{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["27(3)"],"submitter":["Pang JD"],"funding":["National Natural Science Foundation of China"],"pubmed_abstract":["<i>Trichinella spiralis</i> infection is associated with the formation of cysts within host skeletal muscle cells, thereby enabling immune evasion and subsequent growth and development; however, the pathogenic factors involved in this process and their mechanisms remain elusive. Here, we found that <i>Ts</i>-RNF secreted by <i>T. spiralis</i> is required for its growth and development in host cells. Further study revealed that <i>Ts</i>-RNF functions as an E3 ubiquitin ligase that targets the UBA domain of SQSTM1/p62 by forming K63-type ubiquitin chains. This modification interferes with autophagic flux, leading to impaired mitochondrial clearance and abnormal myotube differentiation and fusion. Our results established that <i>T. spiralis</i> increases its escape by interfering with host a"],"journal":["iScience"],"pagination":["109102"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10877949"],"repository":["biostudies-literature"],"pubmed_title":["<i>Trichinella spiralis</i> inhibits myoblast differentiation by targeting SQSTM1/p62 with a secreted E3 ubiquitin ligase."],"pmcid":["PMC10877949"],"pubmed_authors":["Liu Y","Liu XL","Xu N","Dong ZJ","Pang JD","Jin XM","Boireau P","Liu MY","Vallee I","Ding J"],"additional_accession":[]},"is_claimable":false,"name":"<i>Trichinella spiralis</i> inhibits myoblast differentiation by targeting SQSTM1/p62 with a secreted E3 ubiquitin ligase.","description":"<i>Trichinella spiralis</i> infection is associated with the formation of cysts within host skeletal muscle cells, thereby enabling immune evasion and subsequent growth and development; however, the pathogenic factors involved in this process and their mechanisms remain elusive. Here, we found that <i>Ts</i>-RNF secreted by <i>T. spiralis</i> is required for its growth and development in host cells. Further study revealed that <i>Ts</i>-RNF functions as an E3 ubiquitin ligase that targets the UBA domain of SQSTM1/p62 by forming K63-type ubiquitin chains. This modification interferes with autophagic flux, leading to impaired mitochondrial clearance and abnormal myotube differentiation and fusion. Our results established that <i>T. spiralis</i> increases its escape by interfering with host a","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Mar","modification":"2026-06-18T06:53:26.904Z","creation":"2025-04-19T07:35:51.077Z"},"accession":"S-EPMC10877949","cross_references":{"pubmed":["38380253"],"doi":["10.1016/j.isci.2024.109102"]}}