<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Wang J</submitter><funding>Natural Science Foundation of Henan Province</funding><funding>National Natural Science Foundation of China</funding><funding>Hainan Provincial Natural Science Foundation of China and Program for Science &amp;amp; Technology Innovation Talents in Higher Education of Henan Province (23HASTIT050) Higher Education of Henan province</funding><pagination>1844-1862</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC10262811</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>19(6)</volume><pubmed_abstract>&lt;i>L. monocytogenes&lt;/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 &lt;i>L. monocytogenes&lt;/i> infection. TRIM7 expression was induced by a variety range of conditions, including starvation, rapamycin stimulation, and &lt;i>L. monocytogenes&lt;/i> infection. TRIM7 deficiency in m</pubmed_abstract><journal>Autophagy</journal><pubmed_title>TRIM7/RNF90 promotes autophagy via regulation of ATG7 ubiquitination during &lt;i>L. monocytogenes&lt;/i> infection.</pubmed_title><pmcid>PMC10262811</pmcid><funding_grant_id>U1704183</funding_grant_id><funding_grant_id>and 32170871</funding_grant_id><funding_grant_id>212300410065</funding_grant_id><funding_grant_id>31970847</funding_grant_id><funding_grant_id>U2004103</funding_grant_id><funding_grant_id>32070949</funding_grant_id><pubmed_authors>Ma S</pubmed_authors><pubmed_authors>Goren I</pubmed_authors><pubmed_authors>Qin X</pubmed_authors><pubmed_authors>Pei J</pubmed_authors><pubmed_authors>Yang B</pubmed_authors><pubmed_authors>Wang H</pubmed_authors><pubmed_authors>Wang J</pubmed_authors><pubmed_authors>Zhang Q</pubmed_authors><pubmed_authors>Liu Y</pubmed_authors><pubmed_authors>Huang Y</pubmed_authors><pubmed_authors>Xing H</pubmed_authors><pubmed_authors>Wang Y</pubmed_authors><pubmed_authors>Song Z</pubmed_authors></additional><is_claimable>false</is_claimable><name>TRIM7/RNF90 promotes autophagy via regulation of ATG7 ubiquitination during &lt;i>L. monocytogenes&lt;/i> infection.</name><description>&lt;i>L. monocytogenes&lt;/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 &lt;i>L. monocytogenes&lt;/i> infection. TRIM7 expression was induced by a variety range of conditions, including starvation, rapamycin stimulation, and &lt;i>L. monocytogenes&lt;/i> infection. TRIM7 deficiency in m</description><dates><release>2023-01-01T00:00:00Z</release><publication>2023 Jun</publication><modification>2026-06-04T08:05:37.17Z</modification><creation>2025-04-21T15:12:21.833Z</creation></dates><accession>S-EPMC10262811</accession><cross_references><pubmed>36576150</pubmed><doi>10.1080/15548627.2022.2162706</doi></cross_references></HashMap>