THE 17-RESIDUE TRANSMEMBRANE DOMAIN OF BETA-GALACTOSIDE ALPHA-2,6-SIALYLTRANSFERASE IS SUFFICIENT FOR GOLGI RETENTION

Beta-galactoside alpha-2,6-sialyltransferase (ST) is a type II integral membrane protein of the Golgi apparatus involved in the sialylation of N-linked glycans. A series of experiments has shown that the 17-residue transmembrane domain of ST is sufficient to confer localization to the Golgi apparatus when transferred to the corresponding region of a cell surface type II integral membrane protein. Lectin affinity chromatography of chimeric proteins bearing this 17-residue sequence suggests that these chimeric proteins are localized in the trans-Golgi cisternae and/or trans-Golgi network. Further experiments suggest that this 17-residue sequence functions as a retention signal for the Golgi apparatus.