minimal medium lacking nitrogen (MM-N) after 1 and 4 hours between wild type cells and the mutants igo1∆ and ppk18∆ cek1∆.