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• W2080691657 abstract "Autophagy is a primarily non-selective degradation system of cytoplasmic constituents in lysosomes/vacuoles during starvation. In yeast, autophagy is also involved in the selective transport of Ape1, a vacuolar hydrolase, as a biosynthetic route. Ald6, a soluble cytoplasmic enzyme, is preferentially eliminated from cytoplasm via autophagy. However, little is known about the mechanisms of Ald6 targeting to autophagosomes. Here, we show that Lap3, a soluble cytosolic cysteine protease, is spatially associated with Ape1 and selectively transported to the vacuole during nitrogen starvation. The rate of Lap3 transport is much higher than that of Ald6 and is similar to that of Ape1. Moreover, ATG11 and ATG19, essential factors for Ape1 transport, are important for Lap3 transport. Most Lap3 is degraded within a couple of hours in the vacuole in contrast to Ape1; therefore, we conclude that the machinery required for Ape1 biosynthesis is used for selective degradation of Lap3." @default.
• W2080691657 created "2016-06-24" @default.
• W2080691657 creator A5013361099 @default.
• W2080691657 creator A5056765809 @default.
• W2080691657 creator A5057021039 @default.
• W2080691657 date "2009-01-01" @default.
• W2080691657 modified "2023-10-15" @default.
• W2080691657 title "Lap3 is a selective target of autophagy in yeast, Saccharomyces cerevisiae" @default.
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• W2080691657 doi "https://doi.org/10.1016/j.bbrc.2008.11.084" @default.
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