{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,2]],"date-time":"2026-07-02T22:32:47Z","timestamp":1783031567930,"version":"3.54.6"},"reference-count":66,"publisher":"Wiley","license":[{"start":{"date-parts":[[2026,6,16]],"date-time":"2026-06-16T00:00:00Z","timestamp":1781568000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2026,6,16]],"date-time":"2026-06-16T00:00:00Z","timestamp":1781568000000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/100013465","name":"French Muscular Dystrophy Association","doi-asserted-by":"publisher","award":["23115"],"award-info":[{"award-number":["23115"]}],"id":[{"id":"10.13039\/100013465","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100020931","name":"Central European Research Infrastructure Consortium","doi-asserted-by":"publisher","award":["20242056"],"award-info":[{"award-number":["20242056"]}],"id":[{"id":"10.13039\/100020931","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004710","name":"Fondazione Umberto Veronesi","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004710","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100018694","name":"HORIZON EUROPE Marie Sklodowska-Curie Actions","doi-asserted-by":"publisher","award":["813599"],"award-info":[{"award-number":["813599"]}],"id":[{"id":"10.13039\/100018694","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"abstract":"<jats:p>\n                    Mutations in\n                    <jats:italic>TRIM32<\/jats:italic>\n                    cause limb\u2010girdle muscular dystrophy recessive 8 (LGMDR8), a neuromuscular disorder primarily affecting the proximal muscles of hips and shoulders. However, the precise pathogenic mechanism remains unclear. In this study, we used\n                    <jats:italic>Trim32<\/jats:italic>\n                    knock\u2010out C2C12 murine myoblasts to investigate the impact of full\n                    <jats:italic>Trim32<\/jats:italic>\n                    loss along the myogenesis process. We found that\n                    <jats:italic>Trim32<\/jats:italic>\n                    deficiency alters global transcriptomics already in the early phases of the differentiation process leading to impaired myogenic signaling, ultimately resulting in delayed and abnormal myotube formation. Following this up, we discovered that lack of Trim32 disrupts the transition from proliferation to differentiation by limiting the necessary downregulation of the proto\u2010oncogene c\u2010Myc, thus delaying and altering the immediate early onset of differentiation. Interestingly, unlike previous reports that emphasized protein\u2010level regulation, our data reveal that, at this precise stage of differentiation, Trim32 regulates the stability of c\u2010Myc at mRNA level. Attenuating c\u2010Myc expression level is able to partially recover the myogenesis defects observed in the absence of Trim32, suggesting that the Trim32\u2013c\u2010Myc axis may represent an essential hub, although likely not the exclusive mechanism, in muscle regeneration within LGMDR8 pathogenesis.\n                  <\/jats:p>","DOI":"10.1111\/febs.70619","type":"journal-article","created":{"date-parts":[[2026,6,16]],"date-time":"2026-06-16T13:16:17Z","timestamp":1781615777000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["<scp>TRIM32<\/scp>\n                    controls timely cell cycle exit in muscular differentiation through downregulation of c\u2010Myc\n                    <scp>mRNA<\/scp>"],"prefix":"10.1111","author":[{"given":"Lu","family":"Xiong","sequence":"first","affiliation":[{"name":"Department of Life Sciences University of Trieste  Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elisa","family":"Lazzari","sequence":"additional","affiliation":[{"name":"Department of Life Sciences University of Trieste  Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sabrina","family":"Pacor","sequence":"additional","affiliation":[{"name":"Department of Life Sciences University of Trieste  Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Simeone","family":"Dal Monego","sequence":"additional","affiliation":[{"name":"AREA Science Park  Trieste Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Erica","family":"Piovesan","sequence":"additional","affiliation":[{"name":"Department of Life Sciences University of Trieste  Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Danilo","family":"Licastro","sequence":"additional","affiliation":[{"name":"AREA Science Park  Trieste Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2531-114X","authenticated-orcid":false,"given":"Germana","family":"Meroni","sequence":"additional","affiliation":[{"name":"Department of Life Sciences University of Trieste  Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,6,16]]},"reference":[{"key":"e_1_2_10_2_1","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1006\/viro.1995.1266","article-title":"Identification of a novel human zinc finger protein that specifically interacts with the activation domain of lentiviral tat proteins","volume":"209","author":"Fridell RA","year":"1995","journal-title":"Virology"},{"key":"e_1_2_10_3_1","doi-asserted-by":"crossref","first-page":"2140","DOI":"10.1093\/emboj\/20.9.2140","article-title":"The tripartite motif family identifies cell compartments","volume":"20","author":"Reymond A","year":"2001","journal-title":"EMBO 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dystrophy 2H","volume":"8","author":"Lazzari E","year":"2019","journal-title":"Cells"},{"key":"e_1_2_10_8_1","doi-asserted-by":"crossref","first-page":"1204","DOI":"10.15252\/embj.201593741","article-title":"Functional role of TRIM E3 ligase oligomerization and regulation of catalytic activity","volume":"35","author":"Koliopoulos MG","year":"2016","journal-title":"EMBO J"},{"key":"e_1_2_10_9_1","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.semcdb.2015.10.017","article-title":"TRIM\u2010NHL proteins in development and disease","volume":"47","author":"Tocchini C","year":"2015","journal-title":"Semin Cell Dev Biol"},{"key":"e_1_2_10_10_1","doi-asserted-by":"crossref","first-page":"1549","DOI":"10.1038\/s41467-018-03920-7","article-title":"Evolutionary plasticity of the NHL domain underlies distinct solutions to RNA recognition","volume":"9","author":"Kumari P","year":"2018","journal-title":"Nat 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