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Newly synthesized proteins exit the ER and move to the cis-Golgi network (CGN) where they traverse the cis-medial and trans-cisternae before reaching the trans-Golgi network (TGN). N-linked oligosaccharide processing occurs in the TGN, and proteins are sorted to the plasma membrane, lysosomes, endosomes, and secretory granules. TGN38 is a type I integral membrane protein primarily localized to the TGN. It is involved in the sorting of nascent proteins into individual carrier vesicles for transport to appropriate destinations. It is thought to heterodimerize with TGN41 and participate in exocytic budding from the TGN. TGN38 has a molecular weight of 85 to 95kDa. The core polypeptide represents approximately 38kDa, while the remainder is accounted for by N- and O-linked oligosaccharide chains. A 286 aa N-terminal lumenal domain, a 21 aa membrane spanning domain, and a 33 aa C-terminal cytoplasmic tail comprise the structure of TGN38. The cytoplasmic tail contains a tyrosine-based motif, YQRL, that is thought to be involved in TGN localization. Therefore, TGN38 mediates the localization of various proteins to the TGN and serves as a TGN retrieval signal.Immunofluorescence, Western Blotting
