biostudies-literatureMilano SNHHS | NIH | National Institute of General Medical SciencesFoundation for the National Institutes of HealthFoundation for the National Institutes of Health (FNIH)National Science Foundation (NSF)NIGMS NIH HHSHHS | NIH | National Institute of General Medical Sciences (NIGMS)National Science Foundation494-520https://www.ebi.ac.uk/biostudies/studies/S-EPMC11772875biostudies-literatureUnknown26(2)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), suggeEMBO reportsThe role of ER exit sites in maintaining P-body organization and integrity during Drosophila melanogaster oogenesis.PMC117728751SC1GM135132RO1-GM084947SC1 GM135132R01 GM0849471919829Milano SNBratu DPBayer LVCasella CEKo JJfalseThe role of ER exit sites in maintaining P-body organization and integrity during Drosophila melanogaster oogenesis.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), sugge2025-01-01T00:00:00Z2025 Jan2026-07-15T08:52:16.721Z2025-04-22T10:24:19.701ZS-EPMC117728753965385110.1038/s44319-024-00344-x