<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Hilverling A</submitter><funding>Technische Universität Dresden</funding><funding>Deutsche Forschungsgemeinschaft</funding><pagination>155-171</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8732932</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>42(1)</volume><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</pubmed_abstract><journal>Cellular and molecular neurobiology</journal><pubmed_title>Maturing Autophagosomes are Transported Towards the Cell Periphery.</pubmed_title><pmcid>PMC8732932</pmcid><funding_grant_id>FA-658/3-1</funding_grant_id><pubmed_authors>Hilverling A</pubmed_authors><pubmed_authors>Szego EM</pubmed_authors><pubmed_authors>Cozma D</pubmed_authors><pubmed_authors>Dinter E</pubmed_authors><pubmed_authors>Saridaki T</pubmed_authors><pubmed_authors>Falkenburger BH</pubmed_authors></additional><is_claimable>false</is_claimable><name>Maturing Autophagosomes are Transported Towards the Cell Periphery.</name><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</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Jan</publication><modification>2026-04-12T15:45:49.772Z</modification><creation>2022-02-11T15:23:43.118Z</creation></dates><accession>S-EPMC8732932</accession><cross_references><pubmed>34106361</pubmed><doi>10.1007/s10571-021-01116-0</doi></cross_references></HashMap>