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Significance The mammalian Golgi contains numerous glycosyltransferases that continuously recycle from late cisternae to earlier cisternae in COPI vesicles to maintain their steady-state localization in this organelle. How the glycosyltransferases are incorporated into these vesicular carriers is poorly understood. Here, we show that the N-cytoplasmic tails (N-tails) of a subset of these type II transmembrane proteins bind directly to two of the seven subunits of COPI coatomer. These glycosyltransferases share a common amino acid motif in their N-tails. The importance of these interactions is illustrated by mucolipidosis III patients with missense mutations within the N-tail motif of GlcNAc-1-phosphotransferase that impair binding to the COPI subunits, resulting in the mislocalization of this transferase to lysosomes.

Recycling of Golgi glycosyltransferases requires direct binding to coatomer