{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["9(4)"],"submitter":["He Z"],"pubmed_abstract":["The hominoid oncogene TBC1D3 enhances epidermal growth factor receptor (EGFR) signaling and induces cell transformation. However, little is known regarding its spatio-temporal regulation and mechanism of tumorigenesis. In the current study, we identified the microtubule subunit β-tubulin as a potential interaction partner for TBC1D3 using affinity purification combined with mass spectrometry analysis. The interaction between TBC1D3 and β-tubulin was confirmed by co-immunoprecipitation. Using the same method, we also revealed that TBC1D3 co-precipitated with endogenous α-tubulin, another subunit of the microtubule. In agreement with these results, microtubule cosedimentation assays showed that TBC1D3 associated with the microtubule network. The β-tubulin-interacting site of TBC1D3 was mappe"],"journal":["PloS one"],"pagination":["e94134"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3979746"],"repository":["biostudies-literature"],"pubmed_title":["Cytoplasmic retention of a nucleocytoplasmic protein TBC1D3 by microtubule network is required for enhanced EGFR signaling."],"pmcid":["PMC3979746"],"pubmed_authors":["Wan Q","Wang C","Wan M","Shen C","Shen H","Wu H","Zhao L","Bu X","He Z","Zhang Y","Tian T","Guo D","Chen Y","Zhao H"],"additional_accession":[]},"is_claimable":false,"name":"Cytoplasmic retention of a nucleocytoplasmic protein TBC1D3 by microtubule network is required for enhanced EGFR signaling.","description":"The hominoid oncogene TBC1D3 enhances epidermal growth factor receptor (EGFR) signaling and induces cell transformation. However, little is known regarding its spatio-temporal regulation and mechanism of tumorigenesis. In the current study, we identified the microtubule subunit β-tubulin as a potential interaction partner for TBC1D3 using affinity purification combined with mass spectrometry analysis. The interaction between TBC1D3 and β-tubulin was confirmed by co-immunoprecipitation. Using the same method, we also revealed that TBC1D3 co-precipitated with endogenous α-tubulin, another subunit of the microtubule. In agreement with these results, microtubule cosedimentation assays showed that TBC1D3 associated with the microtubule network. The β-tubulin-interacting site of TBC1D3 was mappe","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014","modification":"2025-04-04T21:40:12.626Z","creation":"2019-03-26T23:24:22Z"},"accession":"S-EPMC3979746","cross_references":{"pubmed":["24714105"],"doi":["10.1371/journal.pone.0094134"]}}