Abstract
Selective Transport of α-Mannosidase by Autophagic Pathways: STRUCTURAL BASIS FOR CARGO RECOGNITION BY Atg19 AND Atg34
Highlights
In the yeast Saccharomyces cerevisiae, a precursor form of aminopeptidase I and ␣-mannosidase (Ams1) are selectively transported to the vacuole through the cytoplasm-tovacuole targeting pathway under vegetative conditions and through autophagy under starvation conditions
In vitro pulldown assays showed that the C-terminal domains of both Atg19 and Atg34 are responsible for Ams1 binding; these domains are hereafter referred to as Ams1-binding domains (ABDs)
Atg11 interacts with Atg19 to recruit the cytoplasm-to-vacuole targeting (Cvt) complex to the preautophagosomal structure, the functional entity involved in Cvt vesicle formation [15,16,17]
Summary
Ams1, ␣-mannosidase; ABD, ␣-mannosidasebinding domain; Ape, aminopeptidase I; Cvt, cytoplasm-to-vacuole targeting; HSQC, heteronuclear single quantum correlation; prApe, precursor form of aminopeptidase I; SD, synthetic defined; TOCSY, total correlation spectroscopy. In vivo studies showed that a histidine residue conserved in the Atg and Atg ABDs is critical for Ams delivery to the vacuole. These structures provide a basis for elucidating the molecular mechanism of cargo recognition during selective autophagy
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