{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Milano SN"],"funding":["HHS | NIH | National Institute of General Medical Sciences","Foundation for the National Institutes of Health","Foundation for the National Institutes of Health (FNIH)","National Science Foundation (NSF)","NIGMS NIH HHS","HHS | NIH | National Institute of General Medical Sciences (NIGMS)","National Science Foundation"],"pagination":["494-520"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11772875"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["26(2)"],"pubmed_abstract":["Processing bodies (P-bodies) are cytoplasmic membrane-less organelles which host multiple mRNA processing events. While the fundamental principles of P-body organization are beginning to be elucidated in vitro, a nuanced understanding of how their assembly is regulated in vivo remains elusive. Here, we investigate the potential link between ER exit sites and P-bodies in Drosophila melanogaster egg chambers. Employing a combination of live and super-resolution imaging, we find that P-bodies associated with ER exit sites are larger and less mobile than cytoplasmic P-bodies, indicating that they constitute a distinct class of P-bodies. Moreover, we demonstrate that altering the composition of ER exit sites has differential effects on core P-body proteins (Me31B, Cup, and Trailer Hitch), sugge"],"journal":["EMBO reports"],"pubmed_title":["The role of ER exit sites in maintaining P-body organization and integrity during Drosophila melanogaster oogenesis."],"pmcid":["PMC11772875"],"funding_grant_id":["1SC1GM135132","RO1-GM084947","SC1 GM135132","R01 GM084947","1919829"],"pubmed_authors":["Milano SN","Bratu DP","Bayer LV","Casella CE","Ko JJ"],"additional_accession":[]},"is_claimable":false,"name":"The role of ER exit sites in maintaining P-body organization and integrity during Drosophila melanogaster oogenesis.","description":"Processing bodies (P-bodies) are cytoplasmic membrane-less organelles which host multiple mRNA processing events. While the fundamental principles of P-body organization are beginning to be elucidated in vitro, a nuanced understanding of how their assembly is regulated in vivo remains elusive. Here, we investigate the potential link between ER exit sites and P-bodies in Drosophila melanogaster egg chambers. Employing a combination of live and super-resolution imaging, we find that P-bodies associated with ER exit sites are larger and less mobile than cytoplasmic P-bodies, indicating that they constitute a distinct class of P-bodies. Moreover, we demonstrate that altering the composition of ER exit sites has differential effects on core P-body proteins (Me31B, Cup, and Trailer Hitch), sugge","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jan","modification":"2026-07-15T08:52:16.721Z","creation":"2025-04-22T10:24:19.701Z"},"accession":"S-EPMC11772875","cross_references":{"pubmed":["39653851"],"doi":["10.1038/s44319-024-00344-x"]}}