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• W4213108827 abstract "Autophagy is a ubiquitous process, occurring in all eukaryotic cells. Microautophagy sequesters cytoplasm or organelles by invagination or septation of the vacuolar membrane. In Saccharomyces cerevisiae the piecemeal microautophagy of the nucleus (PMN) degrades nonessential portions of the nucleus. For the first time, this study uncovers the essential function of most of the ATG gene products during PMN. Especially the proteins necessary for the induction and the vesicle nucleation during autophagy are important for PMN. Most of these proteins form the pre-autophagosomal structure called PAS, the formation site of the autophagosomes. Furthermore there are some Cvt-specific proteins, which here are shown to be also needed during PMN. Scission of the PMN vesicles releases a tri-lamellar PMN-vesicle into the vacuolar lumen, whose outermost membrane is derived from portions of the vacuolar membrane and whose double bilayer comes from the ER, which in yeast also forms the nuclear envelope. PMN does not require the complete vacuole homotypic fusion genes. This leads to the conclusion that a spectrum of ATG genes is required for the terminal vacuole enclosure and fusion stages of PMN. The integral membrane protein Atg15p is a putative lipase essential for intravacuolar lysis of autophagic bodies. Atg15p reaches the vacuole via the MVB pathway. The generation of C- or N-terminally GFP-tagged Atg15p allows a direct localization of the protein in the ER and the lumen of the vacuole. Studies on C-terminally truncated versions of GFP-Atg15p may help to identify the putative catalytic triad residues. To test whether the localization of Atg15p to the MVB-vesicles is necessary for itsactivity, a fusion protein was generated that is localized at the vacuolar membrane(ALP-Atg15p). The expression of the chimeric protein disturbed the growth of the cells. Therefore an inactive form of the fusion protein was generated. The active serine residue in Atg15p was changed into an alanine. The resulting fusion protein lost its biological activity. The present study shows that the activity of ALP-Atg15p is independent of Proteinase A. Sna3p and Atg15p are transported in an ubiquitin-independent manner into the MVB pathway. Nevertheless the sorting of Sna3p is controlled by a PxY-motif leading to an interaction with the ubiqiutin ligase Rsp5p. Atg15p also contains a PxY-motif. This study shows that a mutation of the motif has no effect on the functionality of Atg15p but the protein seems to be mislocated within the cells." @default.
• W4213108827 created "2022-02-24" @default.
• W4213108827 creator A5031603879 @default.
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• W4213108827 date "2022-02-20" @default.
• W4213108827 modified "2023-09-27" @default.
• W4213108827 title "Mikroautophagischer Abbau von Teilen der Kernhülle und Untersuchungen zum Transport und der Aktivität von Atg15p in der Hefe Saccharomyces <i>cerevisiae</i>" @default.
• W4213108827 doi "https://doi.org/10.53846/goediss-3334" @default.
• W4213108827 hasPublicationYear "2022" @default.
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