In the ΔAoatg15 mutant, autophagic bodies accumulated in vacuoles, PFT�� molecular weight suggesting that the uptake process proceeded. We therefore propose that the level of autophagy is closely correlated with the degree of differentiation in A. oryzae. In eukaryotes, macroautophagy (autophagy) is a conserved degradation process that mediates the trafficking of cytosolic proteins and organelles into lysosomes/vacuoles for bulk degradation (Reggiori & Klionsky, 2002). Although the process appears to predominantly recycle

macromolecules and aid cell survival during periods of nutritional starvation, autophagy is also involved in development and differentiation in numerous eukaryotes, including yeasts, plants, and

mammals, among others (Levine & Klionsky, 2004). This involvement may have resulted from the autophagic degradation of damaged organelles and cytosol for constitutive cell clearance and cellular remodeling during development and differentiation. The autophagic process proceeds sequentially through several steps, involving the induction of autophagy, formation of autophagosomes, fusion of autophagosomes to lysosomes/vacuoles, and degradation of autophagic bodies selleck chemicals llc (Mizushima, 2007; Pollack et al., 2009). In Saccharomyces cerevisiae, the induction of autophagy results from inactivation of the target of rapamycin (Tor) kinase, allowing formation of the Atg1 kinase complex composed of Atg1, Atg13, and Atg17 (Funakoshi et al., 1997; Kamada et al., 2000; Kabeya et al., 2005). The association of Atg13 with Atg1, which is essential for autophagy, is prevented by phosphorylation of Atg13 in a Tor kinase-dependent manner under conditions suitable for growth. In starvation conditions, Atg13 is dephosphorylated by inhibition of Tor kinase activity, allowing it to associate with Atg1 (Kamada Gefitinib purchase et al., 2000). The induction of autophagy induces the formation of cup-shaped isolation membranes, which subsequently

elongate and sequester cytosol and/or organelles within double-membrane vesicles termed autophagosomes. Saccharomyces cerevisiae Atg8 is a ubiquitin-like protein that is essential for the formation of autophagosomes and is localized in preautophagosomal structures (PAS) and the membranes of autophagosomes and autophagic bodies, and has been used as a marker for these organelles (Suzuki et al., 2001). A critical event for autophagy involves the conjugation of the carboxy (C)-terminal glycine of Atg8 with phosphatidylethanolamine (PE), which is mediated by a ubiquitination-like system composed of Atg4 (cysteine protease), Atg7 (E1-like protein), and Atg3 (E2-like protein) (Ichimura et al., 2000; Kirisako et al., 2000). Atg4 cleaves newly synthesized Atg8 to expose the C-terminal glycine for conjugation with PE, and also cleaves Atg8-conjugated PE (Atg8-PE) to recycle Atg8.