Trans-Golgi network integral membrane protein 2 (TGOLN2) is a heterodimeric type I integral membrane protein. It has a highly conserved N terminus which consists of a signal peptide. The C terminus comprises part of the lumenal domain, a membrane spanning region and cytoplasmic tail.
Trans-Golgi network integral membrane protein 2 (TGOLN2) cycles between the trans-Golgi network (TGN) and the cell surface via an early endosomal compartment. This movement is mediated by a tyrosine-based tetra peptide signal (SDYQRL) in the cytoplasmic domain. It plays an important role in the formation of exocytic vesicles at the TGN by functioning as a receptor for complexes of a cytoplasmic protein known as p62 and one GTP-binding protein. The cytoplasmic domain of TGOLN2 binds to the complex and is essential for budding to occur. Coupling of the segregation of secretory proteins to the budding of exocytic vesicles is mediated by it. The cytosolic domain of TGOLN2 interacts with AP2 clathrin adaptor complexes and also with the coiled coil region of a protein called neurabin.
