{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Knyazeva A"],"funding":["Vetenskapsrådet (VR)","Goran Gustafsson Foundation for Research in Natural Sciences and Medicine","Vetenskapsrådet","European Research Council","Knut och Alice Wallenbergs Stiftelse","Knut och Alice Wallenbergs Stiftelse (Knut and Alice Wallenberg Foundation)"],"pagination":["e2317680121"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11047075"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["121(17)"],"pubmed_abstract":["The endosomal sorting complex required for transport (ESCRT) machinery constitutes multisubunit protein complexes that play an essential role in membrane remodeling and trafficking. ESCRTs regulate a wide array of cellular processes, including cytokinetic abscission, cargo sorting into multivesicular bodies (MVBs), membrane repair, and autophagy. Given the versatile functionality of ESCRTs, and the intricate organizational structure of the ESCRT machinery, the targeted modulation of distinct ESCRT complexes is considerably challenging. This study presents a pseudonatural product targeting IST1-CHMP1B within the ESCRT-III complexes. The compound specifically disrupts the interaction between IST1 and CHMP1B, thereby inhibiting the formation of IST1-CHMP1B copolymers essential for normal-topo"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["A chemical inhibitor of IST1-CHMP1B interaction impairs endosomal recycling and induces noncanonical LC3 lipidation."],"pmcid":["PMC11047075"],"funding_grant_id":["WAF2016","ChemBioAP","GG prize","2018-04585 2022-02932"],"pubmed_authors":["Carlson LA","Waldmann H","Shankar K","Singh B","Knyazeva A","Li S","Herzog LK","Zhang X","Corkery DP","Niggemeyer G","Gilthorpe JD","Gaetani M","Grill D","Wu YW"],"additional_accession":[]},"is_claimable":false,"name":"A chemical inhibitor of IST1-CHMP1B interaction impairs endosomal recycling and induces noncanonical LC3 lipidation.","description":"The endosomal sorting complex required for transport (ESCRT) machinery constitutes multisubunit protein complexes that play an essential role in membrane remodeling and trafficking. ESCRTs regulate a wide array of cellular processes, including cytokinetic abscission, cargo sorting into multivesicular bodies (MVBs), membrane repair, and autophagy. Given the versatile functionality of ESCRTs, and the intricate organizational structure of the ESCRT machinery, the targeted modulation of distinct ESCRT complexes is considerably challenging. This study presents a pseudonatural product targeting IST1-CHMP1B within the ESCRT-III complexes. The compound specifically disrupts the interaction between IST1 and CHMP1B, thereby inhibiting the formation of IST1-CHMP1B copolymers essential for normal-topo","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Apr","modification":"2026-07-15T04:04:24.368Z","creation":"2025-04-04T01:24:41.979Z"},"accession":"S-EPMC11047075","cross_references":{"pubmed":["38635626"],"doi":["10.1073/pnas.2317680121"]}}