{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Qiu R"],"funding":["NIGMS NIH HHS"],"pagination":["1289-1301"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7353152"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["31(12)"],"pubmed_abstract":["The multi-component cytoplasmic dynein transports cellular cargoes with the help of another multi-component complex dynactin, but we do not know enough about factors that may affect the assembly and functions of these proteins. From a genetic screen for mutations affecting early-endosome distribution in <i>Aspergillus nidulans</i>, we identified the <i>prp40A</i><sup>L438*</sup> mutation in Prp40A, a homologue of Prp40, an essential RNA-splicing factor in the budding yeast. Prp40A is not essential for splicing, although it associates with the nuclear splicing machinery. The <i>prp40A</i><sup>L438*</sup> mutant is much healthier than the ∆<i>prp40A</i> mutant, but both mutants exhibit similar defects in dynein-mediated early-endosome transport and nuclear distribution. In the <i>prp40A</i><sup>L438*</sup> mutant, the frequency but not the speed of dynein-mediated early-endosome transport is decreased, which correlates with a decrease in the microtubule plus-end accumulations of dynein and dynactin. Within the dynactin complex, the actin-related protein Arp1 forms a mini-filament. In a pull-down assay, the amount of Arp1 pulled down with its pointed-end protein Arp11 is lowered in the <i>prp40A</i><sup>L438*</sup> mutant. In addition, we found from published interactome data that a mammalian Prp40 homologue PRPF40A interacts with Arp1. Thus, Prp40 homologues may regulate the assembly or function of dynein-dynactin and their mechanisms deserve to be further studied."],"journal":["Molecular biology of the cell"],"pubmed_title":["The splicing-factor Prp40 affects dynein-dynactin function in <i>Aspergillus nidulans</i>."],"pmcid":["PMC7353152"],"funding_grant_id":["R01 GM121850"],"pubmed_authors":["Zhang J","Qiu R","Xiang X"],"additional_accession":[]},"is_claimable":false,"name":"The splicing-factor Prp40 affects dynein-dynactin function in <i>Aspergillus nidulans</i>.","description":"The multi-component cytoplasmic dynein transports cellular cargoes with the help of another multi-component complex dynactin, but we do not know enough about factors that may affect the assembly and functions of these proteins. From a genetic screen for mutations affecting early-endosome distribution in <i>Aspergillus nidulans</i>, we identified the <i>prp40A</i><sup>L438*</sup> mutation in Prp40A, a homologue of Prp40, an essential RNA-splicing factor in the budding yeast. Prp40A is not essential for splicing, although it associates with the nuclear splicing machinery. The <i>prp40A</i><sup>L438*</sup> mutant is much healthier than the ∆<i>prp40A</i> mutant, but both mutants exhibit similar defects in dynein-mediated early-endosome transport and nuclear distribution. In the <i>prp40A</i><sup>L438*</sup> mutant, the frequency but not the speed of dynein-mediated early-endosome transport is decreased, which correlates with a decrease in the microtubule plus-end accumulations of dynein and dynactin. Within the dynactin complex, the actin-related protein Arp1 forms a mini-filament. In a pull-down assay, the amount of Arp1 pulled down with its pointed-end protein Arp11 is lowered in the <i>prp40A</i><sup>L438*</sup> mutant. In addition, we found from published interactome data that a mammalian Prp40 homologue PRPF40A interacts with Arp1. Thus, Prp40 homologues may regulate the assembly or function of dynein-dynactin and their mechanisms deserve to be further studied.","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Jun","modification":"2025-04-04T08:19:51.933Z","creation":"2025-04-04T08:19:51.933Z"},"accession":"S-EPMC7353152","cross_references":{"pubmed":["32267207"],"doi":["10.1091/mbc.E20-03-0166"]}}