TRIP10 (thyroid hormone receptor interactor 10) is a multi-domain scaffolding protein that plays critical roles in actin cytoskeleton organization and membrane dynamics. The protein contains FCH, FBH, HR1, and SH3 domains that facilitate interactions with microtubules, Rho family proteins (particularly CDC42), and WASP family proteins 1. TRIP10 functions in endocytosis by coordinating membrane tubulation with actin reorganization and is required for podosome formation in monocyte-derived cells 2. In glucose metabolism, TRIP10 serves as a target of miR-4431, and its downregulation impairs glucose uptake and insulin sensitivity 3. The protein exhibits context-dependent roles in cancer, functioning as either a tumor suppressor or promoter depending on cell type 4. TRIP10 is subject to epigenetic regulation through DNA methylation, which controls its expression during mesenchymal stem cell differentiation 5 and serves as a biomarker for predicting chemotherapy response in triple-negative breast cancer 6. At epithelial junctions, TRIP10 interacts with VAV2 to regulate E-cadherin levels and junction stability 2, highlighting its importance in maintaining epithelial integrity and cellular adhesion.