<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>17(11)</volume><submitter>Kacal M</submitter><funding>Vetenskapsrådet</funding><funding>Cancerfonden</funding><funding>Ragnar Söderbergs stiftelse</funding><pubmed_abstract>Autophagic pathways are regulated mechanisms that play important roles in lysosome-mediated cellular degradation. Yet, the contribution of different autophagic pathways in lysosomal targeting, and characterization of the extent and specificity in their degradome remains largely uncharacterized. By undertaking a multiplex quantitative mass spectrometry approach, we have previously analyzed the lysosomal proteome during chaperone-mediated autophagy (CMA)-stimulated conditions in cancer cells. Here, we have extended our multiplex quantitative mass spectrometry and bioinformatics analysis on the proteome from isolated lysosomes to gain a comprehensive view of the temporal enriched lysosomal content upon non-macroautophagy-activated conditions. In parallel, we describe the functional dependency</pubmed_abstract><journal>Autophagy</journal><pagination>3865-3874</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8632328</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Quantitative proteomic analysis of temporal lysosomal proteome and the impact of the KFERQ-like motif and LAMP2A in lysosomal targeting.</pubmed_title><pmcid>PMC8632328</pmcid><pubmed_authors>Hao Y</pubmed_authors><pubmed_authors>Norberg E</pubmed_authors><pubmed_authors>Vakifahmetoglu-Norberg H</pubmed_authors><pubmed_authors>Zhang B</pubmed_authors><pubmed_authors>Kacal M</pubmed_authors></additional><is_claimable>false</is_claimable><name>Quantitative proteomic analysis of temporal lysosomal proteome and the impact of the KFERQ-like motif and LAMP2A in lysosomal targeting.</name><description>Autophagic pathways are regulated mechanisms that play important roles in lysosome-mediated cellular degradation. Yet, the contribution of different autophagic pathways in lysosomal targeting, and characterization of the extent and specificity in their degradome remains largely uncharacterized. By undertaking a multiplex quantitative mass spectrometry approach, we have previously analyzed the lysosomal proteome during chaperone-mediated autophagy (CMA)-stimulated conditions in cancer cells. Here, we have extended our multiplex quantitative mass spectrometry and bioinformatics analysis on the proteome from isolated lysosomes to gain a comprehensive view of the temporal enriched lysosomal content upon non-macroautophagy-activated conditions. In parallel, we describe the functional dependency</description><dates><release>2021-01-01T00:00:00Z</release><publication>2021 Nov</publication><modification>2026-05-09T11:40:46.683Z</modification><creation>2022-02-11T14:19:39.222Z</creation></dates><accession>S-EPMC8632328</accession><cross_references><pubmed>33446043</pubmed><doi>10.1080/15548627.2021.1876343</doi></cross_references></HashMap>