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ProteomicsA Lysosome membrane regeneration pathway depends on TBC1D15 and autophagic lysosomal reformation proteins
Acute lysosomal membrane damage reduces the cellular population of functional lysosomes. However, these damaged lysosomes have a remarkable recovery potential independent of lysosomal biogenesis and remain unaffected in TFEB/TFE3-depleted cells. We combined proximity labelling based proteomics, bioc...
ORGANISM(S): Homo sapiens (Human) 
2023-03-07 | PXD040191 | Pride
Autophagy Lysosomal regeneration Lysosomes Autophagic lysosomal reformation Tbc family of proteins 
ProteomicsFamotidine targets Toll-like receptor 3 signaling in SARS-CoV2 infection
Caco2 cells were pretreated with 100µM histamine and 50µM Famotidine for 12h followed by infection with SARS-CoV2 for 24h. After that proteome was analysed.
ORGANISM(S): Homo sapiens (Human) 
2022-02-17 | PXD025703 | Pride
Famotidine Sars-cov2 Toll-like receptor Histamine Anti-viral signaling 
ProteomicsThe Aryl hydrocarbon receptor and FOS mediated cytotoxicity induced by Acenatobacter baumannii
Acinetobacter baumannii is a highly pathogenic and multidrug-resistant Gram-negative bacterium that causes severe nosocomial infections. To better understand the mechanism of pathogenesis, we compare the proteomes of uninfected and infected human cells, revealing that transcription factor FOS is the...
ORGANISM(S): Homo sapiens (Human) 
2024-08-05 | PXD053768 | Pride
Omv Proteome A549 Acenatobacter baumannii 
ProteomicsRufy4 exists as two translationally regulated isoforms, that localize to the mitochondrion in activated macrophages
We report here that RUFY4, a newly characterized member of the "RUN and FYVE domain-containing" family of proteins previously associated with autophagy enhancement, is highly expressed in alveolar macrophages (AM). We show that RUFY4 interacts with mitochondria upon stimulation by microbial-associat...
ORGANISM(S): Homo sapiens (Human) 
2022-02-17 | PXD026728 | Pride
Lps Mitophagy Rufy4 Alveolar macrophages Skp 
ProteomicsSerine ubiquitination of SNAREs generates bacterial vacuoles and prevents their lysosomal fusion
Here we show that Legionella SidE effectors mediate phosphoribosyl-linked serine ubiquitination (PR-Ub) of the autophagic SNARE proteins STX17 and SNAP29. On the one hand, PR-Ub modification of STX17 enhances its interaction with ATG14L, which drives the recruitment of ER membranes to the bacterial ...
ORGANISM(S): Homo sapiens (Human) 
2025-05-14 | PXD058184 | Pride
Legionella pneumophila Xenophagy Syntaxin17 Ubiquitin Autophagy 
UnknownPhosphoribosyl ubiquitination of SNARE proteins regulates autophagy during Legionella infection
Not available
S-SCDT-10_1038-S44318-025-00483-4 | biostudies-other
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