{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["14(1)"],"submitter":["Turkki P"],"funding":["Academy of Finland","Syöpäsäätiö","Sigrid Juselius Foundation","Maud Kuistilan Muistosäätiö","Ella ja Georg Ehrnroothin Säätiö"],"pubmed_abstract":["Integrin adaptor proteins, like tensin-2, are crucial for cell adhesion and signaling. However, the function of tensin-2 beyond localizing to focal adhesions remain poorly understood. We utilized proximity-dependent biotinylation and Strep-tag affinity proteomics to identify interaction partners of tensin-2 in Flp-In 293 T-REx cells. Interactomics linked tensin-2 to known focal adhesion proteins and the dystrophin glycoprotein complex, while also uncovering novel interaction with the glycolytic enzyme GAPDH. We demonstrated that Y483-phosphorylation of tensin-2 regulates the glycolytic rate in Flp-In 293 T-REx and MEF cells and found that pY483 tensin-2 is enriched in adhesions in MEF cells. Our study unveils novel interaction partners for tensin-2 and further solidifies its speculated rol"],"journal":["Scientific reports"],"pagination":["19862"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11350193"],"repository":["biostudies-literature"],"pubmed_title":["Tensin-2 interactomics reveals interaction with GAPDH and a phosphorylation-mediated regulatory role in glycolysis."],"pmcid":["PMC11350193"],"pubmed_authors":["Turkki P","Chowdhury I","Varjosalo M","Ohman T","Hytonen VP","Azizi L"],"additional_accession":[]},"is_claimable":false,"name":"Tensin-2 interactomics reveals interaction with GAPDH and a phosphorylation-mediated regulatory role in glycolysis.","description":"Integrin adaptor proteins, like tensin-2, are crucial for cell adhesion and signaling. However, the function of tensin-2 beyond localizing to focal adhesions remain poorly understood. We utilized proximity-dependent biotinylation and Strep-tag affinity proteomics to identify interaction partners of tensin-2 in Flp-In 293 T-REx cells. Interactomics linked tensin-2 to known focal adhesion proteins and the dystrophin glycoprotein complex, while also uncovering novel interaction with the glycolytic enzyme GAPDH. We demonstrated that Y483-phosphorylation of tensin-2 regulates the glycolytic rate in Flp-In 293 T-REx and MEF cells and found that pY483 tensin-2 is enriched in adhesions in MEF cells. Our study unveils novel interaction partners for tensin-2 and further solidifies its speculated rol","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Aug","modification":"2026-06-03T05:10:23.853Z","creation":"2026-04-24T03:14:22.061Z"},"accession":"S-EPMC11350193","cross_references":{"pubmed":["39191795"],"doi":["10.1038/s41598-024-65787-7"]}}