Year: 2016
Type: article
Abstract: Selective autophagy mediates the degradation of various cargoes, including protein aggregates and organelles, thereby contributing to cellular homeostasis. Cargo receptors ensure selectivity by tethering specific cargo to lipidated Atg8 at the isolation membrane. However, little is known about the structural requirements underlying receptor-mediated cargo recognition. Here, we report structural, biochemical, and cell biological analysis of the major selective cargo protein in budding yeast, aminopeptidase I (Ape1), and its complex with the receptor Atg19. The Ape1 propeptide has a trimeric coiled-coil structure, which tethers dodecameric Ape1 bodies together to form large aggregates. Atg19 disassembles the propeptide trimer and forms a 2:1 heterotrimer, which not only blankets the Ape1 aggregates but also regulates their size. These receptor activities may promote elongation of the isolation membrane along the aggregate surface, enabling sequestration of the cargo with high specificity.
Source: Cell Reports
Language: English
Subfield: Epidemiology
Field: Medicine
Domain: Health Sciences
Open Access status: gold
Estimated APC paid: $5,620
Awards: G225566074, Molecular mechanisms of organelle biogenesis using autophagosome formation as a model system, Studies on RNA degradation by autophagy for cell survival during starvation, G5535307737, Elucidation of mechanisms that regulate target recognition in selective autophagy, G7615071395, Structural and functional analyses of autophagy essencial protein Atg9, Autophagy: Molecular mechanism and its integration into cell physiology
OpenAlex ID: W2440187019