Proteomics

Dataset Information

0

Isolation and mass spectrometry analysis of Atg9 vesicles from Saccharomyces cerevisiae


ABSTRACT: Autophagy is a eukaryotic bulk degradation pathway that allows cells to degrade potentially harmful cytosolic components or to provide necessary nutrients during starvation. This cargo degradation is achieved by its sequestration within double membrane vesicles termed autophagosomes, which fuse with the vacuole where it is degraded. Atg (autophagy-related) proteins are the main group of proteins involved in this process and, interestingly, Atg9 is the only integral membrane yeast Atg protein absolutely required for autophagy progression. In the cell it resides in Golgi-derived vesicles, which are indispensable for the nucleation of the autophagosome. There is not much known about biochemical properties of these vesicles in particular their protein content apart from Atg9. To address this question and to identify putative interaction partners of Atg9, the Atg9-vesicles were isolated and submitted to mass spectrometry analysis.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Markus Hartl  

LAB HEAD: Sascha Martens

PROVIDER: PXD020359 | Pride | 2022-03-03

REPOSITORIES: Pride

altmetric image

Publications

Reconstitution of autophagosome nucleation defines Atg9 vesicles as seeds for membrane formation.

Sawa-Makarska Justyna J   Baumann Verena V   Coudevylle Nicolas N   von Bülow Sören S   Nogellova Veronika V   Abert Christine C   Schuschnig Martina M   Graef Martin M   Hummer Gerhard G   Martens Sascha S  

Science (New York, N.Y.) 20200901 6508


Autophagosomes form de novo in a manner that is incompletely understood. Particularly enigmatic are autophagy-related protein 9 (Atg9)-containing vesicles that are required for autophagy machinery assembly but do not supply the bulk of the autophagosomal membrane. In this study, we reconstituted autophagosome nucleation using recombinant components from yeast. We found that Atg9 proteoliposomes first recruited the phosphatidylinositol 3-phosphate kinase complex, followed by Atg21, the Atg2-Atg18  ...[more]

Similar Datasets

2023-03-30 | PXD040435 | Pride
2022-10-18 | PXD031787 | Pride
2021-09-20 | GSE184340 | GEO
2023-10-02 | E-MTAB-6539 | biostudies-arrayexpress
2019-11-04 | E-MTAB-8439 | biostudies-arrayexpress
2014-04-24 | E-GEOD-57031 | biostudies-arrayexpress
2022-12-14 | GSE220887 | GEO
2016-07-03 | E-GEOD-74475 | biostudies-arrayexpress
2016-07-03 | E-GEOD-74474 | biostudies-arrayexpress
2023-10-01 | E-MTAB-6517 | biostudies-arrayexpress