{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hilverling A"],"funding":["Technische Universität Dresden","Deutsche Forschungsgemeinschaft"],"pagination":["155-171"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8732932"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["42(1)"],"pubmed_abstract":["Autophagosome maturation comprises fusion with lysosomes and acidification. It is a critical step in the degradation of cytosolic protein aggregates that characterize many neurodegenerative diseases. In order to better understand this process, we studied intracellular trafficking of autophagosomes and aggregates of α-synuclein, which characterize Parkinson's disease and other synucleinopathies. The autophagosomal marker LC3 and the aggregation prone A53T mutant of α-synuclein were tagged by fluorescent proteins and expressed in HEK293T cells and primary astrocytes. The subcellular distribution and movement of these vesicle populations were analyzed by (time-lapse) microscopy. Fusion with lysosomes was assayed using the lysosomal marker LAMP1; vesicles with neutral and acidic luminal pH wer"],"journal":["Cellular and molecular neurobiology"],"pubmed_title":["Maturing Autophagosomes are Transported Towards the Cell Periphery."],"pmcid":["PMC8732932"],"funding_grant_id":["FA-658/3-1"],"pubmed_authors":["Hilverling A","Szego EM","Cozma D","Dinter E","Saridaki T","Falkenburger BH"],"additional_accession":[]},"is_claimable":false,"name":"Maturing Autophagosomes are Transported Towards the Cell Periphery.","description":"Autophagosome maturation comprises fusion with lysosomes and acidification. It is a critical step in the degradation of cytosolic protein aggregates that characterize many neurodegenerative diseases. In order to better understand this process, we studied intracellular trafficking of autophagosomes and aggregates of α-synuclein, which characterize Parkinson's disease and other synucleinopathies. The autophagosomal marker LC3 and the aggregation prone A53T mutant of α-synuclein were tagged by fluorescent proteins and expressed in HEK293T cells and primary astrocytes. The subcellular distribution and movement of these vesicle populations were analyzed by (time-lapse) microscopy. Fusion with lysosomes was assayed using the lysosomal marker LAMP1; vesicles with neutral and acidic luminal pH wer","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Jan","modification":"2026-04-12T15:45:49.772Z","creation":"2022-02-11T15:23:43.118Z"},"accession":"S-EPMC8732932","cross_references":{"pubmed":["34106361"],"doi":["10.1007/s10571-021-01116-0"]}}