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PP2A phosphatase regulates autophagy in budding yeast
Author(s) -
Talukdar Muhammad,
Akter Mst,
Kondo Akihiro,
Ushimaru Takashi
Publication year - 2015
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.29.1_supplement.724.15
Subject(s) - autophagy , autophagy related protein 13 , microbiology and biotechnology , protein phosphatase 2 , bag3 , saccharomyces cerevisiae , biology , phosphatase , kinase , protein kinase a , phosphorylation , biochemistry , protein phosphorylation , yeast , apoptosis
Autophagy is a highly conserved, degradative process in eukaryotic cells. It maintains homeostasis by degradation of damaged or unnecessary proteins and intracellular organelles, and supplied nutrients as degraded products. Dysfunction of autophagy leads to cellular disorder, such as cancer and neurodegenerative diseases including Alzheimer's, Parkinson's and Huntington's diseases. In budding yeast Saccharomyces cerevisiae, TORC1 phosphorylates Atg13 to prevent complex formation between Atg13 and other ATG proteins including the protein kinase Atg1. When TORC1 is inactivated by nutrient depletion, Atg13 is rapidly dephosphorylated and forms the Atg1‐13‐17‐29‐31 complex that triggers autophagy. In addition, protein kinase A (PKA) is involved in autophagy. Thus, various protein kinases involve in autophagy regulation are discovered, whereas protein phosphatases (PPs) involved autophagy are largely unknown. To find out protein phosphatases involved autophagy regulation, we assessed various autophagy profiles in 36 budding yeast PP‐knockout mutants and found that cells lacking PP2A are defective in autophagy and assembly of the pre‐autophagosomal structure (PAS). This study reveals that PP2A promotes autophagy after TORC1 inactivation.