{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wang J"],"funding":["Natural Science Foundation of Henan Province","National Natural Science Foundation of China","Hainan Provincial Natural Science Foundation of China and Program for Science &amp; Technology Innovation Talents in Higher Education of Henan Province (23HASTIT050) Higher Education of Henan province"],"pagination":["1844-1862"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10262811"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["19(6)"],"pubmed_abstract":["<i>L. monocytogenes</i> is a widely used infection model for the research on pathogenesis and host defense against gram-positive intracellular bacteria. Emerging evidence indicates that posttranslational modifications play a critical role in the regulation of macroautophagy/autophagy. However, little is known about the posttranslational modifications of ATG7, the essential protein in the autophagy process. In this study, we demonstrated that the RING-type E3 ligase TRIM7/RNF90 positively regulated autophagosome accumulation by promoting the ubiquitination of ATG7 at K413, thereby affecting <i>L. monocytogenes</i> infection. TRIM7 expression was induced by a variety range of conditions, including starvation, rapamycin stimulation, and <i>L. monocytogenes</i> infection. TRIM7 deficiency in m"],"journal":["Autophagy"],"pubmed_title":["TRIM7/RNF90 promotes autophagy via regulation of ATG7 ubiquitination during <i>L. monocytogenes</i> infection."],"pmcid":["PMC10262811"],"funding_grant_id":["U1704183","and 32170871","212300410065","31970847","U2004103","32070949"],"pubmed_authors":["Ma S","Goren I","Qin X","Pei J","Yang B","Wang H","Wang J","Zhang Q","Liu Y","Huang Y","Xing H","Wang Y","Song Z"],"additional_accession":[]},"is_claimable":false,"name":"TRIM7/RNF90 promotes autophagy via regulation of ATG7 ubiquitination during <i>L. monocytogenes</i> infection.","description":"<i>L. monocytogenes</i> is a widely used infection model for the research on pathogenesis and host defense against gram-positive intracellular bacteria. Emerging evidence indicates that posttranslational modifications play a critical role in the regulation of macroautophagy/autophagy. However, little is known about the posttranslational modifications of ATG7, the essential protein in the autophagy process. In this study, we demonstrated that the RING-type E3 ligase TRIM7/RNF90 positively regulated autophagosome accumulation by promoting the ubiquitination of ATG7 at K413, thereby affecting <i>L. monocytogenes</i> infection. TRIM7 expression was induced by a variety range of conditions, including starvation, rapamycin stimulation, and <i>L. monocytogenes</i> infection. TRIM7 deficiency in m","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jun","modification":"2026-06-04T08:05:37.17Z","creation":"2025-04-21T15:12:21.833Z"},"accession":"S-EPMC10262811","cross_references":{"pubmed":["36576150"],"doi":["10.1080/15548627.2022.2162706"]}}