Fungal Genomics & Biology
Open Access
ISSN: 2165-8056
ISSN: 2165-8056
Life Science Data Research Center, Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa, Chiba, Japan
Mini Review
How do Two Domains of Atg15 Work for Autophagosomal Membrane Degradation?
Author(s): Eri Hirata and Kuninori Suzuki*
During autophagy in Saccharomyces cerevisiae, cytosolic components are engulfed by double-membrane compartments
called autophagosomes, transported to the vacuole, and degraded there. The cytoplasm-to-vacuole targeting (Cvt)
pathway delivers the vacuolar hydrolase aminopeptidase I (Ape1) through double-membrane compartments termed
Cvt vesicles. These pathways share common mechanisms including the degradation of their compartments. The
outer membranes of autophagosomes and Cvt vesicles fuse with the vacuole membrane and inner membranebound
structures and, autophagic bodies and Cvt bodies, are released into the vacuole lumen. The membranes
of autophagic bodies and Cvt bodies are degraded by a vacuolar lipase, Atg15, to allow other vacuolar hydrolases
to access their cargoes for degradation. Atg15 is the only vacuolar lipase in S. cerevisiae and has .. View More»
DOI:
10.35841/2165-8056.22.12.188