{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["19(12)"],"submitter":["Tian Y"],"pubmed_abstract":["Ataxin-2 is a protein containing a polyQ extension and intermediate length of polyQ extensions increases the risk of Amyotrophic Lateral Sclerosis (ALS). Down-regulation of Ataxin-2 has been shown to mitigate TDP-43 proteinopathy in ALS models. To identify alternative therapeutic targets that can mitigate TDP-43 toxicity, we examined the interaction between Ataxin-2 and TDP-43. Co-immunoprecipitation demonstrated that Ataxin-2 and TDP-43 interact, that their interaction is mediated through the RNA recognition motif (RRM) of TDP-43, and knocking down Ataxin-2 or mutating the RRM domains rescued TDP-43 toxicity in an iPSC-derived neuronal model with TDP-43 overexpression. To decipher the Ataxin-2 and TDP-43 interactome, we used co-immunoprecipitation followed by mass spectrometry to identify"],"journal":["PloS one"],"pagination":["e0308428"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11687654"],"repository":["biostudies-literature"],"pubmed_title":["Deciphering the interactome of Ataxin-2 and TDP-43 in iPSC-derived neurons for potential ALS targets."],"pmcid":["PMC11687654"],"pubmed_authors":["Heinsinger N","Lim UM","Hu Y","Klein B","Parmentier-Batteur S","Tian Y","Fernandis AZ","Wang Y","Uslaner JM","Smith SM"],"additional_accession":[]},"is_claimable":false,"name":"Deciphering the interactome of Ataxin-2 and TDP-43 in iPSC-derived neurons for potential ALS targets.","description":"Ataxin-2 is a protein containing a polyQ extension and intermediate length of polyQ extensions increases the risk of Amyotrophic Lateral Sclerosis (ALS). Down-regulation of Ataxin-2 has been shown to mitigate TDP-43 proteinopathy in ALS models. To identify alternative therapeutic targets that can mitigate TDP-43 toxicity, we examined the interaction between Ataxin-2 and TDP-43. Co-immunoprecipitation demonstrated that Ataxin-2 and TDP-43 interact, that their interaction is mediated through the RNA recognition motif (RRM) of TDP-43, and knocking down Ataxin-2 or mutating the RRM domains rescued TDP-43 toxicity in an iPSC-derived neuronal model with TDP-43 overexpression. To decipher the Ataxin-2 and TDP-43 interactome, we used co-immunoprecipitation followed by mass spectrometry to identify","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024","modification":"2026-06-01T21:55:58.12Z","creation":"2025-04-04T13:41:21.001Z"},"accession":"S-EPMC11687654","cross_references":{"pubmed":["39739690"],"doi":["10.1371/journal.pone.0308428"]}}