<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>9(4)</volume><submitter>He Z</submitter><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</pubmed_abstract><journal>PloS one</journal><pagination>e94134</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3979746</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Cytoplasmic retention of a nucleocytoplasmic protein TBC1D3 by microtubule network is required for enhanced EGFR signaling.</pubmed_title><pmcid>PMC3979746</pmcid><pubmed_authors>Wan Q</pubmed_authors><pubmed_authors>Wang C</pubmed_authors><pubmed_authors>Wan M</pubmed_authors><pubmed_authors>Shen C</pubmed_authors><pubmed_authors>Shen H</pubmed_authors><pubmed_authors>Wu H</pubmed_authors><pubmed_authors>Zhao L</pubmed_authors><pubmed_authors>Bu X</pubmed_authors><pubmed_authors>He Z</pubmed_authors><pubmed_authors>Zhang Y</pubmed_authors><pubmed_authors>Tian T</pubmed_authors><pubmed_authors>Guo D</pubmed_authors><pubmed_authors>Chen Y</pubmed_authors><pubmed_authors>Zhao H</pubmed_authors></additional><is_claimable>false</is_claimable><name>Cytoplasmic retention of a nucleocytoplasmic protein TBC1D3 by microtubule network is required for enhanced EGFR signaling.</name><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</description><dates><release>2014-01-01T00:00:00Z</release><publication>2014</publication><modification>2025-04-04T21:40:12.626Z</modification><creation>2019-03-26T23:24:22Z</creation></dates><accession>S-EPMC3979746</accession><cross_references><pubmed>24714105</pubmed><doi>10.1371/journal.pone.0094134</doi></cross_references></HashMap>